ID THRB_HUMAN Reviewed; 622 AA.
AC P00734; B2R7F7; B4E1A7; Q4QZ40; Q53H04; Q53H06; Q7Z7P3; Q9UCA1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 01-MAY-2013, entry version 186.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Wang Z.;
RT "Prothrombin Shanghai: hypoprothrombinaemia caused by substitution of
RT Gla29 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-622.
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.,
RA Tsugawa R., 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, 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 ENZYME REGULATION, AND HETERODIMER WITH SERPINA5.
RX PubMed=6323392;
RA Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.;
RT "Mechanism of inhibition of activated protein C by protein C
RT inhibitor.";
RL J. Biochem. 95:187-195(1984).
RN [12]
RP PROTEOLYTIC PROCESSING.
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
RT activation in human plasma.";
RL J. Biol. Chem. 261:13210-13215(1986).
RN [13]
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
RT modulate thrombin mitogenesis.";
RL Pept. Res. 1:65-73(1988).
RN [14]
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 [15]
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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121 AND ASN-143, AND MASS
RP SPECTROMETRY.
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 [17]
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
RT induce chemotaxis of human osteoblasts and microvascular endothelial
RT cells.";
RL J. Orthop. Res. 23:680-685(2005).
RN [18]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-143 AND ASN-416,
RP AND MASS SPECTROMETRY.
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.,
RA Moore R.J., 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 [19]
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
RT in a placebo-controlled phase I/II study.";
RL Wound Repair Regen. 15:23-34(2007).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, AND MASS
RP SPECTROMETRY.
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
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [21]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-416, CARBOHYDRATE
RP STRUCTURE, AND MASS SPECTROMETRY.
RC TISSUE=Cerebrospinal fluid;
RX PubMed=19838169; DOI=10.1038/nmeth.1392;
RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
RA Brinkmalm G., Larson G.;
RT "Enrichment of glycopeptides for glycan structure and attachment site
RT identification.";
RL Nat. Methods 6:809-811(2009).
RN [22]
RP GLYCOSYLATION AT ASN-121 AND ASN-143, STRUCTURE OF CARBOHYDRATES, AND
RP 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
RT N-and O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2583108;
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:
RT interaction with D-Phe-Pro-Arg chloromethylketone and significance of
RT the Tyr-Pro-Pro-Trp insertion segment.";
RL EMBO J. 8:3467-3475(1989).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH HIRUDIN.
RX PubMed=2369893;
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
RT serine protease inhibition.";
RL EMBO J. 9:2361-2365(1990).
RN [25]
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.,
RA Roitsch C., 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 [26]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 328-622 IN COMPLEXES WITH
RP HIRUDIN AND SYNTHETIC INHIBITOR.
RX PubMed=8251938;
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 [27]
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 [28]
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
RT rearrangements: implications for the interaction with antithrombin and
RT thrombomodulin.";
RL EMBO J. 16:2977-2984(1997).
RN [29]
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 [30]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 333-621 IN COMPLEX WITH
RP SYNTHETIC 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
RT proceeds via a metastable pentacoordinated phosphorus intermediate.";
RL J. Mol. Biol. 311:549-555(2001).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 334-620 IN COMPLEX WITH
RP HIRUDIN AND SYNTHETIC INHIBITOR.
RX PubMed=16763681; DOI=10.1039/b602585d;
RA Schweizer E., Hoffmann-Roeder A., Olsen J.A., Seiler P.,
RA Obst-Sander U., Wagner B., Kansy M., Banner D.W., Diederich F.;
RT "Multipolar interactions in the D pocket of thrombin: large
RT differences between tricyclic imide and lactam inhibitors.";
RL Org. Biomol. Chem. 4:2364-2375(2006).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 334-621 IN COMPLEX WITH
RP 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
RT thrombin.";
RL J. Am. Chem. Soc. 129:10648-10649(2007).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 335-621 IN COMPLEX WITH
RP SYNTHETIC 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.,
RA Naylor-Olsen A.M., McMasters D.R., Krueger J.A., Lewis S.D.,
RA Lucas B.J., Kuo L.C., Yan Y., 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 [34]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 315-622 IN COMPLEX WITH
RP SERPINA5 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
RT revealed by the 1.6-A structure of the heparin-bridged complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:4661-4666(2008).
RN [35]
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
RT type 3 (157 Glu leads to Lys) and the localization of a third thrombin
RT cleavage site.";
RL Br. J. Haematol. 54:245-254(1983).
RN [36]
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
RT for arginine at residue 273.";
RL J. Biol. Chem. 261:15045-15048(1986).
RN [37]
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.,
RA Iwanaga S.;
RT "Prothrombin Tokushima, a replacement of arginine-418 by tryptophan
RT that impairs the fibrinogen clotting activity of derived thrombin
RT Tokushima.";
RL Biochemistry 26:1117-1122(1987).
RN [38]
RP VARIANT FA2D TRP-461.
RX PubMed=3801671;
RA Inomoto T., Shirakami A., Kawauchi S., Shigekiyo T., Saito S.,
RA Miyoshi K., Morita T., Iwanaga S.;
RT "Prothrombin Tokushima: characterization of dysfunctional thrombin
RT derived from a variant of human prothrombin.";
RL Blood 69:565-569(1987).
RN [39]
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 [40]
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 [41]
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.,
RA Iwanaga S.;
RT "Prothrombin Salakta: substitution of glutamic acid-466 by alanine
RT reduces the fibrinogen clotting activity and the esterase activity.";
RL Biochemistry 31:7457-7462(1992).
RN [42]
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 [43]
RP VARIANT FA2D TRP-461.
RX PubMed=1349838;
RA Iwahana H., Yoshimoto K., Shigekiyo T., Shirakami A., Saito S.,
RA 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 [44]
RP VARIANT FA2D HIS-314.
RX PubMed=7865694;
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 [45]
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 [46]
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
RT of human genes.";
RL Nat. Genet. 22:231-238(1999).
RN [47]
RP ERRATUM.
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 [48]
RP VARIANTS MET-165; LYS-200; THR-386 AND GLN-532, AND MASS 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.,
RA Lin X., 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,
CC converts fibrinogen to fibrin and activates factors V, VII, VIII,
CC XIII, and, in complex with thrombomodulin, protein C. Functions in
CC blood homeostasis, inflammation and wound healing.
CC -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in
CC fibrinogen to form fibrin and release fibrinopeptides A and B.
CC -!- ENZYME REGULATION: Inhibited by SERPINA5.
CC -!- SUBUNIT: Heterodimer (named alpha-thrombin) of a light and a heavy
CC chain; disulfide-linked. Forms a heterodimer with SERPINA5.
CC -!- INTERACTION:
CC Q846V4:- (xeno); NbExp=5; IntAct=EBI-297094, EBI-989571;
CC P07204:THBD; NbExp=4; IntAct=EBI-297094, EBI-941422;
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
CC are necessary for the calcium-dependent interaction with a
CC negatively charged phospholipid surface, which is essential for
CC the conversion of prothrombin to thrombin.
CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-121:
CC Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).
CC At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major).
CC -!- DISEASE: Factor II deficiency (FA2D) [MIM:613679]: A very rare
CC blood coagulation disorder characterized by mucocutaneous bleeding
CC symptoms. The severity of the bleeding manifestations correlates
CC with blood factor II levels. Note=The disease is caused by
CC mutations affecting the gene represented in this entry.
CC -!- DISEASE: Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an
CC acute neurologic event leading to death of neural tissue of the
CC brain and resulting in loss of motor, sensory and/or cognitive
CC function. Ischemic strokes, resulting from vascular occlusion, is
CC considered to be a highly complex disease consisting of a group of
CC heterogeneous disorders with multiple genetic and environmental
CC risk factors. Note=Disease susceptibility is associated with
CC variations affecting the gene represented in this entry.
CC -!- DISEASE: Thrombophilia due to thrombin defect (THPH1)
CC [MIM:188050]: A multifactorial disorder of hemostasis
CC characterized by abnormal platelet aggregation in response to
CC various agents and recurrent thrombi formation. Note=The disease
CC is caused by mutations affecting the gene represented in this
CC entry. A common genetic variation in the 3-prime untranslated
CC region of the prothrombin gene is associated with elevated plasma
CC prothrombin levels and an increased risk of venous thrombosis.
CC -!- DISEASE: Pregnancy loss, recurrent, 2 (RPRGL2) [MIM:614390]: A
CC common complication of pregnancy, resulting in spontaneous
CC abortion before the fetus has reached viability. The term includes
CC all miscarriages from the time of conception until 24 weeks of
CC gestation. Recurrent pregnancy loss is defined as 3 or more
CC consecutive spontaneous abortions. Note=Disease susceptibility is
CC associated with variations affecting the gene represented in this
CC entry.
CC -!- PHARMACEUTICAL: The peptide TP508 also known as Chrysalin
CC (Orthologic) could be used to accelerate repair of both soft and
CC 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
CC the activation peptide and cleaves the remaining part into light
CC and heavy chains. The activation process starts slowly because
CC factor V itself has to be activated by the initial, small amounts
CC 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
CC Xa.
CC -!- MISCELLANEOUS: The cleavage after Arg-198, observed in vitro, does
CC not occur in plasma.
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC -!- SIMILARITY: Contains 2 kringle domains.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Thrombin entry;
CC URL="http://en.wikipedia.org/wiki/Thrombin";
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/F2";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/f2/";
CC -----------------------------------------------------------------------
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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 IPI; IPI00019568; -.
DR PIR; A29351; TBHU.
DR RefSeq; NP_000497.1; NM_000506.3.
DR UniGene; Hs.655207; -.
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=331-360, 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=328-363.
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=364-620.
DR PDB; 1EB1; X-ray; 1.80 A; H=364-620, L=334-360.
DR PDB; 1EOJ; X-ray; 2.10 A; A=334-620.
DR PDB; 1EOL; X-ray; 2.10 A; A=334-620.
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=336-622.
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=328-363.
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=334-360.
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=328-363.
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=328-363.
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=328-363.
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=328-363, B=364-622.
DR PDB; 1THR; X-ray; 2.30 A; H=364-622, L=328-363.
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=364-622, L=333-360.
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=334-361, 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=336-621.
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=334-363, 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=328-363, B=364-622.
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=328-363, 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=328-363, 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=318-363, 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; 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=364-622, 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; 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; 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; 4HFY; X-ray; 3.00 A; A/B=333-622.
DR PDB; 4HTC; X-ray; 2.30 A; H=364-622, L=328-363.
DR PDB; 4THN; X-ray; 2.50 A; H=364-622, L=328-363.
DR PDB; 5GDS; X-ray; 2.10 A; H=364-622, L=328-363.
DR PDB; 7KME; X-ray; 2.10 A; H=364-622, L=328-363.
DR PDB; 8KME; X-ray; 2.10 A; 1=328-363, 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; 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; 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; 4HFY; -.
DR PDBsum; 4HTC; -.
DR PDBsum; 4THN; -.
DR PDBsum; 5GDS; -.
DR PDBsum; 7KME; -.
DR PDBsum; 8KME; -.
DR ProteinModelPortal; P00734; -.
DR DIP; DIP-6115N; -.
DR IntAct; P00734; 7.
DR STRING; 9606.ENSP00000308541; -.
DR MEROPS; S01.217; -.
DR GlycoSuiteDB; P00734; -.
DR PhosphoSite; P00734; -.
DR DMDM; 135807; -.
DR SWISS-2DPAGE; P00734; -.
DR PaxDb; P00734; -.
DR PeptideAtlas; P00734; -.
DR PRIDE; P00734; -.
DR DNASU; 2147; -.
DR Ensembl; ENST00000311907; ENSP00000308541; ENSG00000180210.
DR GeneID; 2147; -.
DR KEGG; hsa:2147; -.
DR UCSC; uc001ndf.4; human.
DR CTD; 2147; -.
DR GeneCards; GC11P046740; -.
DR H-InvDB; HIX0026188; -.
DR HGNC; HGNC:3535; F2.
DR HPA; CAB016780; -.
DR HPA; CAB018650; -.
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 Orphanet; 325; Congenital factor II deficiency.
DR Orphanet; 64738; Non rare thrombophilia.
DR PharmGKB; PA157; -.
DR eggNOG; COG5640; -.
DR HOVERGEN; HBG108381; -.
DR InParanoid; P00734; -.
DR KO; K01313; -.
DR OMA; ECQLWRS; -.
DR OrthoDB; EOG4MPHPV; -.
DR Pathway_Interaction_DB; angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
DR Pathway_Interaction_DB; hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.
DR Pathway_Interaction_DB; syndecan_4_pathway; Syndecan-4-mediated signaling events.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_604; Hemostasis.
DR SABIO-RK; P00734; -.
DR BindingDB; P00734; -.
DR ChEMBL; CHEMBL204; -.
DR DrugBank; DB00025; Antihemophilic Factor.
DR DrugBank; DB00278; Argatroban.
DR DrugBank; DB00006; Bivalirudin.
DR DrugBank; DB00100; Coagulation Factor IX.
DR DrugBank; DB00055; Drotrecogin alfa.
DR DrugBank; DB01225; Enoxaparin.
DR DrugBank; DB01109; Heparin.
DR DrugBank; DB00001; Lepirudin.
DR DrugBank; DB00170; Menadione.
DR DrugBank; DB01123; Proflavine.
DR DrugBank; DB00641; Simvastatin.
DR DrugBank; DB04786; Suramin.
DR DrugBank; DB00682; Warfarin.
DR DrugBank; DB04898; Ximelagatran.
DR EvolutionaryTrace; P00734; -.
DR GenomeRNAi; 2147; -.
DR NextBio; 8681; -.
DR PMAP-CutDB; P00734; -.
DR ArrayExpress; P00734; -.
DR Bgee; P00734; -.
DR CleanEx; HS_F2; -.
DR Genevestigator; P00734; -.
DR GermOnline; ENSG00000180210; Homo sapiens.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
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:0004252; F:serine-type endopeptidase activity; IDA: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:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051480; P:cytosolic calcium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0042730; P:fibrinolysis; IDA:UniProtKB.
DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:BHF-UCL.
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:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR GO; GO:0030168; P:platelet activation; IDA:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Compara.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IEA:Compara.
DR GO; GO:1900738; P:positive regulation of phospholipase C-activating G-protein coupled receptor signaling pathway; 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:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR GO; GO:0006508; P:proteolysis; TAS:Reactome.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Compara.
DR Gene3D; 2.40.20.10; -; 2.
DR Gene3D; 4.10.140.10; -; 1.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR003966; Prothrombin/thrombin.
DR InterPro; IPR018992; Thrombin_light_chain.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
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; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR SUPFAM; SSF57630; VitK_dep_GLA; 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; Complete proteome;
KW Direct protein sequencing; Disease mutation; Disulfide bond;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW Kringle; Pharmaceutical; Polymorphism; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Thrombophilia; Zymogen.
FT SIGNAL 1 24 Potential.
FT PROPEP 25 43
FT /FTId=PRO_0000028159.
FT CHAIN 44 622 Prothrombin.
FT /FTId=PRO_0000028160.
FT PEPTIDE 44 198 Activation peptide fragment 1.
FT /FTId=PRO_0000028161.
FT PEPTIDE 199 327 Activation peptide fragment 2.
FT /FTId=PRO_0000028162.
FT CHAIN 328 363 Thrombin light chain.
FT /FTId=PRO_0000028163.
FT CHAIN 364 622 Thrombin heavy chain.
FT /FTId=PRO_0000028164.
FT DOMAIN 44 89 Gla.
FT DOMAIN 108 186 Kringle 1.
FT DOMAIN 213 291 Kringle 2.
FT DOMAIN 364 618 Peptidase S1.
FT REGION 551 573 High affinity receptor-binding region
FT which is also known as the TP508 peptide.
FT ACT_SITE 406 406 Charge relay system.
FT ACT_SITE 462 462 Charge relay system.
FT ACT_SITE 568 568 Charge relay system.
FT SITE 198 199 Cleavage; by thrombin.
FT SITE 327 328 Cleavage; by factor Xa.
FT SITE 363 364 Cleavage; by factor Xa.
FT MOD_RES 49 49 4-carboxyglutamate.
FT MOD_RES 50 50 4-carboxyglutamate.
FT MOD_RES 57 57 4-carboxyglutamate.
FT MOD_RES 59 59 4-carboxyglutamate.
FT MOD_RES 62 62 4-carboxyglutamate.
FT MOD_RES 63 63 4-carboxyglutamate.
FT MOD_RES 68 68 4-carboxyglutamate.
FT MOD_RES 69 69 4-carboxyglutamate.
FT MOD_RES 72 72 4-carboxyglutamate.
FT MOD_RES 75 75 4-carboxyglutamate.
FT CARBOHYD 121 121 N-linked (GlcNAc...) (complex).
FT CARBOHYD 143 143 N-linked (GlcNAc...) (complex).
FT CARBOHYD 416 416 N-linked (GlcNAc...) (complex).
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 Interchain (between light and heavy
FT chains).
FT DISULFID 391 407
FT DISULFID 536 550 By similarity.
FT DISULFID 564 594 By similarity.
FT VARIANT 72 72 E -> G (in FA2D; Shanghai).
FT /FTId=VAR_055232.
FT VARIANT 165 165 T -> M (polymorphism confirmed at protein
FT level; dbSNP:rs5896).
FT /FTId=VAR_011781.
FT VARIANT 200 200 E -> K (in FA2D; prothrombin type 3;
FT variant confirmed at protein level).
FT /FTId=VAR_006711.
FT VARIANT 314 314 R -> C (in FA2D; Barcelona/Madrid).
FT /FTId=VAR_006712.
FT VARIANT 314 314 R -> H (in FA2D; Padua-1).
FT /FTId=VAR_006713.
FT VARIANT 380 380 M -> T (in FA2D; Himi-1).
FT /FTId=VAR_006714.
FT VARIANT 386 386 P -> T (polymorphism confirmed at protein
FT level; dbSNP:rs5897).
FT /FTId=VAR_011782.
FT VARIANT 425 425 R -> C (in FA2D; Quick-1).
FT /FTId=VAR_006715.
FT VARIANT 431 431 R -> H (in FA2D; Himi-2).
FT /FTId=VAR_006716.
FT VARIANT 461 461 R -> W (in FA2D; Tokushima).
FT /FTId=VAR_006717.
FT VARIANT 509 509 E -> A (in FA2D; Salakta/Frankfurt).
FT /FTId=VAR_006718.
FT VARIANT 532 532 E -> Q (polymorphism confirmed at protein
FT level).
FT /FTId=VAR_068913.
FT VARIANT 601 601 G -> V (in FA2D; Quick-2).
FT /FTId=VAR_006719.
FT CONFLICT 9 25 Missing (in Ref. 3; BAG64719).
FT CONFLICT 66 66 S -> N (in Ref. 4; BAD96497).
FT CONFLICT 119 119 H -> N (in Ref. 9; AA sequence).
FT CONFLICT 121 121 N -> S (in Ref. 9; AA sequence).
FT CONFLICT 164 164 T -> I (in Ref. 9; AA sequence).
FT CONFLICT 164 164 T -> N (in Ref. 7; CAA23842).
FT CONFLICT 176 176 V -> A (in Ref. 9; AA sequence).
FT CONFLICT 183 183 I -> T (in Ref. 9; AA sequence).
FT CONFLICT 194 195 AM -> MV (in Ref. 9; AA sequence).
FT CONFLICT 308 308 D -> DEE (in Ref. 9; AA sequence).
FT CONFLICT 335 335 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 337 337 G -> R (in Ref. 4; BAD96495).
FT CONFLICT 349 349 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 369 369 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 398 398 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 414 414 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 485 485 D -> N (in Ref. 10; AA sequence).
FT CONFLICT 494 494 Q -> G (in Ref. 10; AA sequence).
FT CONFLICT 504 504 W -> Y (in Ref. 10; AA sequence).
FT CONFLICT 509 509 E -> S (in Ref. 10; AA sequence).
FT CONFLICT 511 511 W -> V (in Ref. 10; AA sequence).
FT CONFLICT 514 514 N -> D (in Ref. 10; AA sequence).
FT CONFLICT 529 530 PI -> AL (in Ref. 10; AA sequence).
FT HELIX 216 218
FT HELIX 240 243
FT STRAND 244 246
FT STRAND 273 279
FT STRAND 283 285
FT HELIX 326 329
FT TURN 334 337
FT TURN 340 342
FT HELIX 343 345
FT HELIX 352 358
FT STRAND 367 369
FT STRAND 378 383
FT TURN 384 387
FT STRAND 388 395
FT STRAND 397 403
FT HELIX 405 407
FT HELIX 411 413
FT HELIX 419 421
FT STRAND 422 427
FT STRAND 430 433
FT TURN 436 438
FT STRAND 440 449
FT TURN 455 458
FT STRAND 464 470
FT HELIX 486 492
FT STRAND 498 505
FT HELIX 506 511
FT HELIX 513 515
FT STRAND 524 530
FT HELIX 533 538
FT STRAND 540 542
FT STRAND 548 551
FT HELIX 555 557
FT HELIX 563 565
FT STRAND 571 575
FT TURN 577 579
FT STRAND 582 590
FT STRAND 592 595
FT STRAND 601 605
FT HELIX 607 609
FT HELIX 610 618
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
//
