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Database: UniProt
Entry: P00734
LinkDB: P00734
Original site: P00734 
ID   THRB_HUMAN              Reviewed;         622 AA.
AC   P00734; B2R7F7; B4E1A7; Q4QZ40; Q53H04; Q53H06; Q69EZ7; Q7Z7P3; Q9UCA1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   29-SEP-2021, entry version 268.
DE   RecName: Full=Prothrombin;
DE            EC=3.4.21.5;
DE   AltName: Full=Coagulation factor II;
DE   Contains:
DE     RecName: Full=Activation peptide fragment 1;
DE   Contains:
DE     RecName: Full=Activation peptide fragment 2;
DE   Contains:
DE     RecName: Full=Thrombin light chain;
DE   Contains:
DE     RecName: Full=Thrombin heavy chain;
DE   Flags: Precursor;
GN   Name=F2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2825773; DOI=10.1021/bi00393a033;
RA   Degen S.J.F., Davie E.W.;
RT   "Nucleotide sequence of the gene for human prothrombin.";
RL   Biochemistry 26:6165-6177(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT FA2D GLY-72.
RC   TISSUE=Blood;
RX   PubMed=14962227; DOI=10.1046/j.1365-2516.2003.00838.x;
RA   Wang W., Fu Q., Zhou R., Wu W., Ding Q., Hu Y., Wang X., Wang H., Wang Z.;
RT   "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of Gla29
RT   by Gly.";
RL   Haemophilia 10:94-97(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-165.
RC   TISSUE=Liver, and Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-165.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-622, AND GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-49; GLU-50; GLU-57; GLU-59; GLU-62; GLU-63; GLU-68; GLU-69; GLU-72 AND
RP   GLU-75.
RX   PubMed=6305407; DOI=10.1021/bi00278a008;
RA   Degen S.J.F., McGillivray R.T.A., Davie E.W.;
RT   "Characterization of the complementary deoxyribonucleic acid and gene
RT   coding for human prothrombin.";
RL   Biochemistry 22:2087-2097(1983).
RN   [8]
RP   PROTEIN SEQUENCE OF 44-64.
RC   TISSUE=Urine;
RX   PubMed=8073540; DOI=10.1007/bf00431548;
RA   Suzuki K., Moriyama M., Nakajima C., Kawamura K., Miyazawa K., Tsugawa R.,
RA   Kikuchi N., Nagata K.;
RT   "Isolation and partial characterization of crystal matrix protein as a
RT   potent inhibitor of calcium oxalate crystal aggregation: evidence of
RT   activation peptide of human prothrombin.";
RL   Urol. Res. 22:45-50(1994).
RN   [9]
RP   PROTEIN SEQUENCE OF 44-314.
RX   PubMed=266717; DOI=10.1073/pnas.74.5.1969;
RA   Walz D.A., Hewett-Emmett D., Seegers W.H.;
RT   "Amino acid sequence of human prothrombin fragments 1 and 2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 74:1969-1972(1977).
RN   [10]
RP   PROTEIN SEQUENCE OF 315-622, GLYCOSYLATION AT ASN-416, AND VARIANT GLN-532.
RX   PubMed=873923;
RA   Butkowski R.J., Elion J., Downing M.R., Mann K.G.;
RT   "Primary structure of human prethrombin 2 and alpha-thrombin.";
RL   J. Biol. Chem. 252:4942-4957(1977).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 364-622.
RA   Gruber A., Hanson S.R., DiCera E.;
RT   "Antithrombotic thrombin variants.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   ACTIVITY REGULATION, AND HETERODIMER WITH SERPINA5.
RX   PubMed=6323392; DOI=10.1093/oxfordjournals.jbchem.a134583;
RA   Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
RT   "Mechanism of inhibition of activated protein C by protein C inhibitor.";
RL   J. Biochem. 95:187-195(1984).
RN   [13]
RP   PROTEOLYTIC PROCESSING, AND GAMMA-CARBOXYGLUTAMATION AT GLU-49 AND GLU-50.
RX   PubMed=3759958;
RA   Rabiet M.J., Blashill A., Furie B., Furie B.C.;
RT   "Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation
RT   in human plasma.";
RL   J. Biol. Chem. 261:13210-13215(1986).
RN   [14]
RP   FUNCTION, AND CHARACTERIZATION.
RX   PubMed=2856554;
RA   Glenn K.C., Frost G.H., Bergmann J.S., Carney D.H.;
RT   "Synthetic peptides bind to high-affinity thrombin receptors and modulate
RT   thrombin mitogenesis.";
RL   Pept. Res. 1:65-73(1988).
RN   [15]
RP   INVOLVEMENT IN RPRGL2 SUSCEPTIBILITY.
RX   PubMed=11506076; DOI=10.1111/j.8755-8920.2001.460202.x;
RA   Pihusch R., Buchholz T., Lohse P., Rubsamen H., Rogenhofer N.,
RA   Hasbargen U., Hiller E., Thaler C.J.;
RT   "Thrombophilic gene mutations and recurrent spontaneous abortion:
RT   prothrombin mutation increases the risk in the first trimester.";
RL   Am. J. Reprod. Immunol. 46:124-131(2001).
RN   [16]
RP   INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
RX   PubMed=15534175; DOI=10.1001/archneur.61.11.1652;
RA   Casas J.P., Hingorani A.D., Bautista L.E., Sharma P.;
RT   "Meta-analysis of genetic studies in ischemic stroke: thirty-two genes
RT   involving approximately 18,000 cases and 58,000 controls.";
RL   Arch. Neurol. 61:1652-1661(2004).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143.
RC   TISSUE=Plasma;
RX   PubMed=14760718; DOI=10.1002/pmic.200300556;
RA   Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT   "Screening for N-glycosylated proteins by liquid chromatography mass
RT   spectrometry.";
RL   Proteomics 4:454-465(2004).
RN   [18]
RP   CHARACTERIZATION OF THE TP508 PEPTIDE.
RX   PubMed=15885491; DOI=10.1016/j.orthres.2004.12.005;
RA   Li G., Cui Y., McIlmurray L., Allen W.E., Wang H.;
RT   "rhBMP-2, rhVEGF(165), rhPTN and thrombin-related peptide, TP508 induce
RT   chemotaxis of human osteoblasts and microvascular endothelial cells.";
RL   J. Orthop. Res. 23:680-685(2005).
RN   [19]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [20]
RP   THERAPEUTIC USAGE OF THE TP508 PEPTIDE.
RX   PubMed=17244316; DOI=10.1111/j.1524-475x.2006.00181.x;
RA   Fife C., Mader J.T., Stone J., Brill L., Satterfield K., Norfleet A.,
RA   Zwernemann A., Ryaby J.T., Carney D.H.;
RT   "Thrombin peptide Chrysalin stimulates healing of diabetic foot ulcers in a
RT   placebo-controlled phase I/II study.";
RL   Wound Repair Regen. 15:23-34(2007).
RN   [21]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [22]
RP   GLYCOSYLATION AT ASN-416.
RX   PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA   Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA   Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA   Ying W.T., He S.M., Qian X.H.;
RT   "A strategy for precise and large scale identification of core fucosylated
RT   glycoproteins.";
RL   Mol. Cell. Proteomics 8:913-923(2009).
RN   [23]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, AND STRUCTURE OF
RP   CARBOHYDRATE.
RC   TISSUE=Cerebrospinal fluid;
RX   PubMed=19838169; DOI=10.1038/nmeth.1392;
RA   Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G.,
RA   Larson G.;
RT   "Enrichment of glycopeptides for glycan structure and attachment site
RT   identification.";
RL   Nat. Methods 6:809-811(2009).
RN   [24]
RP   GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA   Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT   "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT   O-linked glycosylations by CID and ECD.";
RL   Mol. Cell. Proteomics 11:1-17(2012).
RN   [25]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=2583108; DOI=10.1002/j.1460-2075.1989.tb08511.x;
RA   Bode W., Mayr I., Baumann U., Huber R., Stone S.R., Hofsteenge J.;
RT   "The refined 1.9 A crystal structure of human alpha-thrombin: interaction
RT   with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-
RT   Trp insertion segment.";
RL   EMBO J. 8:3467-3475(1989).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
RX   PubMed=2369893; DOI=10.1002/j.1460-2075.1990.tb07410.x;
RA   Gruetter M.G., Priestle J.P., Rahuel J., Grossenbacher H., Bode W.,
RA   Hofsteenge J., Stone S.R.;
RT   "Crystal structure of the thrombin-hirudin complex: a novel mode of serine
RT   protease inhibition.";
RL   EMBO J. 9:2361-2365(1990).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
RX   PubMed=2374926; DOI=10.1126/science.2374926;
RA   Rydel T.J., Ravichandran K.G., Tulinsky A., Bode W., Huber R., Roitsch C.,
RA   Fenton J.W. II;
RT   "The structure of a complex of recombinant hirudin and human alpha-
RT   thrombin.";
RL   Science 249:277-280(1990).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH HIRUDIN
RP   AND SYNTHETIC INHIBITOR.
RX   PubMed=8251938; DOI=10.1002/pro.5560021009;
RA   Priestle J.P., Rahuel J., Rink H., Tones M., Gruetter M.G.;
RT   "Changes in interactions in complexes of hirudin derivatives and human
RT   alpha-thrombin due to different crystal forms.";
RL   Protein Sci. 2:1630-1642(1993).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=8071320;
RA   Rydel T.J., Yin M., Padmanabhan K.P., Blankenship D.T., Cardin A.D.,
RA   Correa P.E., Fenton J.W. II, Tulinsky A.;
RT   "Crystallographic structure of human gamma-thrombin.";
RL   J. Biol. Chem. 269:22000-22006(1994).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=9214615; DOI=10.1093/emboj/16.11.2977;
RA   van de Locht A., Bode W., Huber R., le Bonniec B.F., Stone S.R.,
RA   Esmon C.T., Stubbs M.T.;
RT   "The thrombin E192Q-BPTI complex reveals gross structural rearrangements:
RT   implications for the interaction with antithrombin and thrombomodulin.";
RL   EMBO J. 16:2977-2984(1997).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 328-601.
RX   PubMed=10051558; DOI=10.1073/pnas.96.5.1852;
RA   Guinto E.R., Caccia S., Rose T., Fuetterer K., Waksman G., di Cera E.;
RT   "Unexpected crucial role of residue 225 in serine proteases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1852-1857(1999).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH SYNTHETIC
RP   INHIBITOR.
RX   PubMed=11493008; DOI=10.1006/jmbi.2001.4872;
RA   Skordalakes E., Dodson G.G., Green D.S., Goodwin C.A., Scully M.F.,
RA   Hudson H.R., Kakkar V.V., Deadman J.J.;
RT   "Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds
RT   via a metastable pentacoordinated phosphorus intermediate.";
RL   J. Mol. Biol. 311:549-555(2001).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH HIRUDIN
RP   AND SYNTHETIC INHIBITOR.
RX   PubMed=16763681; DOI=10.1039/b602585d;
RA   Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P., Obst-Sander U.,
RA   Wagner B., Kansy M., Banner D.W., Diederich F.;
RT   "Multipolar interactions in the D pocket of thrombin: large differences
RT   between tricyclic imide and lactam inhibitors.";
RL   Org. Biomol. Chem. 4:2364-2375(2006).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH HIRUDIN.
RX   PubMed=17685615; DOI=10.1021/ja0735002;
RA   Liu C.C., Brustad E., Liu W., Schultz P.G.;
RT   "Crystal structure of a biosynthetic sulfo-hirudin complexed to thrombin.";
RL   J. Am. Chem. Soc. 129:10648-10649(2007).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH SYNTHETIC
RP   INHIBITOR.
RX   PubMed=18291642; DOI=10.1016/j.bmcl.2008.01.098;
RA   Isaacs R.C.A., Solinsky M.G., Cutrona K.J., Newton C.L., Naylor-Olsen A.M.,
RA   McMasters D.R., Krueger J.A., Lewis S.D., Lucas B.J., Kuo L.C., Yan Y.,
RA   Lynch J.J., Lyle E.A.;
RT   "Structure-based design of novel groups for use in the P1 position of
RT   thrombin inhibitor scaffolds. Part 2: N-acetamidoimidazoles.";
RL   Bioorg. Med. Chem. Lett. 18:2062-2066(2008).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH SERPINA5
RP   AND HEPARIN.
RX   PubMed=18362344; DOI=10.1073/pnas.0711055105;
RA   Li W., Adams T.E., Nangalia J., Esmon C.T., Huntington J.A.;
RT   "Molecular basis of thrombin recognition by protein C inhibitor revealed by
RT   the 1.6-A structure of the heparin-bridged complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
RN   [38]
RP   VARIANT FA2D LYS-200, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=6405779; DOI=10.1111/j.1365-2141.1983.tb02092.x;
RA   Board P.G., Shaw D.C.;
RT   "Determination of the amino acid substitution in human prothrombin type 3
RT   (157 Glu leads to Lys) and the localization of a third thrombin cleavage
RT   site.";
RL   Br. J. Haematol. 54:245-254(1983).
RN   [39]
RP   VARIANT FA2D CYS-314, AND PROTEIN SEQUENCE OF 310-327.
RX   PubMed=3771562;
RA   Rabiet M.-J., Furie B.C., Furie B.;
RT   "Molecular defect of prothrombin Barcelona. Substitution of cysteine for
RT   arginine at residue 273.";
RL   J. Biol. Chem. 261:15045-15048(1986).
RN   [40]
RP   VARIANT FA2D TRP-461, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3567158; DOI=10.1021/bi00378a020;
RA   Miyata T., Morita T., Inomoto T., Kawauchi S., Shirakami A., Iwanaga S.;
RT   "Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that
RT   impairs the fibrinogen clotting activity of derived thrombin Tokushima.";
RL   Biochemistry 26:1117-1122(1987).
RN   [41]
RP   VARIANT FA2D TRP-461.
RX   PubMed=3801671;
RA   Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S., Miyoshi K.,
RA   Morita T., Iwanaga S.;
RT   "Prothrombin Tokushima: characterization of dysfunctional thrombin derived
RT   from a variant of human prothrombin.";
RL   Blood 69:565-569(1987).
RN   [42]
RP   VARIANT FA2D CYS-425, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3242619; DOI=10.1021/bi00426a013;
RA   Henriksen R.A., Mann K.G.;
RT   "Identification of the primary structural defect in the dysthrombin
RT   thrombin Quick I: substitution of cysteine for arginine-382.";
RL   Biochemistry 27:9160-9165(1988).
RN   [43]
RP   VARIANT FA2D VAL-601, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2719946; DOI=10.1021/bi00431a017;
RA   Henriksen R.A., Mann K.G.;
RT   "Substitution of valine for glycine-558 in the congenital dysthrombin
RT   thrombin Quick II alters primary substrate specificity.";
RL   Biochemistry 28:2078-2082(1989).
RN   [44]
RP   VARIANT FA2D ALA-509, AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1354985; DOI=10.1021/bi00148a005;
RA   Miyata T., Aruga R., Umeyama H., Bezeaud A., Guillin M.-C., Iwanaga S.;
RT   "Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces
RT   the fibrinogen clotting activity and the esterase activity.";
RL   Biochemistry 31:7457-7462(1992).
RN   [45]
RP   VARIANTS FA2D THR-380 AND HIS-431.
RX   PubMed=1421398;
RA   Morishita E., Saito M., Kumabashiri I., Asakura H., Matsuda T.,
RA   Yamaguchi K.;
RT   "Prothrombin Himi: a compound heterozygote for two dysfunctional
RT   prothrombin molecules (Met-337-->Thr and Arg-388-->His).";
RL   Blood 80:2275-2280(1992).
RN   [46]
RP   VARIANT FA2D TRP-461.
RX   PubMed=1349838;
RA   Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S., Itakura M.;
RT   "Detection of a single base substitution of the gene for prothrombin
RT   Tokushima. The application of PCR-SSCP for the genetic and molecular
RT   analysis of dysprothrombinemia.";
RL   Int. J. Hematol. 55:93-100(1992).
RN   [47]
RP   VARIANT FA2D HIS-314.
RX   PubMed=7865694; DOI=10.1097/00001721-199410000-00025;
RA   James H.L., Kim D.J., Zheng D.-Q., Girolami A.;
RT   "Prothrombin Padua I: incomplete activation due to an amino acid
RT   substitution at a factor Xa cleavage site.";
RL   Blood Coagul. Fibrinolysis 5:841-844(1994).
RN   [48]
RP   VARIANT FA2D ALA-509.
RX   PubMed=7792730;
RA   Degen S.J.F., McDowell S.A., Sparks L.M., Scharrer I.;
RT   "Prothrombin Frankfurt: a dysfunctional prothrombin characterized by
RT   substitution of Glu-466 by Ala.";
RL   Thromb. Haemost. 73:203-209(1995).
RN   [49]
RP   VARIANTS MET-165 AND THR-386.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [50]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
RN   [51]
RP   VARIANTS MET-165; LYS-200; THR-386 AND GLN-532, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA   Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA   Zeng R., Wu J.R.;
RT   "Quantitative detection of single amino acid polymorphisms by targeted
RT   proteomics.";
RL   J. Mol. Cell Biol. 3:309-315(2011).
CC   -!- FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts
CC       fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in
CC       complex with thrombomodulin, protein C. Functions in blood homeostasis,
CC       inflammation and wound healing. {ECO:0000269|PubMed:2856554}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form
CC         fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
CC   -!- ACTIVITY REGULATION: Inhibited by SERPINA5.
CC       {ECO:0000269|PubMed:6323392}.
CC   -!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
CC       chain; disulfide-linked. Forms a heterodimer with SERPINA5.
CC       {ECO:0000269|PubMed:11493008, ECO:0000269|PubMed:16763681,
CC       ECO:0000269|PubMed:17685615, ECO:0000269|PubMed:18291642,
CC       ECO:0000269|PubMed:18362344, ECO:0000269|PubMed:2369893,
CC       ECO:0000269|PubMed:2374926}.
CC   -!- INTERACTION:
CC       P00734; P05067: APP; NbExp=3; IntAct=EBI-297094, EBI-77613;
CC       P00734; P07204: THBD; NbExp=4; IntAct=EBI-297094, EBI-941422;
CC       P00734; Q846V4; Xeno; NbExp=5; IntAct=EBI-297094, EBI-989571;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC   -!- PTM: The gamma-carboxyglutamyl residues, which bind calcium ions,
CC       result from the carboxylation of glutamyl residues by a microsomal
CC       enzyme, the vitamin K-dependent carboxylase. The modified residues are
CC       necessary for the calcium-dependent interaction with a negatively
CC       charged phospholipid surface, which is essential for the conversion of
CC       prothrombin to thrombin. {ECO:0000269|PubMed:3759958,
CC       ECO:0000269|PubMed:6305407}.
CC   -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3
CC       (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143:
CC       Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).
CC       {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952,
CC       ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
CC       ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320,
CC       ECO:0000269|PubMed:873923}.
CC   -!- DISEASE: Factor II deficiency (FA2D) [MIM:613679]: A very rare blood
CC       coagulation disorder characterized by mucocutaneous bleeding symptoms.
CC       The severity of the bleeding manifestations correlates with blood
CC       factor II levels. {ECO:0000269|PubMed:1349838,
CC       ECO:0000269|PubMed:1354985, ECO:0000269|PubMed:1421398,
CC       ECO:0000269|PubMed:14962227, ECO:0000269|PubMed:2719946,
CC       ECO:0000269|PubMed:3242619, ECO:0000269|PubMed:3567158,
CC       ECO:0000269|PubMed:3771562, ECO:0000269|PubMed:3801671,
CC       ECO:0000269|PubMed:6405779, ECO:0000269|PubMed:7792730,
CC       ECO:0000269|PubMed:7865694}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute
CC       neurologic event leading to death of neural tissue of the brain and
CC       resulting in loss of motor, sensory and/or cognitive function. Ischemic
CC       strokes, resulting from vascular occlusion, is considered to be a
CC       highly complex disease consisting of a group of heterogeneous disorders
CC       with multiple genetic and environmental risk factors.
CC       {ECO:0000269|PubMed:15534175}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Thrombophilia due to thrombin defect (THPH1) [MIM:188050]: A
CC       multifactorial disorder of hemostasis characterized by abnormal
CC       platelet aggregation in response to various agents and recurrent
CC       thrombi formation. {ECO:0000269|PubMed:2825773}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry. A
CC       common genetic variation in the 3-prime untranslated region of the
CC       prothrombin gene is associated with elevated plasma prothrombin levels
CC       and an increased risk of venous thrombosis.
CC   -!- DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A common
CC       complication of pregnancy, resulting in spontaneous abortion before the
CC       fetus has reached viability. The term includes all miscarriages from
CC       the time of conception until 24 weeks of gestation. Recurrent pregnancy
CC       loss is defined as 3 or more consecutive spontaneous abortions.
CC       {ECO:0000269|PubMed:11506076}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- PHARMACEUTICAL: The peptide TP508 also known as Chrysalin (Orthologic)
CC       could be used to accelerate repair of both soft and hard tissues.
CC   -!- MISCELLANEOUS: Prothrombin is activated on the surface of a
CC       phospholipid membrane that binds the amino end of prothrombin and
CC       factors Va and Xa in Ca-dependent interactions; factor Xa removes the
CC       activation peptide and cleaves the remaining part into light and heavy
CC       chains. The activation process starts slowly because factor V itself
CC       has to be activated by the initial, small amounts of thrombin.
CC   -!- MISCELLANEOUS: It is not known whether 1 or 2 smaller activation
CC       peptides, with additional cleavage after Arg-314, are released in
CC       natural blood clotting.
CC   -!- MISCELLANEOUS: Thrombin can itself cleave the N-terminal fragment
CC       (fragment 1) of the prothrombin, prior to its activation by factor Xa.
CC   -!- MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does not
CC       occur in plasma.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry;
CC       URL="https://en.wikipedia.org/wiki/Thrombin";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/f2/";
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DR   EMBL; M17262; AAC63054.1; -; Genomic_DNA.
DR   EMBL; AJ972449; CAJ01369.1; -; mRNA.
DR   EMBL; AK303747; BAG64719.1; -; mRNA.
DR   EMBL; AK312965; BAG35804.1; -; mRNA.
DR   EMBL; AK222775; BAD96495.1; -; mRNA.
DR   EMBL; AK222777; BAD96497.1; -; mRNA.
DR   EMBL; AF478696; AAL77436.1; -; Genomic_DNA.
DR   EMBL; BC051332; AAH51332.1; -; mRNA.
DR   EMBL; V00595; CAA23842.1; -; mRNA.
DR   EMBL; AY344794; AAR08143.1; -; mRNA.
DR   CCDS; CCDS31476.1; -.
DR   PIR; A29351; TBHU.
DR   RefSeq; NP_000497.1; NM_000506.4.
DR   RefSeq; NP_001298186.1; NM_001311257.1.
DR   PDB; 1A2C; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 1A3B; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 1A3E; X-ray; 1.85 A; H=364-622, L=328-363.
DR   PDB; 1A46; X-ray; 2.12 A; H=364-622, L=328-363.
DR   PDB; 1A4W; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 1A5G; X-ray; 2.06 A; H=364-622, L=328-363.
DR   PDB; 1A61; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 1ABI; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1ABJ; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 1AD8; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1AE8; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1AFE; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1AHT; X-ray; 1.60 A; H=364-622, L=328-363.
DR   PDB; 1AI8; X-ray; 1.85 A; H=364-622, L=328-363.
DR   PDB; 1AIX; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 1AWF; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 1AWH; X-ray; 3.00 A; A/C=328-363, B/D=364-622.
DR   PDB; 1AY6; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 1B5G; X-ray; 2.07 A; H=364-622, L=328-363.
DR   PDB; 1B7X; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 1BA8; X-ray; 1.80 A; A=328-363, B=364-622.
DR   PDB; 1BB0; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 1BCU; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1BHX; X-ray; 2.30 A; A=331-349, B=364-510, F=518-622.
DR   PDB; 1BMM; X-ray; 2.60 A; H=364-622, L=328-363.
DR   PDB; 1BMN; X-ray; 2.80 A; H=364-622, L=328-363.
DR   PDB; 1BTH; X-ray; 2.30 A; H/K=364-622, J/L=328-363.
DR   PDB; 1C1U; X-ray; 1.75 A; H=364-616, L=328-363.
DR   PDB; 1C1V; X-ray; 1.98 A; H=364-616, L=328-363.
DR   PDB; 1C1W; X-ray; 1.90 A; H=364-616, L=328-363.
DR   PDB; 1C4U; X-ray; 2.10 A; 1=328-363, 2=364-622.
DR   PDB; 1C4V; X-ray; 2.10 A; 1=328-363, 2=364-622.
DR   PDB; 1C4Y; X-ray; 2.70 A; 1=328-363, 2=364-622.
DR   PDB; 1C5L; X-ray; 1.47 A; H=364-622, L=328-363.
DR   PDB; 1C5N; X-ray; 1.50 A; H=364-622, L=328-363.
DR   PDB; 1C5O; X-ray; 1.90 A; H=364-622, L=328-363.
DR   PDB; 1CA8; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 1D3D; X-ray; 2.04 A; A=333-360, B=364-620.
DR   PDB; 1D3P; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 1D3Q; X-ray; 2.90 A; A=328-363, B=364-622.
DR   PDB; 1D3T; X-ray; 3.00 A; A=328-363, B=364-622.
DR   PDB; 1D4P; X-ray; 2.07 A; A=328-363, B=364-622.
DR   PDB; 1D6W; X-ray; 2.00 A; A=334-620.
DR   PDB; 1D9I; X-ray; 2.30 A; A=334-621.
DR   PDB; 1DE7; X-ray; 2.00 A; H/K=364-619, J/L=328-360.
DR   PDB; 1DIT; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1DM4; X-ray; 2.50 A; A=328-362, B=363-622.
DR   PDB; 1DOJ; X-ray; 1.70 A; A=328-622.
DR   PDB; 1DWB; X-ray; 3.16 A; H=364-622, L=328-363.
DR   PDB; 1DWC; X-ray; 3.00 A; H=364-622, L=328-363.
DR   PDB; 1DWD; X-ray; 3.00 A; H=364-622, L=328-363.
DR   PDB; 1DWE; X-ray; 3.00 A; H=364-622, L=328-363.
DR   PDB; 1DX5; X-ray; 2.30 A; A/B/C/D=328-363, M/N/O/P=364-622.
DR   PDB; 1E0F; X-ray; 3.10 A; A/B/C=328-363, D/E/F=364-622.
DR   PDB; 1EB1; X-ray; 1.80 A; H=364-620, L=334-360.
DR   PDB; 1EOJ; X-ray; 2.10 A; A=332-620.
DR   PDB; 1EOL; X-ray; 2.10 A; A=332-620.
DR   PDB; 1FPC; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1FPH; X-ray; 2.50 A; H=364-622, L=328-363.
DR   PDB; 1G30; X-ray; 2.00 A; A=328-363, B=364-622.
DR   PDB; 1G32; X-ray; 1.90 A; A=328-363, B=364-622.
DR   PDB; 1G37; X-ray; 2.00 A; A=334-620.
DR   PDB; 1GHV; X-ray; 1.85 A; H=364-620, L=328-363.
DR   PDB; 1GHW; X-ray; 1.75 A; H=364-620, L=328-363.
DR   PDB; 1GHX; X-ray; 1.65 A; H=364-620, L=328-363.
DR   PDB; 1GHY; X-ray; 1.85 A; H=364-620, L=328-363.
DR   PDB; 1GJ4; X-ray; 1.81 A; H=364-621, L=328-363.
DR   PDB; 1GJ5; X-ray; 1.73 A; H=364-621, L=328-363.
DR   PDB; 1H8D; X-ray; 1.40 A; H=364-621, L=333-360.
DR   PDB; 1H8I; X-ray; 1.75 A; H=364-622, L=334-360.
DR   PDB; 1HAG; X-ray; 2.00 A; E=328-622.
DR   PDB; 1HAH; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1HAI; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 1HAO; X-ray; 2.80 A; H=364-622, L=328-363.
DR   PDB; 1HAP; X-ray; 2.80 A; H=364-622, L=328-360.
DR   PDB; 1HBT; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1HDT; X-ray; 2.60 A; H=364-622, L=331-363.
DR   PDB; 1HGT; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 1HLT; X-ray; 3.00 A; H/K=364-622, J/L=334-349.
DR   PDB; 1HUT; X-ray; 2.90 A; H=364-622, L=328-363.
DR   PDB; 1HXE; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 1HXF; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 1IHS; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1IHT; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 1JMO; X-ray; 2.20 A; H=363-622, L=315-362.
DR   PDB; 1JOU; X-ray; 1.80 A; A/C/E=315-363, B/D/F=364-622.
DR   PDB; 1JWT; X-ray; 2.50 A; A=328-622.
DR   PDB; 1K21; X-ray; 1.86 A; H=364-622, L=328-363.
DR   PDB; 1K22; X-ray; 1.93 A; H=364-622, L=328-363.
DR   PDB; 1KTS; X-ray; 2.40 A; A=328-363, B=364-622.
DR   PDB; 1KTT; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 1LHC; X-ray; 1.95 A; H=364-622, L=328-363.
DR   PDB; 1LHD; X-ray; 2.35 A; H=364-622, L=328-363.
DR   PDB; 1LHE; X-ray; 2.25 A; H=364-622, L=328-363.
DR   PDB; 1LHF; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 1LHG; X-ray; 2.25 A; H=364-622, L=328-363.
DR   PDB; 1MH0; X-ray; 2.80 A; A/B=334-620.
DR   PDB; 1MU6; X-ray; 1.99 A; A=328-363, B=364-622.
DR   PDB; 1MU8; X-ray; 2.00 A; A=328-363, B=364-622.
DR   PDB; 1MUE; X-ray; 2.00 A; A=328-363, B=364-622.
DR   PDB; 1NM6; X-ray; 1.80 A; A=335-621.
DR   PDB; 1NO9; X-ray; 1.90 A; H=364-622, L=328-363.
DR   PDB; 1NRN; X-ray; 3.10 A; H=364-622, L=328-363.
DR   PDB; 1NRO; X-ray; 3.10 A; H=364-622, L=328-363.
DR   PDB; 1NRP; X-ray; 3.00 A; H=364-622, L=328-363.
DR   PDB; 1NRQ; X-ray; 3.50 A; H=364-622, L=328-363.
DR   PDB; 1NRR; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 1NRS; X-ray; 2.40 A; H=364-622, L=328-349.
DR   PDB; 1NT1; X-ray; 2.00 A; A=335-621.
DR   PDB; 1NU7; X-ray; 2.20 A; A/E=332-359, B/F=364-622.
DR   PDB; 1NU9; X-ray; 2.20 A; A/D=332-622.
DR   PDB; 1NY2; X-ray; 2.30 A; 1=328-363, 2=364-622.
DR   PDB; 1NZQ; X-ray; 2.18 A; H=364-620, L=328-361.
DR   PDB; 1O0D; X-ray; 2.44 A; H=364-622, L=328-363.
DR   PDB; 1O2G; X-ray; 1.58 A; H=364-622, L=328-363.
DR   PDB; 1O5G; X-ray; 1.75 A; H=364-622, L=328-363.
DR   PDB; 1OOK; X-ray; 2.30 A; A=328-363, B=364-622.
DR   PDB; 1OYT; X-ray; 1.67 A; H=364-622, L=328-363.
DR   PDB; 1P8V; X-ray; 2.60 A; B=333-361, C=364-621.
DR   PDB; 1PPB; X-ray; 1.92 A; H=364-622, L=328-363.
DR   PDB; 1QBV; X-ray; 1.80 A; H=364-622, L=328-359.
DR   PDB; 1QHR; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 1QJ1; X-ray; 2.00 A; A=328-363, B=364-622.
DR   PDB; 1QJ6; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 1QJ7; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 1QUR; X-ray; 2.00 A; H=364-620, L=334-360.
DR   PDB; 1RD3; X-ray; 2.50 A; A/C=328-363, B/D=364-622.
DR   PDB; 1RIW; X-ray; 2.04 A; A=328-363, B=364-510, C=518-622.
DR   PDB; 1SB1; X-ray; 1.90 A; H=364-621, L=333-361.
DR   PDB; 1SFQ; X-ray; 1.91 A; A/D=328-363, B/E=364-622.
DR   PDB; 1SG8; X-ray; 2.30 A; A/D=328-363, B/E=364-622.
DR   PDB; 1SGI; X-ray; 2.30 A; A/D=328-363, B/E=364-622.
DR   PDB; 1SHH; X-ray; 1.55 A; A/D=328-363, B/E=364-622.
DR   PDB; 1SL3; X-ray; 1.81 A; A=335-621.
DR   PDB; 1SR5; X-ray; 3.10 A; B=328-363, C=364-622.
DR   PDB; 1T4U; X-ray; 2.00 A; H=364-622, L=334-359.
DR   PDB; 1T4V; X-ray; 2.00 A; H=364-622, L=334-359.
DR   PDB; 1TA2; X-ray; 2.30 A; A=335-621.
DR   PDB; 1TA6; X-ray; 1.90 A; A=335-621.
DR   PDB; 1TB6; X-ray; 2.50 A; H=364-622, L=315-363.
DR   PDB; 1TBZ; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1THP; X-ray; 2.10 A; A=328-362, B=364-620.
DR   PDB; 1THR; X-ray; 2.30 A; H=364-622, L=328-349.
DR   PDB; 1THS; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 1TMB; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 1TMT; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 1TMU; X-ray; 2.50 A; H=364-620, L=333-349.
DR   PDB; 1TOM; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 1TQ0; X-ray; 2.80 A; A/C=333-363, B/D=364-620.
DR   PDB; 1TQ7; X-ray; 2.40 A; A=320-363, B=364-620.
DR   PDB; 1TWX; X-ray; 2.40 A; A=334-349, B=364-622.
DR   PDB; 1UMA; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 1UVS; X-ray; 2.80 A; H=364-622, L=328-363.
DR   PDB; 1VR1; X-ray; 1.90 A; H=364-620, L=334-360.
DR   PDB; 1VZQ; X-ray; 1.54 A; H=364-620, L=334-360.
DR   PDB; 1W7G; X-ray; 1.65 A; H=364-622, L=328-363.
DR   PDB; 1WAY; X-ray; 2.02 A; A=328-363, B=364-622.
DR   PDB; 1WBG; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 1XM1; X-ray; 2.30 A; A=328-622.
DR   PDB; 1XMN; X-ray; 1.85 A; A/C/E/G=328-363, B/D/F/H=364-622.
DR   PDB; 1YPE; X-ray; 1.81 A; H=364-620, L=334-360.
DR   PDB; 1YPG; X-ray; 1.80 A; H=364-620, L=334-360.
DR   PDB; 1YPJ; X-ray; 1.78 A; H=364-620, L=334-360.
DR   PDB; 1YPK; X-ray; 1.78 A; H=364-620, L=334-360.
DR   PDB; 1YPL; X-ray; 1.85 A; H=364-620, L=334-360.
DR   PDB; 1YPM; X-ray; 1.85 A; H=364-620, L=334-360.
DR   PDB; 1Z71; X-ray; 1.80 A; A=335-621.
DR   PDB; 1Z8I; X-ray; 2.00 A; A=324-361, B=364-622.
DR   PDB; 1Z8J; X-ray; 2.00 A; A=322-361, B=364-622.
DR   PDB; 1ZGI; X-ray; 2.20 A; A=335-621.
DR   PDB; 1ZGV; X-ray; 2.20 A; A=335-621.
DR   PDB; 1ZRB; X-ray; 1.90 A; A=335-621.
DR   PDB; 2A0Q; X-ray; 1.90 A; A/C=334-349, B/D=364-620.
DR   PDB; 2A2X; X-ray; 2.44 A; H=364-622, L=330-363.
DR   PDB; 2A45; X-ray; 3.65 A; A/D=328-363, B/E=364-622.
DR   PDB; 2AFQ; X-ray; 1.93 A; A/C=332-360, B/D=364-622.
DR   PDB; 2ANK; X-ray; 2.46 A; H=364-622, L=330-363.
DR   PDB; 2ANM; X-ray; 2.40 A; H=364-620, L=328-363.
DR   PDB; 2B5T; X-ray; 2.10 A; A/C=315-363, B/D=364-622.
DR   PDB; 2BDY; X-ray; 1.61 A; A=334-622.
DR   PDB; 2BVR; X-ray; 1.25 A; H=364-622, L=328-363.
DR   PDB; 2BVS; X-ray; 1.40 A; H=364-622, L=328-363.
DR   PDB; 2BVX; X-ray; 3.20 A; H=364-622, L=328-363.
DR   PDB; 2BXT; X-ray; 1.83 A; H=364-622, L=328-363.
DR   PDB; 2BXU; X-ray; 2.80 A; H=364-622, L=328-363.
DR   PDB; 2C8W; X-ray; 1.96 A; A=328-363, B=364-622.
DR   PDB; 2C8X; X-ray; 2.17 A; A=328-363, B=364-622.
DR   PDB; 2C8Y; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 2C8Z; X-ray; 2.14 A; A=328-363, B=364-622.
DR   PDB; 2C90; X-ray; 2.25 A; A=328-363, B=364-622.
DR   PDB; 2C93; X-ray; 2.20 A; A=328-363, B=364-622.
DR   PDB; 2CF8; X-ray; 1.30 A; H=364-620, L=334-361.
DR   PDB; 2CF9; X-ray; 1.79 A; H=364-620, L=334-361.
DR   PDB; 2CN0; X-ray; 1.30 A; H=364-620, L=334-361.
DR   PDB; 2FEQ; X-ray; 2.44 A; H=364-622, L=328-363.
DR   PDB; 2FES; X-ray; 2.42 A; H=364-622, L=328-363.
DR   PDB; 2GDE; X-ray; 2.00 A; H=364-622, L=328-363.
DR   PDB; 2GP9; X-ray; 1.87 A; A=328-362, B=364-620.
DR   PDB; 2H9T; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 2HGT; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 2HNT; X-ray; 2.50 A; C=364-433, E=437-517, F=518-622, L=328-363.
DR   PDB; 2HPP; X-ray; 3.30 A; H=364-622, L=328-363.
DR   PDB; 2HPQ; X-ray; 3.30 A; H=364-622, L=328-363, P=213-291.
DR   PDB; 2HWL; X-ray; 2.40 A; A/C=328-363, B/D=364-622.
DR   PDB; 2JH0; X-ray; 1.70 A; C=328-361, D=364-622.
DR   PDB; 2JH5; X-ray; 2.50 A; C=328-363, D=364-622.
DR   PDB; 2JH6; X-ray; 2.21 A; C=328-361, D=364-622.
DR   PDB; 2OD3; X-ray; 1.75 A; A=328-363, B=364-622.
DR   PDB; 2PGB; X-ray; 1.54 A; A=328-363, B=364-622.
DR   PDB; 2PGQ; X-ray; 1.80 A; A=319-363, B=364-622.
DR   PDB; 2PKS; X-ray; 2.50 A; A=334-360, B=364-510, C=518-619.
DR   PDB; 2PW8; X-ray; 1.84 A; H=364-621, L=334-360.
DR   PDB; 2R2M; X-ray; 2.10 A; A=334-359, B=364-622.
DR   PDB; 2THF; X-ray; 2.10 A; A=328-363, B=364-622.
DR   PDB; 2UUF; X-ray; 1.26 A; A=328-363, B=364-622.
DR   PDB; 2UUJ; X-ray; 1.32 A; A=328-363, B=364-622.
DR   PDB; 2UUK; X-ray; 1.39 A; A=328-363, B=364-622.
DR   PDB; 2V3H; X-ray; 1.79 A; H=364-620, L=334-361.
DR   PDB; 2V3O; X-ray; 1.79 A; H=364-620, L=334-361.
DR   PDB; 2ZC9; X-ray; 1.58 A; H=364-622, L=328-363.
DR   PDB; 2ZDA; X-ray; 1.73 A; H=364-622, L=328-363.
DR   PDB; 2ZDV; X-ray; 1.72 A; H=364-622, L=328-363.
DR   PDB; 2ZF0; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 2ZFF; X-ray; 1.47 A; H=364-622, L=328-363.
DR   PDB; 2ZFP; X-ray; 2.25 A; H=364-622, L=328-363.
DR   PDB; 2ZFQ; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 2ZFR; X-ray; 1.85 A; H=364-622, L=328-363.
DR   PDB; 2ZG0; X-ray; 1.75 A; H=364-622, L=328-363.
DR   PDB; 2ZGB; X-ray; 1.60 A; H=364-622, L=328-363.
DR   PDB; 2ZGX; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 2ZHE; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 2ZHF; X-ray; 1.98 A; H=364-622, L=328-363.
DR   PDB; 2ZHQ; X-ray; 1.96 A; H=364-622, L=328-363.
DR   PDB; 2ZHW; X-ray; 2.02 A; H=364-622, L=328-363.
DR   PDB; 2ZI2; X-ray; 1.65 A; H=364-622, L=328-363.
DR   PDB; 2ZIQ; X-ray; 1.65 A; H=364-622, L=328-363.
DR   PDB; 2ZNK; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 2ZO3; X-ray; 1.70 A; H=364-622, L=328-363.
DR   PDB; 3B23; X-ray; 2.40 A; A=328-363, B=364-622.
DR   PDB; 3B9F; X-ray; 1.60 A; H=364-622, L=315-363.
DR   PDB; 3BEF; X-ray; 2.20 A; A/D=320-363, B/E=364-622.
DR   PDB; 3BEI; X-ray; 1.55 A; A=320-363, B=364-622.
DR   PDB; 3BF6; X-ray; 2.50 A; H=364-622, L=328-363.
DR   PDB; 3BIU; X-ray; 2.30 A; H=364-620, L=333-361.
DR   PDB; 3BIV; X-ray; 1.80 A; H=364-620, L=333-361.
DR   PDB; 3BV9; X-ray; 1.80 A; A=333-363, B=364-622.
DR   PDB; 3C1K; X-ray; 1.84 A; A=335-621.
DR   PDB; 3C27; X-ray; 2.18 A; A=334-359, B=364-622.
DR   PDB; 3D49; X-ray; 1.50 A; H=364-622, L=328-363.
DR   PDB; 3DA9; X-ray; 1.80 A; A=328-363, B=364-622.
DR   PDB; 3DD2; X-ray; 1.90 A; H=364-621, L=332-361.
DR   PDB; 3DHK; X-ray; 1.73 A; H=364-622, L=328-363.
DR   PDB; 3DT0; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 3DUX; X-ray; 1.60 A; H=364-622, L=328-363.
DR   PDB; 3E6P; X-ray; 2.10 A; H=364-622, L=206-363.
DR   PDB; 3EE0; X-ray; 2.75 A; A=328-363, B=364-622.
DR   PDB; 3EGK; X-ray; 2.20 A; H=364-622, L=328-363.
DR   PDB; 3EQ0; X-ray; 1.53 A; H=364-622, L=328-363.
DR   PDB; 3F68; X-ray; 1.75 A; H=364-622, L=328-363.
DR   PDB; 3GIC; X-ray; 1.55 A; A=328-363, B=364-622.
DR   PDB; 3GIS; X-ray; 2.40 A; A/C/E=315-363, B/D/F=364-622.
DR   PDB; 3HAT; X-ray; 2.50 A; H=364-622, L=328-363.
DR   PDB; 3HKJ; X-ray; 2.60 A; A/D=333-363, B/E=364-622.
DR   PDB; 3HTC; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 3JZ1; X-ray; 1.60 A; A=328-363, B=364-622.
DR   PDB; 3JZ2; X-ray; 2.40 A; A=328-363, B=364-622.
DR   PDB; 3K65; X-ray; 1.85 A; A=199-314, B=315-622.
DR   PDB; 3LDX; X-ray; 2.25 A; H=364-622, L=328-363.
DR   PDB; 3LU9; X-ray; 1.80 A; A/D=318-363, B/E=364-622.
DR   PDB; 3NXP; X-ray; 2.20 A; A=199-622.
DR   PDB; 3P17; X-ray; 1.43 A; H=364-622, L=328-363.
DR   PDB; 3P6Z; X-ray; 1.70 A; A/G=328-363, B/H=364-622.
DR   PDB; 3P70; X-ray; 2.55 A; A/C/E/G=328-363, B/D/F/H=364-622.
DR   PDB; 3PMH; X-ray; 3.20 A; A=328-363, B=364-622.
DR   PDB; 3PO1; X-ray; 1.65 A; A=334-360, B=364-510, C=518-619.
DR   PDB; 3QDZ; X-ray; 2.80 A; A/C=333-363, B/D=364-622.
DR   PDB; 3QGN; X-ray; 2.10 A; A=333-363, B=364-622.
DR   PDB; 3QLP; X-ray; 2.14 A; H=364-622, L=328-363.
DR   PDB; 3QTO; X-ray; 1.52 A; H=364-622, L=328-363.
DR   PDB; 3QTV; X-ray; 1.63 A; H=364-622, L=328-363.
DR   PDB; 3QWC; X-ray; 1.75 A; H=364-622, L=328-363.
DR   PDB; 3QX5; X-ray; 1.35 A; H=364-622, L=328-363.
DR   PDB; 3R3G; X-ray; 1.75 A; A=333-363, B=364-622.
DR   PDB; 3RLW; X-ray; 1.69 A; H=364-622, L=328-363.
DR   PDB; 3RLY; X-ray; 1.51 A; H=364-622, L=328-363.
DR   PDB; 3RM0; X-ray; 1.34 A; H=364-622, L=328-363.
DR   PDB; 3RM2; X-ray; 1.23 A; H=364-622, L=328-363.
DR   PDB; 3RML; X-ray; 1.53 A; H=364-622, L=328-363.
DR   PDB; 3RMM; X-ray; 1.58 A; H=364-622, L=328-363.
DR   PDB; 3RMN; X-ray; 1.78 A; H=364-622, L=328-363.
DR   PDB; 3RMO; X-ray; 1.40 A; H=364-622, L=328-363.
DR   PDB; 3S7H; X-ray; 1.90 A; A=329-363, B=364-622.
DR   PDB; 3S7K; X-ray; 1.90 A; A/C=329-363, B/D=364-622.
DR   PDB; 3SHA; X-ray; 1.52 A; H=364-622, L=328-363.
DR   PDB; 3SHC; X-ray; 1.90 A; H=364-622, L=328-363.
DR   PDB; 3SI3; X-ray; 1.55 A; H=364-622, L=328-363.
DR   PDB; 3SI4; X-ray; 1.27 A; H=364-622, L=328-363.
DR   PDB; 3SQE; X-ray; 1.90 A; E=333-622.
DR   PDB; 3SQH; X-ray; 2.20 A; E=333-622.
DR   PDB; 3SV2; X-ray; 1.30 A; H=364-622, L=328-363.
DR   PDB; 3T5F; X-ray; 1.45 A; H=364-622, L=328-363.
DR   PDB; 3TU7; X-ray; 2.49 A; H=364-622, L=328-363.
DR   PDB; 3U69; X-ray; 1.55 A; H=364-622, L=334-363.
DR   PDB; 3U8O; X-ray; 1.28 A; H=364-622, L=334-363.
DR   PDB; 3U8R; X-ray; 1.47 A; H=364-622, L=334-363.
DR   PDB; 3U8T; X-ray; 1.86 A; H=364-620, L=334-360.
DR   PDB; 3U98; X-ray; 1.45 A; H=364-622, L=328-363.
DR   PDB; 3U9A; X-ray; 1.58 A; H=364-622, L=328-363.
DR   PDB; 3UTU; X-ray; 1.55 A; H=364-622, L=328-363.
DR   PDB; 3UWJ; X-ray; 1.50 A; H=364-622, L=328-363.
DR   PDB; 3VXE; X-ray; 1.25 A; H=364-622, L=328-363.
DR   PDB; 3VXF; Other; 1.60 A; H=364-622, L=328-363.
DR   PDB; 4AX9; X-ray; 1.90 A; H=364-620, L=334-361.
DR   PDB; 4AYV; X-ray; 2.80 A; A=332-361, B=364-620.
DR   PDB; 4AYY; X-ray; 2.60 A; A=332-361, B=364-620.
DR   PDB; 4AZ2; X-ray; 2.60 A; A=332-361, B=364-620.
DR   PDB; 4BAH; X-ray; 1.94 A; A=328-363, B=364-622.
DR   PDB; 4BAK; X-ray; 1.94 A; A=328-363, B=364-622.
DR   PDB; 4BAM; X-ray; 1.88 A; A=328-363, B=364-622.
DR   PDB; 4BAN; X-ray; 1.87 A; A=328-363, B=364-622.
DR   PDB; 4BAO; X-ray; 1.87 A; A=328-363, B=364-622.
DR   PDB; 4BAQ; X-ray; 1.89 A; A=328-363, B=364-622.
DR   PDB; 4BOH; X-ray; 2.60 A; A/H=364-622, B/L=328-363.
DR   PDB; 4CH2; X-ray; 1.60 A; A/C=328-363, B/D=364-622.
DR   PDB; 4CH8; X-ray; 1.75 A; A/C/E/G=328-363, B/D/F/H=364-622.
DR   PDB; 4DIH; X-ray; 1.80 A; H=364-622, L=328-363.
DR   PDB; 4DII; X-ray; 2.05 A; H=364-622, L=328-363.
DR   PDB; 4DT7; X-ray; 1.90 A; A/C=332-363, B/D=364-622.
DR   PDB; 4DY7; X-ray; 2.80 A; A/D=315-363, B/E=364-622.
DR   PDB; 4E05; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 4E06; X-ray; 3.20 A; H=364-622, L=328-363.
DR   PDB; 4E7R; X-ray; 2.25 A; G/H=364-622, L/M=328-363.
DR   PDB; 4H6S; X-ray; 2.19 A; A=333-363, B=364-622.
DR   PDB; 4H6T; X-ray; 2.40 A; A=317-622.
DR   PDB; 4HFP; X-ray; 2.40 A; A/C=333-363, B/D=364-622.
DR   PDB; 4HTC; X-ray; 2.30 A; H=364-622, L=328-363.
DR   PDB; 4HZH; X-ray; 3.30 A; A/B=90-622.
DR   PDB; 4I7Y; X-ray; 2.40 A; H=364-622, L=328-363.
DR   PDB; 4LOY; X-ray; 1.77 A; H=364-620, L=334-360.
DR   PDB; 4LXB; X-ray; 1.61 A; H=364-622, L=328-363.
DR   PDB; 4LZ1; X-ray; 1.65 A; H=364-622, L=328-363.
DR   PDB; 4LZ4; X-ray; 2.56 A; A/C=328-363, B/D=364-622.
DR   PDB; 4MLF; X-ray; 2.20 A; A=331-363, B=364-622.
DR   PDB; 4NZQ; X-ray; 2.81 A; A=44-622.
DR   PDB; 4O03; X-ray; 3.38 A; A=44-622.
DR   PDB; 4RKJ; X-ray; 1.70 A; A=330-363, B=364-622.
DR   PDB; 4RKO; X-ray; 1.84 A; A=322-363, B=364-622.
DR   PDB; 4RN6; X-ray; 3.00 A; A/B=333-622.
DR   PDB; 4THN; X-ray; 2.50 A; H=364-622, L=328-363.
DR   PDB; 4UD9; X-ray; 1.12 A; H=364-622, L=333-360.
DR   PDB; 4UDW; X-ray; 1.16 A; H=364-621, L=333-360.
DR   PDB; 4UE7; X-ray; 1.13 A; H=364-621, L=333-360.
DR   PDB; 4UEH; X-ray; 1.16 A; H=364-621, L=333-361.
DR   PDB; 4UFD; X-ray; 1.43 A; H=364-621, L=333-360.
DR   PDB; 4UFE; X-ray; 1.59 A; H=364-621, L=333-361.
DR   PDB; 4UFF; X-ray; 1.55 A; H=364-621, L=333-361.
DR   PDB; 4UFG; X-ray; 1.65 A; H=364-621, L=333-361.
DR   PDB; 4YES; X-ray; 1.50 A; A=328-363, B=364-622.
DR   PDB; 5A2M; X-ray; 1.40 A; H=364-621, L=333-361.
DR   PDB; 5AF9; X-ray; 1.18 A; H=364-621, L=333-361.
DR   PDB; 5AFY; X-ray; 1.12 A; H=364-621, L=333-361.
DR   PDB; 5AFZ; X-ray; 1.53 A; H=364-621, L=333-361.
DR   PDB; 5AHG; X-ray; 1.24 A; H=364-621, L=333-361.
DR   PDB; 5CMX; X-ray; 2.98 A; H=364-622, L=328-363.
DR   PDB; 5DO4; X-ray; 1.86 A; H=364-621, L=328-363.
DR   PDB; 5E8E; X-ray; 1.90 A; H=364-622, L=328-363.
DR   PDB; 5EDK; X-ray; 3.21 A; A=44-622.
DR   PDB; 5EDM; X-ray; 2.20 A; A=44-622.
DR   PDB; 5EW1; X-ray; 2.95 A; H=364-622, L=328-363.
DR   PDB; 5EW2; X-ray; 3.59 A; H=364-622, L=328-363.
DR   PDB; 5GDS; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 5GIM; X-ray; 2.09 A; A=328-363.
DR   PDB; 5JDU; X-ray; 1.70 A; A/C=331-363, B/D=364-622.
DR   PDB; 5JFD; X-ray; 1.46 A; H=364-622, L=328-363.
DR   PDB; 5JZY; X-ray; 1.27 A; H=364-622, L=328-363.
DR   PDB; 5L6N; X-ray; 1.63 A; H=364-622, L=328-363.
DR   PDB; 5MJT; X-ray; 1.40 A; H=364-622, L=328-363.
DR   PDB; 5MLS; X-ray; 1.62 A; H=364-622, L=328-363.
DR   PDB; 5MM6; X-ray; 1.29 A; H=364-622, L=328-363.
DR   PDB; 5NHU; X-ray; 1.45 A; A/C/H=364-622, B/D/L=328-363.
DR   PDB; 5TO3; X-ray; 2.34 A; A=318-363, B=364-621.
DR   PDB; 5Z5W; NMR; -; A=606-617.
DR   PDB; 5Z5X; NMR; -; A=605-622.
DR   PDB; 6BJR; X-ray; 6.00 A; A=44-622.
DR   PDB; 6C2W; X-ray; 4.12 A; A/B=44-622.
DR   PDB; 6EO6; X-ray; 1.69 A; H=364-622, L=328-363.
DR   PDB; 6EO7; X-ray; 2.24 A; H=364-622, L=328-363.
DR   PDB; 6EO8; X-ray; 1.94 A; H=364-622, L=328-363.
DR   PDB; 6EO9; X-ray; 1.84 A; H=364-622, L=328-363.
DR   PDB; 6V5T; X-ray; 2.10 A; E=333-622.
DR   PDB; 7KME; X-ray; 2.10 A; H=364-622, L=328-363.
DR   PDB; 8KME; X-ray; 2.10 A; 1=328-359, 2=364-620.
DR   PDBsum; 1A2C; -.
DR   PDBsum; 1A3B; -.
DR   PDBsum; 1A3E; -.
DR   PDBsum; 1A46; -.
DR   PDBsum; 1A4W; -.
DR   PDBsum; 1A5G; -.
DR   PDBsum; 1A61; -.
DR   PDBsum; 1ABI; -.
DR   PDBsum; 1ABJ; -.
DR   PDBsum; 1AD8; -.
DR   PDBsum; 1AE8; -.
DR   PDBsum; 1AFE; -.
DR   PDBsum; 1AHT; -.
DR   PDBsum; 1AI8; -.
DR   PDBsum; 1AIX; -.
DR   PDBsum; 1AWF; -.
DR   PDBsum; 1AWH; -.
DR   PDBsum; 1AY6; -.
DR   PDBsum; 1B5G; -.
DR   PDBsum; 1B7X; -.
DR   PDBsum; 1BA8; -.
DR   PDBsum; 1BB0; -.
DR   PDBsum; 1BCU; -.
DR   PDBsum; 1BHX; -.
DR   PDBsum; 1BMM; -.
DR   PDBsum; 1BMN; -.
DR   PDBsum; 1BTH; -.
DR   PDBsum; 1C1U; -.
DR   PDBsum; 1C1V; -.
DR   PDBsum; 1C1W; -.
DR   PDBsum; 1C4U; -.
DR   PDBsum; 1C4V; -.
DR   PDBsum; 1C4Y; -.
DR   PDBsum; 1C5L; -.
DR   PDBsum; 1C5N; -.
DR   PDBsum; 1C5O; -.
DR   PDBsum; 1CA8; -.
DR   PDBsum; 1D3D; -.
DR   PDBsum; 1D3P; -.
DR   PDBsum; 1D3Q; -.
DR   PDBsum; 1D3T; -.
DR   PDBsum; 1D4P; -.
DR   PDBsum; 1D6W; -.
DR   PDBsum; 1D9I; -.
DR   PDBsum; 1DE7; -.
DR   PDBsum; 1DIT; -.
DR   PDBsum; 1DM4; -.
DR   PDBsum; 1DOJ; -.
DR   PDBsum; 1DWB; -.
DR   PDBsum; 1DWC; -.
DR   PDBsum; 1DWD; -.
DR   PDBsum; 1DWE; -.
DR   PDBsum; 1DX5; -.
DR   PDBsum; 1E0F; -.
DR   PDBsum; 1EB1; -.
DR   PDBsum; 1EOJ; -.
DR   PDBsum; 1EOL; -.
DR   PDBsum; 1FPC; -.
DR   PDBsum; 1FPH; -.
DR   PDBsum; 1G30; -.
DR   PDBsum; 1G32; -.
DR   PDBsum; 1G37; -.
DR   PDBsum; 1GHV; -.
DR   PDBsum; 1GHW; -.
DR   PDBsum; 1GHX; -.
DR   PDBsum; 1GHY; -.
DR   PDBsum; 1GJ4; -.
DR   PDBsum; 1GJ5; -.
DR   PDBsum; 1H8D; -.
DR   PDBsum; 1H8I; -.
DR   PDBsum; 1HAG; -.
DR   PDBsum; 1HAH; -.
DR   PDBsum; 1HAI; -.
DR   PDBsum; 1HAO; -.
DR   PDBsum; 1HAP; -.
DR   PDBsum; 1HBT; -.
DR   PDBsum; 1HDT; -.
DR   PDBsum; 1HGT; -.
DR   PDBsum; 1HLT; -.
DR   PDBsum; 1HUT; -.
DR   PDBsum; 1HXE; -.
DR   PDBsum; 1HXF; -.
DR   PDBsum; 1IHS; -.
DR   PDBsum; 1IHT; -.
DR   PDBsum; 1JMO; -.
DR   PDBsum; 1JOU; -.
DR   PDBsum; 1JWT; -.
DR   PDBsum; 1K21; -.
DR   PDBsum; 1K22; -.
DR   PDBsum; 1KTS; -.
DR   PDBsum; 1KTT; -.
DR   PDBsum; 1LHC; -.
DR   PDBsum; 1LHD; -.
DR   PDBsum; 1LHE; -.
DR   PDBsum; 1LHF; -.
DR   PDBsum; 1LHG; -.
DR   PDBsum; 1MH0; -.
DR   PDBsum; 1MU6; -.
DR   PDBsum; 1MU8; -.
DR   PDBsum; 1MUE; -.
DR   PDBsum; 1NM6; -.
DR   PDBsum; 1NO9; -.
DR   PDBsum; 1NRN; -.
DR   PDBsum; 1NRO; -.
DR   PDBsum; 1NRP; -.
DR   PDBsum; 1NRQ; -.
DR   PDBsum; 1NRR; -.
DR   PDBsum; 1NRS; -.
DR   PDBsum; 1NT1; -.
DR   PDBsum; 1NU7; -.
DR   PDBsum; 1NU9; -.
DR   PDBsum; 1NY2; -.
DR   PDBsum; 1NZQ; -.
DR   PDBsum; 1O0D; -.
DR   PDBsum; 1O2G; -.
DR   PDBsum; 1O5G; -.
DR   PDBsum; 1OOK; -.
DR   PDBsum; 1OYT; -.
DR   PDBsum; 1P8V; -.
DR   PDBsum; 1PPB; -.
DR   PDBsum; 1QBV; -.
DR   PDBsum; 1QHR; -.
DR   PDBsum; 1QJ1; -.
DR   PDBsum; 1QJ6; -.
DR   PDBsum; 1QJ7; -.
DR   PDBsum; 1QUR; -.
DR   PDBsum; 1RD3; -.
DR   PDBsum; 1RIW; -.
DR   PDBsum; 1SB1; -.
DR   PDBsum; 1SFQ; -.
DR   PDBsum; 1SG8; -.
DR   PDBsum; 1SGI; -.
DR   PDBsum; 1SHH; -.
DR   PDBsum; 1SL3; -.
DR   PDBsum; 1SR5; -.
DR   PDBsum; 1T4U; -.
DR   PDBsum; 1T4V; -.
DR   PDBsum; 1TA2; -.
DR   PDBsum; 1TA6; -.
DR   PDBsum; 1TB6; -.
DR   PDBsum; 1TBZ; -.
DR   PDBsum; 1THP; -.
DR   PDBsum; 1THR; -.
DR   PDBsum; 1THS; -.
DR   PDBsum; 1TMB; -.
DR   PDBsum; 1TMT; -.
DR   PDBsum; 1TMU; -.
DR   PDBsum; 1TOM; -.
DR   PDBsum; 1TQ0; -.
DR   PDBsum; 1TQ7; -.
DR   PDBsum; 1TWX; -.
DR   PDBsum; 1UMA; -.
DR   PDBsum; 1UVS; -.
DR   PDBsum; 1VR1; -.
DR   PDBsum; 1VZQ; -.
DR   PDBsum; 1W7G; -.
DR   PDBsum; 1WAY; -.
DR   PDBsum; 1WBG; -.
DR   PDBsum; 1XM1; -.
DR   PDBsum; 1XMN; -.
DR   PDBsum; 1YPE; -.
DR   PDBsum; 1YPG; -.
DR   PDBsum; 1YPJ; -.
DR   PDBsum; 1YPK; -.
DR   PDBsum; 1YPL; -.
DR   PDBsum; 1YPM; -.
DR   PDBsum; 1Z71; -.
DR   PDBsum; 1Z8I; -.
DR   PDBsum; 1Z8J; -.
DR   PDBsum; 1ZGI; -.
DR   PDBsum; 1ZGV; -.
DR   PDBsum; 1ZRB; -.
DR   PDBsum; 2A0Q; -.
DR   PDBsum; 2A2X; -.
DR   PDBsum; 2A45; -.
DR   PDBsum; 2AFQ; -.
DR   PDBsum; 2ANK; -.
DR   PDBsum; 2ANM; -.
DR   PDBsum; 2B5T; -.
DR   PDBsum; 2BDY; -.
DR   PDBsum; 2BVR; -.
DR   PDBsum; 2BVS; -.
DR   PDBsum; 2BVX; -.
DR   PDBsum; 2BXT; -.
DR   PDBsum; 2BXU; -.
DR   PDBsum; 2C8W; -.
DR   PDBsum; 2C8X; -.
DR   PDBsum; 2C8Y; -.
DR   PDBsum; 2C8Z; -.
DR   PDBsum; 2C90; -.
DR   PDBsum; 2C93; -.
DR   PDBsum; 2CF8; -.
DR   PDBsum; 2CF9; -.
DR   PDBsum; 2CN0; -.
DR   PDBsum; 2FEQ; -.
DR   PDBsum; 2FES; -.
DR   PDBsum; 2GDE; -.
DR   PDBsum; 2GP9; -.
DR   PDBsum; 2H9T; -.
DR   PDBsum; 2HGT; -.
DR   PDBsum; 2HNT; -.
DR   PDBsum; 2HPP; -.
DR   PDBsum; 2HPQ; -.
DR   PDBsum; 2HWL; -.
DR   PDBsum; 2JH0; -.
DR   PDBsum; 2JH5; -.
DR   PDBsum; 2JH6; -.
DR   PDBsum; 2OD3; -.
DR   PDBsum; 2PGB; -.
DR   PDBsum; 2PGQ; -.
DR   PDBsum; 2PKS; -.
DR   PDBsum; 2PW8; -.
DR   PDBsum; 2R2M; -.
DR   PDBsum; 2THF; -.
DR   PDBsum; 2UUF; -.
DR   PDBsum; 2UUJ; -.
DR   PDBsum; 2UUK; -.
DR   PDBsum; 2V3H; -.
DR   PDBsum; 2V3O; -.
DR   PDBsum; 2ZC9; -.
DR   PDBsum; 2ZDA; -.
DR   PDBsum; 2ZDV; -.
DR   PDBsum; 2ZF0; -.
DR   PDBsum; 2ZFF; -.
DR   PDBsum; 2ZFP; -.
DR   PDBsum; 2ZFQ; -.
DR   PDBsum; 2ZFR; -.
DR   PDBsum; 2ZG0; -.
DR   PDBsum; 2ZGB; -.
DR   PDBsum; 2ZGX; -.
DR   PDBsum; 2ZHE; -.
DR   PDBsum; 2ZHF; -.
DR   PDBsum; 2ZHQ; -.
DR   PDBsum; 2ZHW; -.
DR   PDBsum; 2ZI2; -.
DR   PDBsum; 2ZIQ; -.
DR   PDBsum; 2ZNK; -.
DR   PDBsum; 2ZO3; -.
DR   PDBsum; 3B23; -.
DR   PDBsum; 3B9F; -.
DR   PDBsum; 3BEF; -.
DR   PDBsum; 3BEI; -.
DR   PDBsum; 3BF6; -.
DR   PDBsum; 3BIU; -.
DR   PDBsum; 3BIV; -.
DR   PDBsum; 3BV9; -.
DR   PDBsum; 3C1K; -.
DR   PDBsum; 3C27; -.
DR   PDBsum; 3D49; -.
DR   PDBsum; 3DA9; -.
DR   PDBsum; 3DD2; -.
DR   PDBsum; 3DHK; -.
DR   PDBsum; 3DT0; -.
DR   PDBsum; 3DUX; -.
DR   PDBsum; 3E6P; -.
DR   PDBsum; 3EE0; -.
DR   PDBsum; 3EGK; -.
DR   PDBsum; 3EQ0; -.
DR   PDBsum; 3F68; -.
DR   PDBsum; 3GIC; -.
DR   PDBsum; 3GIS; -.
DR   PDBsum; 3HAT; -.
DR   PDBsum; 3HKJ; -.
DR   PDBsum; 3HTC; -.
DR   PDBsum; 3JZ1; -.
DR   PDBsum; 3JZ2; -.
DR   PDBsum; 3K65; -.
DR   PDBsum; 3LDX; -.
DR   PDBsum; 3LU9; -.
DR   PDBsum; 3NXP; -.
DR   PDBsum; 3P17; -.
DR   PDBsum; 3P6Z; -.
DR   PDBsum; 3P70; -.
DR   PDBsum; 3PMH; -.
DR   PDBsum; 3PO1; -.
DR   PDBsum; 3QDZ; -.
DR   PDBsum; 3QGN; -.
DR   PDBsum; 3QLP; -.
DR   PDBsum; 3QTO; -.
DR   PDBsum; 3QTV; -.
DR   PDBsum; 3QWC; -.
DR   PDBsum; 3QX5; -.
DR   PDBsum; 3R3G; -.
DR   PDBsum; 3RLW; -.
DR   PDBsum; 3RLY; -.
DR   PDBsum; 3RM0; -.
DR   PDBsum; 3RM2; -.
DR   PDBsum; 3RML; -.
DR   PDBsum; 3RMM; -.
DR   PDBsum; 3RMN; -.
DR   PDBsum; 3RMO; -.
DR   PDBsum; 3S7H; -.
DR   PDBsum; 3S7K; -.
DR   PDBsum; 3SHA; -.
DR   PDBsum; 3SHC; -.
DR   PDBsum; 3SI3; -.
DR   PDBsum; 3SI4; -.
DR   PDBsum; 3SQE; -.
DR   PDBsum; 3SQH; -.
DR   PDBsum; 3SV2; -.
DR   PDBsum; 3T5F; -.
DR   PDBsum; 3TU7; -.
DR   PDBsum; 3U69; -.
DR   PDBsum; 3U8O; -.
DR   PDBsum; 3U8R; -.
DR   PDBsum; 3U8T; -.
DR   PDBsum; 3U98; -.
DR   PDBsum; 3U9A; -.
DR   PDBsum; 3UTU; -.
DR   PDBsum; 3UWJ; -.
DR   PDBsum; 3VXE; -.
DR   PDBsum; 3VXF; -.
DR   PDBsum; 4AX9; -.
DR   PDBsum; 4AYV; -.
DR   PDBsum; 4AYY; -.
DR   PDBsum; 4AZ2; -.
DR   PDBsum; 4BAH; -.
DR   PDBsum; 4BAK; -.
DR   PDBsum; 4BAM; -.
DR   PDBsum; 4BAN; -.
DR   PDBsum; 4BAO; -.
DR   PDBsum; 4BAQ; -.
DR   PDBsum; 4BOH; -.
DR   PDBsum; 4CH2; -.
DR   PDBsum; 4CH8; -.
DR   PDBsum; 4DIH; -.
DR   PDBsum; 4DII; -.
DR   PDBsum; 4DT7; -.
DR   PDBsum; 4DY7; -.
DR   PDBsum; 4E05; -.
DR   PDBsum; 4E06; -.
DR   PDBsum; 4E7R; -.
DR   PDBsum; 4H6S; -.
DR   PDBsum; 4H6T; -.
DR   PDBsum; 4HFP; -.
DR   PDBsum; 4HTC; -.
DR   PDBsum; 4HZH; -.
DR   PDBsum; 4I7Y; -.
DR   PDBsum; 4LOY; -.
DR   PDBsum; 4LXB; -.
DR   PDBsum; 4LZ1; -.
DR   PDBsum; 4LZ4; -.
DR   PDBsum; 4MLF; -.
DR   PDBsum; 4NZQ; -.
DR   PDBsum; 4O03; -.
DR   PDBsum; 4RKJ; -.
DR   PDBsum; 4RKO; -.
DR   PDBsum; 4RN6; -.
DR   PDBsum; 4THN; -.
DR   PDBsum; 4UD9; -.
DR   PDBsum; 4UDW; -.
DR   PDBsum; 4UE7; -.
DR   PDBsum; 4UEH; -.
DR   PDBsum; 4UFD; -.
DR   PDBsum; 4UFE; -.
DR   PDBsum; 4UFF; -.
DR   PDBsum; 4UFG; -.
DR   PDBsum; 4YES; -.
DR   PDBsum; 5A2M; -.
DR   PDBsum; 5AF9; -.
DR   PDBsum; 5AFY; -.
DR   PDBsum; 5AFZ; -.
DR   PDBsum; 5AHG; -.
DR   PDBsum; 5CMX; -.
DR   PDBsum; 5DO4; -.
DR   PDBsum; 5E8E; -.
DR   PDBsum; 5EDK; -.
DR   PDBsum; 5EDM; -.
DR   PDBsum; 5EW1; -.
DR   PDBsum; 5EW2; -.
DR   PDBsum; 5GDS; -.
DR   PDBsum; 5GIM; -.
DR   PDBsum; 5JDU; -.
DR   PDBsum; 5JFD; -.
DR   PDBsum; 5JZY; -.
DR   PDBsum; 5L6N; -.
DR   PDBsum; 5MJT; -.
DR   PDBsum; 5MLS; -.
DR   PDBsum; 5MM6; -.
DR   PDBsum; 5NHU; -.
DR   PDBsum; 5TO3; -.
DR   PDBsum; 5Z5W; -.
DR   PDBsum; 5Z5X; -.
DR   PDBsum; 6BJR; -.
DR   PDBsum; 6C2W; -.
DR   PDBsum; 6EO6; -.
DR   PDBsum; 6EO7; -.
DR   PDBsum; 6EO8; -.
DR   PDBsum; 6EO9; -.
DR   PDBsum; 6V5T; -.
DR   PDBsum; 7KME; -.
DR   PDBsum; 8KME; -.
DR   BMRB; P00734; -.
DR   SMR; P00734; -.
DR   BioGRID; 108447; 24.
DR   ComplexPortal; CPX-6222; alpha-thrombin complex.
DR   DIP; DIP-6115N; -.
DR   IntAct; P00734; 16.
DR   MINT; P00734; -.
DR   STRING; 9606.ENSP00000308541; -.
DR   BindingDB; P00734; -.
DR   ChEMBL; CHEMBL204; -.
DR   DrugBank; DB07211; (2R)-2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}PROPENE-1-SULFONAMIDE.
DR   DrugBank; DB07796; (3ASR,4RS,8ASR,8BRS)-4-(2-(4-FLUOROBENZYL)-1,3-DIOXODEACAHYDROPYRROLO[3,4-A] PYRROLIZIN-4-YL)BENZAMIDINE.
DR   DrugBank; DB07016; (3R)-8-(dioxidosulfanyl)-3-methyl-1,2,3,4-tetrahydroquinoline.
DR   DrugBank; DB07521; (3Z,6S)-6-Chloro-1-(2-{[(5-chloro-1-benzothiophen-3-yl)methyl]amino}ethyl)-3-({2-[(2R)-2-piperidinyl]ethyl}imino)-2-piperazinol.
DR   DrugBank; DB06850; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexylamino)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07091; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclohexyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB06845; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentylamino)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07088; (S)-N-(4-carbamimidoylbenzyl)-1-(2-(cyclopentyloxy)ethanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07131; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclohexylpropanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07095; (S)-N-(4-carbamimidoylbenzyl)-1-(3-cyclopentylpropanoyl)pyrrolidine-2-carboxamide.
DR   DrugBank; DB07515; 1-(2-{[(6-amino-2-methylpyridin-3-yl)methyl]amino}ethyl)-6-chloro-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-1,4-dihydropyrazin-2-ol.
DR   DrugBank; DB07897; 1-(HYDROXYMETHYLENEAMINO)-8-HYDROXY-OCTANE.
DR   DrugBank; DB06878; 1-[(2R)-2-aminobutanoyl]-N-(3-chlorobenzyl)-L-prolinamide.
DR   DrugBank; DB06947; 1-[(2R)-2-aminobutanoyl]-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB08624; 1-[(4S)-4-amino-5-(1,3-benzothiazol-2-yl)-5-oxopentyl]guanidine.
DR   DrugBank; DB06869; 1-[2-AMINO-2-CYCLOHEXYL-ACETYL]-PYRROLIDINE-3-CARBOXYLIC ACID 5-CHLORO-2-(2-ETHYLCARBAMOYL-ETHOXY)-BENZYLAMIDE.
DR   DrugBank; DB06929; 1-butanoyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB07400; 1-ETHOXYCARBONYL-D-PHE-PRO-2(4-AMINOBUTYL)HYDRAZINE.
DR   DrugBank; DB04771; 1-GUANIDINO-4-(N-NITRO-BENZOYLAMINO-L-LEUCYL-L-PROLYLAMINO)BUTANE.
DR   DrugBank; DB04772; 1-GUANIDINO-4-(N-PHENYLMETHANESULFONYL-L-LEUCYL-L-PROLYLAMINO)BUTANE.
DR   DrugBank; DB02287; 2-(2-hydroxy-phenyl)-3H-benzoimidazole-5-carboxamidine.
DR   DrugBank; DB07277; 2-(5-CHLORO-2-THIENYL)-N-{(3S)-1-[(1S)-1-METHYL-2-MORPHOLIN-4-YL-2-OXOETHYL]-2-OXOPYRROLIDIN-3-YL}ETHANESULFONAMIDE.
DR   DrugBank; DB07550; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(1-OXIDO-2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUOROPHENYL)METHYL]ACETAMIDE.
DR   DrugBank; DB07549; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-3-METHYL-6-PYRIDINYL)METHYL]ACETAMIDE.
DR   DrugBank; DB07548; 2-(6-CHLORO-3-{[2,2-DIFLUORO-2-(2-PYRIDINYL)ETHYL]AMINO}-2-OXO-1(2H)-PYRAZINYL)-N-[(2-FLUORO-6-PYRIDINYL)METHYL]ACETAMIDE.
DR   DrugBank; DB07105; 2-[2-(4-Chloro-Phenylsulfanyl)-Acetylamino]-3-(4-Guanidino-Phenyl)-Propionamide.
DR   DrugBank; DB04722; 2-[3-chloro-6-[2,2-difluoro-2-(1-oxidopyridin-1-ium-2-yl)ethyl]imino-1-hydroxypyridin-2-yl]-N-[(1R)-1-(3-chlorophenyl)ethyl]acetamide.
DR   DrugBank; DB07366; 2-[N'-(4-AMINO-BUTYL)-HYDRAZINOCARBONYL]-PYRROLIDINE-1-CARBOXYLIC ACID BENZYL ESTER.
DR   DrugBank; DB08254; 2-Naphthalenesulfonic acid.
DR   DrugBank; DB01725; 2-{2-hydroxy-[1,1'-biphenyl]-3-yl}-1H-1,3-benzodiazole-5-carboximidamide.
DR   DrugBank; DB08062; 3-(4-CHLOROPHENYL)-5-(METHYLTHIO)-4H-1,2,4-TRIAZOLE.
DR   DrugBank; DB07639; 3-(7-DIAMINOMETHYL-NAPHTHALEN-2-YL)-PROPIONIC ACID ETHYL ESTER.
DR   DrugBank; DB07461; 3-AMINO-3-BENZYL-9-CARBOXAMIDE[4.3.0]BICYCLO-1,6-DIAZANONAN-2-ONE.
DR   DrugBank; DB07120; 3-Carbamimidamido-1,1-diphenylurea.
DR   DrugBank; DB07190; 3-cyclohexyl-D-alanyl-N-(3-chlorobenzyl)-L-prolinamide.
DR   DrugBank; DB07741; 4-(1R,3AS,4R,8AS,8BR)-[1-DIFLUOROMETHYL-2-(4-FLUOROBENZYL)-3-OXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZAMIDINE.
DR   DrugBank; DB07353; 4-(2,5-DIAMINO-5-HYDROXY-PENTYL)-PHENOL.
DR   DrugBank; DB07508; 4-(5-BENZENESULFONYLAMINO-1-METHYL-1H-BENZOIMIDAZOL-2-YLMETHYL)-BENZAMIDINE.
DR   DrugBank; DB07809; 4-({[4-(3-METHYLBENZOYL)PYRIDIN-2-YL]AMINO}METHYL)BENZENECARBOXIMIDAMIDE.
DR   DrugBank; DB08546; 4-[(3AS,4R,7R,8AS,8BR)-2-(1,3-BENZODIOXOL-5-YLMETHYL)-7-HYDROXY-1,3-DIOXODECAHYDROPYRROLO[3,4-A]PYRROLIZIN-4-YL]BENZENECARBOXIMIDAMIDE.
DR   DrugBank; DB08061; 4-[3-(4-CHLOROPHENYL)-1H-PYRAZOL-5-YL]PIPERIDINE.
DR   DrugBank; DB07718; 4-Hydroxyphenylpyruvic acid.
DR   DrugBank; DB03136; 4-Iodobenzo[B]Thiophene-2-Carboxamidine.
DR   DrugBank; DB02723; 4-Oxo-2-Phenylmethanesulfonyl-Octahydro-Pyrrolo[1,2-a]Pyrazine-6-Carboxylic Acid [1-(N-Hydroxycarbamimidoyl)-Piperidin-4-Ylmethyl]-Amide.
DR   DrugBank; DB07440; 4-TERT-BUTYLBENZENESULFONIC ACID.
DR   DrugBank; DB07376; 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID).
DR   DrugBank; DB06861; 6-(2-HYDROXY-CYCLOPENTYL)-7-OXO-HEPTANAMIDINE.
DR   DrugBank; DB06866; 6-CARBAMIMIDOYL-2-[2-HYDROXY-5-(3-METHOXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID.
DR   DrugBank; DB06865; 6-CARBAMIMIDOYL-2-[2-HYDROXY-6-(4-HYDROXY-PHENYL)-INDAN-1-YL]-HEXANOIC ACID.
DR   DrugBank; DB03865; 6-Chloro-2-(2-Hydroxy-Biphenyl-3-Yl)-1h-Indole-5-Carboxamidine.
DR   DrugBank; DB06841; [(2R)-1-[(2S)-2-[[(2S,3S)-1-Chloro-6-(diaminomethylideneamino)-2-hydroxyhexan-3-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]azanium.
DR   DrugBank; DB07934; [[CYCLOHEXANESULFONYL-GLYCYL]-3[PYRIDIN-4-YL-AMINOMETHYL]ALANYL]PIPERIDINE.
DR   DrugBank; DB08422; [PHENYLALANINYL-PROLINYL]-[2-(PYRIDIN-4-YLAMINO)-ETHYL]-AMINE.
DR   DrugBank; DB07659; AC-(D)PHE-PRO-BOROHOMOLYS-OH.
DR   DrugBank; DB07660; AC-(D)PHE-PRO-BOROHOMOORNITHINE-OH.
DR   DrugBank; DB07658; AC-(D)Phe-pro-borolys-OH.
DR   DrugBank; DB13151; Anti-inhibitor coagulant complex.
DR   DrugBank; DB00025; Antihemophilic factor, human recombinant.
DR   DrugBank; DB11166; Antithrombin Alfa.
DR   DrugBank; DB00278; Argatroban.
DR   DrugBank; DB01766; Beta-(2-Naphthyl)-Alanine.
DR   DrugBank; DB07083; beta-phenyl-D-phenylalanyl-N-propyl-L-prolinamide.
DR   DrugBank; DB12364; Betrixaban.
DR   DrugBank; DB00006; Bivalirudin.
DR   DrugBank; DB00100; Coagulation Factor IX (Recombinant).
DR   DrugBank; DB13152; Coagulation Factor IX Human.
DR   DrugBank; DB09228; Conestat alfa.
DR   DrugBank; DB09130; Copper.
DR   DrugBank; DB03159; CRA_8696.
DR   DrugBank; DB06911; D-leucyl-N-(3-chlorobenzyl)-L-prolinamide.
DR   DrugBank; DB06996; D-leucyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB06919; D-phenylalanyl-N-(3-chlorobenzyl)-L-prolinamide.
DR   DrugBank; DB07027; D-phenylalanyl-N-(3-fluorobenzyl)-L-prolinamide.
DR   DrugBank; DB07133; D-phenylalanyl-N-(3-methylbenzyl)-L-prolinamide.
DR   DrugBank; DB07143; D-phenylalanyl-N-benzyl-L-prolinamide.
DR   DrugBank; DB07005; D-phenylalanyl-N-{4-[amino(iminio)methyl]benzyl}-L-prolinamide.
DR   DrugBank; DB06695; Dabigatran etexilate.
DR   DrugBank; DB00055; Drotrecogin alfa.
DR   DrugBank; DB05714; Flovagatran.
DR   DrugBank; DB12831; Gabexate.
DR   DrugBank; DB03847; gamma-carboxy-L-glutamic acid.
DR   DrugBank; DB07278; GW-813893.
DR   DrugBank; DB01767; Hemi-Babim.
DR   DrugBank; DB06404; Human C1-esterase inhibitor.
DR   DrugBank; DB09332; Kappadione.
DR   DrugBank; DB00001; Lepirudin.
DR   DrugBank; DB13998; Lonoctocog alfa.
DR   DrugBank; DB04136; Lysophosphotidylserine.
DR   DrugBank; DB00170; Menadione.
DR   DrugBank; DB06838; methyl L-phenylalaninate.
DR   DrugBank; DB13999; Moroctocog alfa.
DR   DrugBank; DB06868; N-(3-chlorobenzyl)-1-(4-methylpentanoyl)-L-prolinamide.
DR   DrugBank; DB06942; N-(4-carbamimidoylbenzyl)-1-(3-phenylpropanoyl)-L-prolinamide.
DR   DrugBank; DB06936; N-(4-carbamimidoylbenzyl)-1-(4-methylpentanoyl)-L-prolinamide.
DR   DrugBank; DB07165; N-(5-CHLORO-BENZO[B]THIOPHEN-3-YLMETHYL)-2-[6-CHLORO-OXO-3-(2-PYRIDIN-2-YL-ETHYLAMINO)-2H-PYRAZIN-1-YL]-ACETAMIDE.
DR   DrugBank; DB07527; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]-4-METHOXY-2,3,6-TRIMETHYLBENZENESULFONAMIDE.
DR   DrugBank; DB07522; N-[(2R,3S)-3-AMINO-2-HYDROXY-4-PHENYLBUTYL]NAPHTHALENE-2-SULFONAMIDE.
DR   DrugBank; DB07665; N-[2-(carbamimidamidooxy)ethyl]-2-{6-cyano-3-[(2,2-difluoro-2-pyridin-2-ylethyl)amino]-2-fluorophenyl}acetamide.
DR   DrugBank; DB07946; N-[2-({[amino(imino)methyl]amino}oxy)ethyl]-2-{6-chloro-3-[(2,2-difluoro-2-phenylethyl)amino]-2-fluorophenyl}acetamide.
DR   DrugBank; DB06859; N-ALLYL-5-AMIDINOAMINOOXY-PROPYLOXY-3-CHLORO-N-CYCLOPENTYLBENZAMIDE.
DR   DrugBank; DB06853; N-cycloheptylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB06858; N-cyclooctylglycyl-N-(4-carbamimidoylbenzyl)-L-prolinamide.
DR   DrugBank; DB07279; N-ETHYL-N-ISOPROPYL-3-METHYL-5-{[(2S)-2-(PYRIDIN-4-YLAMINO)PROPYL]OXY}BENZAMIDE.
DR   DrugBank; DB08187; N-Methylphenylalanyl-N-[(trans-4-aminocyclohexyl)methyl]-L-prolinamide.
DR   DrugBank; DB04591; N-{2,2-DIFLUORO-2-[(2R)-PIPERIDIN-2-YL]ETHYL}-2-[2-(1H-1,2,4-TRIAZOL-1-YL)BENZYL][1,3]OXAZOLO[4,5-C]PYRIDIN-4-AMINE.
DR   DrugBank; DB07944; N-{3-METHYL-5-[2-(PYRIDIN-4-YLAMINO)-ETHOXY]-PHENYL}-BENZENESULFONAMIDE.
DR   DrugBank; DB07128; N7-BUTYL-N2-(5-CHLORO-2-METHYLPHENYL)-5-METHYL[1,2,4]TRIAZOLO[1,5-A]PYRIMIDINE-2,7-DIAMINE.
DR   DrugBank; DB12598; Nafamostat.
DR   DrugBank; DB01123; Proflavine.
DR   DrugBank; DB04786; Suramin.
DR   DrugBank; DB05777; Thrombomodulin Alfa.
DR   DrugBank; DB04697; TRANS-4-(GUANIDINOMETHYL)-CYCLOHEXANE-L-YL-D-3-CYCLOHEXYLALANYL-L-AZETIDINE-2-YL-D-TYROSINYL-L-HOMOARGININAMIDE.
DR   DrugBank; DB09109; Turoctocog alfa.
DR   DrugBank; DB14738; Turoctocog alfa pegol.
DR   DrugBank; DB04898; Ximelagatran.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB08152; {(2S)-1-[N-(tert-butoxycarbonyl)glycyl]pyrrolidin-2-yl}methyl (3-chlorophenyl)acetate.
DR   DrugCentral; P00734; -.
DR   GuidetoPHARMACOLOGY; 2362; -.
DR   MEROPS; S01.217; -.
DR   MoonDB; P00734; Curated.
DR   GlyConnect; 518; 39 N-Linked glycans (4 sites).
DR   GlyGen; P00734; 10 sites, 51 N-linked glycans (4 sites), 1 O-linked glycan (6 sites).
DR   iPTMnet; P00734; -.
DR   PhosphoSitePlus; P00734; -.
DR   BioMuta; F2; -.
DR   DMDM; 135807; -.
DR   SWISS-2DPAGE; P00734; -.
DR   EPD; P00734; -.
DR   jPOST; P00734; -.
DR   MassIVE; P00734; -.
DR   MaxQB; P00734; -.
DR   PaxDb; P00734; -.
DR   PeptideAtlas; P00734; -.
DR   PRIDE; P00734; -.
DR   ProteomicsDB; 51269; -.
DR   TopDownProteomics; P00734; -.
DR   ABCD; P00734; 3 sequenced antibodies.
DR   Antibodypedia; 857; 1158 antibodies.
DR   DNASU; 2147; -.
DR   Ensembl; ENST00000311907; ENSP00000308541; ENSG00000180210.
DR   GeneID; 2147; -.
DR   KEGG; hsa:2147; -.
DR   UCSC; uc001ndf.5; human.
DR   CTD; 2147; -.
DR   DisGeNET; 2147; -.
DR   GeneCards; F2; -.
DR   GeneReviews; F2; -.
DR   HGNC; HGNC:3535; F2.
DR   HPA; ENSG00000180210; Tissue enriched (liver).
DR   MalaCards; F2; -.
DR   MIM; 176930; gene.
DR   MIM; 188050; phenotype.
DR   MIM; 601367; phenotype.
DR   MIM; 613679; phenotype.
DR   MIM; 614390; phenotype.
DR   neXtProt; NX_P00734; -.
DR   OpenTargets; ENSG00000180210; -.
DR   Orphanet; 329217; Cerebral sinovenous thrombosis.
DR   Orphanet; 325; Congenital factor II deficiency.
DR   Orphanet; 64738; NON RARE IN EUROPE: Non rare thrombophilia.
DR   PharmGKB; PA157; -.
DR   VEuPathDB; HostDB:ENSG00000180210; -.
DR   eggNOG; ENOG502QTSX; Eukaryota.
DR   GeneTree; ENSGT00940000154234; -.
DR   HOGENOM; CLU_006842_19_4_1; -.
DR   InParanoid; P00734; -.
DR   OMA; VMIFRKS; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P00734; -.
DR   TreeFam; TF327329; -.
DR   BRENDA; 3.4.21.5; 2681.
DR   PathwayCommons; P00734; -.
DR   Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR   Reactome; R-HSA-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-HSA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR   Reactome; R-HSA-9657688; Defective factor XII causes hereditary angioedema.
DR   Reactome; R-HSA-9672391; Defective F8 cleavage by thrombin.
DR   Reactome; R-HSA-977606; Regulation of Complement cascade.
DR   SABIO-RK; P00734; -.
DR   SIGNOR; P00734; -.
DR   BioGRID-ORCS; 2147; 10 hits in 1004 CRISPR screens.
DR   EvolutionaryTrace; P00734; -.
DR   GeneWiki; Thrombin; -.
DR   GenomeRNAi; 2147; -.
DR   Pharos; P00734; Tclin.
DR   PRO; PR:P00734; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P00734; protein.
DR   Bgee; ENSG00000180210; Expressed in right lobe of liver and 93 other tissues.
DR   ExpressionAtlas; P00734; baseline and differential.
DR   Genevisible; P00734; HS.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; TAS:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0070053; F:thrombospondin receptor activity; IDA:BHF-UCL.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0051838; P:cytolysis by host of symbiont cells; IDA:UniProtKB.
DR   GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:BHF-UCL.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
DR   GO; GO:0051918; P:negative regulation of fibrinolysis; TAS:BHF-UCL.
DR   GO; GO:0010544; P:negative regulation of platelet activation; TAS:BHF-UCL.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IDA:BHF-UCL.
DR   GO; GO:0070945; P:neutrophil-mediated killing of gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0030168; P:platelet activation; IDA:BHF-UCL.
DR   GO; GO:0030194; P:positive regulation of blood coagulation; IDA:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0090218; P:positive regulation of lipid kinase activity; IDA:BHF-UCL.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:1900738; P:positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; NAS:BHF-UCL.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0030193; P:regulation of blood coagulation; TAS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR   GO; GO:0009611; P:response to wounding; IDA:BHF-UCL.
DR   CDD; cd00108; KR; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   Gene3D; 2.40.20.10; -; 2.
DR   Gene3D; 4.10.140.10; -; 1.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR003966; Prothrombin/thrombin.
DR   InterPro; IPR018992; Thrombin_light_chain.
DR   InterPro; IPR037111; Thrombin_light_chain_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24254:SF10; PTHR24254:SF10; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00051; Kringle; 2.
DR   Pfam; PF09396; Thrombin_light; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001149; Thrombin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   PRINTS; PR01505; PROTHROMBIN.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00130; KR; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57440; SSF57440; 2.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS00021; KRINGLE_1; 2.
DR   PROSITE; PS50070; KRINGLE_2; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acute phase; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disease variant; Disulfide bond; Gamma-carboxyglutamic acid; Glycoprotein;
KW   Hemostasis; Hydrolase; Kringle; Pharmaceutical; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Thrombophilia; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..43
FT                   /evidence="ECO:0000269|PubMed:266717,
FT                   ECO:0000269|PubMed:8073540"
FT                   /id="PRO_0000028159"
FT   CHAIN           44..622
FT                   /note="Prothrombin"
FT                   /id="PRO_0000028160"
FT   PEPTIDE         44..198
FT                   /note="Activation peptide fragment 1"
FT                   /id="PRO_0000028161"
FT   PEPTIDE         199..327
FT                   /note="Activation peptide fragment 2"
FT                   /id="PRO_0000028162"
FT   CHAIN           328..363
FT                   /note="Thrombin light chain"
FT                   /id="PRO_0000028163"
FT   CHAIN           364..622
FT                   /note="Thrombin heavy chain"
FT                   /id="PRO_0000028164"
FT   DOMAIN          44..89
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          108..186
FT                   /note="Kringle 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          213..291
FT                   /note="Kringle 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT   DOMAIN          364..618
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   REGION          551..573
FT                   /note="High affinity receptor-binding region which is also
FT                   known as the TP508 peptide"
FT   ACT_SITE        406
FT                   /note="Charge relay system"
FT   ACT_SITE        462
FT                   /note="Charge relay system"
FT   ACT_SITE        568
FT                   /note="Charge relay system"
FT   SITE            198..199
FT                   /note="Cleavage; by thrombin"
FT   SITE            327..328
FT                   /note="Cleavage; by factor Xa"
FT   SITE            363..364
FT                   /note="Cleavage; by factor Xa"
FT   MOD_RES         49
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407"
FT   MOD_RES         50
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407"
FT   MOD_RES         57
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         59
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         62
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         63
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         68
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         69
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         72
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   MOD_RES         75
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:6305407"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:14760718,
FT                   ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320"
FT   CARBOHYD        416
FT                   /note="N-linked (GlcNAc...) (complex) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952,
FT                   ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218,
FT                   ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923"
FT   DISULFID        60..65
FT   DISULFID        90..103
FT   DISULFID        108..186
FT   DISULFID        129..169
FT   DISULFID        157..181
FT   DISULFID        213..291
FT   DISULFID        234..274
FT   DISULFID        262..286
FT   DISULFID        336..482
FT                   /note="Interchain (between light and heavy chains)"
FT   DISULFID        391..407
FT   DISULFID        536..550
FT                   /evidence="ECO:0000250"
FT   DISULFID        564..594
FT                   /evidence="ECO:0000250"
FT   VARIANT         72
FT                   /note="E -> G (in FA2D; Shanghai)"
FT                   /evidence="ECO:0000269|PubMed:14962227"
FT                   /id="VAR_055232"
FT   VARIANT         165
FT                   /note="T -> M (confirmed at protein level; dbSNP:rs5896)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_011781"
FT   VARIANT         200
FT                   /note="E -> K (in FA2D; prothrombin type 3; variant
FT                   confirmed at protein level; dbSNP:rs62623459)"
FT                   /evidence="ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|PubMed:6405779"
FT                   /id="VAR_006711"
FT   VARIANT         314
FT                   /note="R -> C (in FA2D; Barcelona/Madrid;
FT                   dbSNP:rs121918477)"
FT                   /evidence="ECO:0000269|PubMed:3771562"
FT                   /id="VAR_006712"
FT   VARIANT         314
FT                   /note="R -> H (in FA2D; Padua-1; dbSNP:rs754231232)"
FT                   /evidence="ECO:0000269|PubMed:7865694"
FT                   /id="VAR_006713"
FT   VARIANT         380
FT                   /note="M -> T (in FA2D; Himi-1; dbSNP:rs121918481)"
FT                   /evidence="ECO:0000269|PubMed:1421398"
FT                   /id="VAR_006714"
FT   VARIANT         386
FT                   /note="P -> T (confirmed at protein level; dbSNP:rs5897)"
FT                   /evidence="ECO:0000269|PubMed:10391209,
FT                   ECO:0000269|PubMed:22028381"
FT                   /id="VAR_011782"
FT   VARIANT         425
FT                   /note="R -> C (in FA2D; Quick-1; dbSNP:rs121918479)"
FT                   /evidence="ECO:0000269|PubMed:3242619"
FT                   /id="VAR_006715"
FT   VARIANT         431
FT                   /note="R -> H (in FA2D; Himi-2; dbSNP:rs121918482)"
FT                   /evidence="ECO:0000269|PubMed:1421398"
FT                   /id="VAR_006716"
FT   VARIANT         461
FT                   /note="R -> W (in FA2D; Tokushima; dbSNP:rs121918478)"
FT                   /evidence="ECO:0000269|PubMed:1349838,
FT                   ECO:0000269|PubMed:3567158, ECO:0000269|PubMed:3801671"
FT                   /id="VAR_006717"
FT   VARIANT         509
FT                   /note="E -> A (in FA2D; Salakta/Frankfurt)"
FT                   /evidence="ECO:0000269|PubMed:1354985,
FT                   ECO:0000269|PubMed:7792730"
FT                   /id="VAR_006718"
FT   VARIANT         532
FT                   /note="E -> Q"
FT                   /evidence="ECO:0000269|PubMed:22028381,
FT                   ECO:0000269|PubMed:873923"
FT                   /id="VAR_068913"
FT   VARIANT         601
FT                   /note="G -> V (in FA2D; Quick-2; dbSNP:rs121918480)"
FT                   /evidence="ECO:0000269|PubMed:2719946"
FT                   /id="VAR_006719"
FT   CONFLICT        9..25
FT                   /note="Missing (in Ref. 3; BAG64719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="S -> N (in Ref. 4; BAD96497)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="H -> N (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="N -> S (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="T -> I (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="T -> N (in Ref. 7; CAA23842)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        176
FT                   /note="V -> A (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="I -> T (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194..195
FT                   /note="AM -> MV (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        308
FT                   /note="D -> DEE (in Ref. 9; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="G -> R (in Ref. 4; BAD96495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        369
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        485
FT                   /note="D -> N (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="Q -> G (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="W -> Y (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="E -> S (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        511
FT                   /note="W -> V (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="N -> D (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        529..530
FT                   /note="PI -> AL (in Ref. 10; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        590..592
FT                   /note="WGE -> AGA (in Ref. 11; AAR08143)"
FT                   /evidence="ECO:0000305"
FT   HELIX           47..60
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   HELIX           67..74
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   HELIX           77..89
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   HELIX           97..105
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:4HZH"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:5EDK"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:5EDK"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          148..150
FT                   /evidence="ECO:0007829|PDB:4NZQ"
FT   STRAND          167..173
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   TURN            186..188
FT                   /evidence="ECO:0007829|PDB:4NZQ"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          211..214
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   HELIX           216..218
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:4HZH"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:4HZH"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:4NZQ"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:5EDK"
FT   STRAND          253..255
FT                   /evidence="ECO:0007829|PDB:5EDK"
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:3BEI"
FT   TURN            326..328
FT                   /evidence="ECO:0007829|PDB:4O03"
FT   HELIX           329..333
FT                   /evidence="ECO:0007829|PDB:5NHU"
FT   TURN            334..337
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            340..342
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           343..345
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           352..358
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            360..362
FT                   /evidence="ECO:0007829|PDB:1NO9"
FT   STRAND          367..369
FT                   /evidence="ECO:0007829|PDB:3SQH"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:3QDZ"
FT   STRAND          378..383
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            384..387
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          388..395
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          397..403
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           405..407
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          408..410
FT                   /evidence="ECO:0007829|PDB:4DY7"
FT   HELIX           411..413
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           419..421
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          422..427
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          430..433
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            436..438
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          440..449
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            455..458
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          464..470
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:4O03"
FT   HELIX           486..492
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          495..497
FT                   /evidence="ECO:0007829|PDB:5EDM"
FT   STRAND          498..504
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          507..510
FT                   /evidence="ECO:0007829|PDB:4UD9"
FT   TURN            513..515
FT                   /evidence="ECO:0007829|PDB:4CH2"
FT   STRAND          516..518
FT                   /evidence="ECO:0007829|PDB:4CH2"
FT   STRAND          524..530
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           533..538
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          540..542
FT                   /evidence="ECO:0007829|PDB:1MH0"
FT   STRAND          548..551
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           555..557
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            565..569
FT                   /evidence="ECO:0007829|PDB:3U8O"
FT   STRAND          571..575
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   TURN            577..579
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          582..590
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          592..595
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   STRAND          596..598
FT                   /evidence="ECO:0007829|PDB:3K65"
FT   STRAND          601..605
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           607..609
FT                   /evidence="ECO:0007829|PDB:5AFY"
FT   HELIX           610..619
FT                   /evidence="ECO:0007829|PDB:5AFY"
SQ   SEQUENCE   622 AA;  70037 MW;  8A25E1DA88208FCF CRC64;
     MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFLEE VRKGNLEREC
     VEETCSYEEA FEALESSTAT DVFWAKYTAC ETARTPRDKL AACLEGNCAE GLGTNYRGHV
     NITRSGIECQ LWRSRYPHKP EINSTTHPGA DLQENFCRNP DSSTTGPWCY TTDPTVRRQE
     CSIPVCGQDQ VTVAMTPRSE GSSVNLSPPL EQCVPDRGQQ YQGRLAVTTH GLPCLAWASA
     QAKALSKHQD FNSAVQLVEN FCRNPDGDEE GVWCYVAGKP GDFGYCDLNY CEEAVEEETG
     DGLDEDSDRA IEGRTATSEY QTFFNPRTFG SGEADCGLRP LFEKKSLEDK TERELLESYI
     DGRIVEGSDA EIGMSPWQVM LFRKSPQELL CGASLISDRW VLTAAHCLLY PPWDKNFTEN
     DLLVRIGKHS RTRYERNIEK ISMLEKIYIH PRYNWRENLD RDIALMKLKK PVAFSDYIHP
     VCLPDRETAA SLLQAGYKGR VTGWGNLKET WTANVGKGQP SVLQVVNLPI VERPVCKDST
     RIRITDNMFC AGYKPDEGKR GDACEGDSGG PFVMKSPFNN RWYQMGIVSW GEGCDRDGKY
     GFYTHVFRLK KWIQKVIDQF GE
//
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