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 27-MAR-2024, entry version 280.
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; DOI=10.1016/s0021-9258(17)40144-x;
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; DOI=10.1016/s0021-9258(18)69292-0;
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 INTERACTION WITH ALPHA-1-MICROGLOBULIN.
RX PubMed=9183005; DOI=10.1111/j.1432-1033.1997.00676.x;
RA Berggaard T., Thelin N., Falkenberg C., Enghild J.J., Akerstroem B.;
RT "Prothrombin, albumin and immunoglobulin A form covalent complexes with
RT alpha1-microglobulin in human plasma.";
RL Eur. J. Biochem. 245:676-683(1997).
RN [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
RP PROTHROMBIN ACTIVATION, AND MUTAGENESIS OF ARG-314; ARG-363 AND SER-568.
RX PubMed=34265300; DOI=10.1016/j.jbc.2021.100955;
RA Stojanovski B.M., Di Cera E.;
RT "Role of sequence and position of the cleavage sites in prothrombin
RT activation.";
RL J. Biol. Chem. 297:100955-100955(2021).
RN [28]
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 [29]
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 [30]
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 [31]
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 [32]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=8071320; DOI=10.1016/s0021-9258(17)31746-5;
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
RP VARIANT FA2D CYS-314, AND PROTEIN SEQUENCE OF 310-327.
RX PubMed=3771562; DOI=10.1016/s0021-9258(18)66826-7;
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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. In plasma,
CC interacts (via N-terminus) with alpha-1-microglobulin with molar ratio
CC 1:2 and 1:1; this interaction does not prevent the activation of
CC prothrombin to thrombin. {ECO:0000269|PubMed:11493008,
CC ECO:0000269|PubMed:16763681, ECO:0000269|PubMed:17685615,
CC ECO:0000269|PubMed:18291642, ECO:0000269|PubMed:18362344,
CC ECO:0000269|PubMed:2369893, ECO:0000269|PubMed:2374926,
CC ECO:0000269|PubMed:9183005}.
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 PRO_0000028160; PRO_0000032489 [P01008]: SERPINC1; NbExp=2; IntAct=EBI-26959170, EBI-26959093;
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 -!- PTM: In the penultimate step of the coagulation cascade, prothrombin is
CC converted to thrombin by the prothrombinase complex composed of factor
CC Xa (F10), cofactor Va (F5), and phospholipids. This activation requires
CC factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg-
CC 363, along 2 possible pathways. In the first pathway, the first
CC cleavage occurs at Arg-314, leading to the formation of the inactive
CC intermediate prethrombin-2. This pathway preferentially occurs on
CC platelets and in the absence of cofactor Va. In the second pathway, the
CC first cleavage occurs at Arg-363, which separates protease domain into
CC 2 chains that remain connected through a disulfide bond and generates
CC the active intermediate meizothrombin. The presence of cofactor Va
CC directs activation along the meizothrombin pathway and greatly
CC accelerates the rate of cleavage at Arg-363, but has a smaller effect
CC on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates
CC as an intermediate when prothrombinase is assembled on the membrane of
CC red blood cells. {ECO:0000305|PubMed:34265300}.
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: 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; 7TPP; EM; 4.10 A; E=44-622.
DR PDB; 8BWW; NMR; -; A=605-622.
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; 7TPP; -.
DR PDBsum; 8BWW; -.
DR PDBsum; 8KME; -.
DR AlphaFoldDB; P00734; -.
DR BMRB; P00734; -.
DR EMDB; EMD-26060; -.
DR SMR; P00734; -.
DR BioGRID; 108447; 38.
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; 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; DB01225; Enoxaparin.
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 GlyCosmos; P00734; 10 sites, 50 glycans.
DR GlyGen; P00734; 11 sites, 53 N-linked glycans (5 sites), 2 O-linked glycans (7 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; 9606-ENSP00000308541; -.
DR PeptideAtlas; P00734; -.
DR ProteomicsDB; 51269; -.
DR TopDownProteomics; P00734; -.
DR ABCD; P00734; 3 sequenced antibodies.
DR Antibodypedia; 857; 1316 antibodies from 42 providers.
DR DNASU; 2147; -.
DR Ensembl; ENST00000311907.10; ENSP00000308541.5; ENSG00000180210.15.
DR GeneID; 2147; -.
DR KEGG; hsa:2147; -.
DR MANE-Select; ENST00000311907.10; ENSP00000308541.5; NM_000506.5; NP_000497.1.
DR UCSC; uc001ndf.5; human.
DR AGR; HGNC:3535; -.
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; 211181at2759; -.
DR PhylomeDB; P00734; -.
DR TreeFam; TF327329; -.
DR BioCyc; MetaCyc:HS11470-MONOMER; -.
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 SignaLink; P00734; -.
DR SIGNOR; P00734; -.
DR BioGRID-ORCS; 2147; 14 hits in 1152 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 101 other cell types or 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:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1990806; P:ligand-gated ion channel signaling pathway; IEA:Ensembl.
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:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0090218; P:positive regulation of lipid kinase activity; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; 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; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 4.10.140.10; Thrombin light chain domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; PROTHROMBIN; 1.
DR PANTHER; PTHR24254:SF10; PROTHROMBIN; 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; PR00018; KRINGLE.
DR PRINTS; PR01505; PROTHROMBIN.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00130; KR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 315..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 314..315
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000269|PubMed:34265300"
FT SITE 363..364
FT /note="Cleavage; by factor Xa"
FT /evidence="ECO:0000269|PubMed:34265300"
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 MUTAGEN 314
FT /note="R->Q: Loss of cleavage by factor Xa."
FT /evidence="ECO:0000269|PubMed:34265300"
FT MUTAGEN 363
FT /note="R->Q: Loss of cleavage by factor Xa."
FT /evidence="ECO:0000269|PubMed:34265300"
FT MUTAGEN 568
FT /note="S->A: Loss of catalytic activity; no effect on
FT cleavage at R-198 by factor Xa."
FT /evidence="ECO:0000269|PubMed:34265300"
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
//
