ID Q5FVW1_XENTR Unreviewed; 607 AA. AC Q5FVW1; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 12-OCT-2022, entry version 142. DE RecName: Full=Prothrombin {ECO:0000256|ARBA:ARBA00014840, ECO:0000256|PIRNR:PIRNR001149}; DE EC=3.4.21.5 {ECO:0000256|ARBA:ARBA00012174, ECO:0000256|PIRNR:PIRNR001149}; DE AltName: Full=Coagulation factor II {ECO:0000256|ARBA:ARBA00032835, ECO:0000256|PIRNR:PIRNR001149}; GN Name=f2 {ECO:0000313|EMBL:AAH89747.1, GN ECO:0000313|Ensembl:ENSXETP00000060492, GN ECO:0000313|RefSeq:NP_001015797.1, GN ECO:0000313|Xenbase:XB-GENE-481539}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH89747.1}; RN [1] {ECO:0000313|RefSeq:NP_001015797.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12454917; DOI=10.1002/dvdy.10174; RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W., RA Richardson P.; RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus RT initiative."; RL Dev. Dyn. 225:384-391(2002). RN [2] {ECO:0000313|EMBL:AAH89747.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole body {ECO:0000313|EMBL:AAH89747.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSXETP00000060492} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000060492}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L., RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R., RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J., RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H., RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K., RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A., RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T., RA Khokha M.K., Richardson P.M., Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [4] {ECO:0000313|Ensembl:ENSXETP00000060492} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2020) to UniProtKB. RN [5] {ECO:0000313|RefSeq:NP_001015797.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) to UniProtKB. 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:0000256|ARBA:ARBA00025390, CC ECO:0000256|PIRNR:PIRNR001149}. 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 Evidence={ECO:0000256|ARBA:ARBA00001621, CC ECO:0000256|PIRNR:PIRNR001149}; CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|PIRNR:PIRNR001149}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC089747; AAH89747.1; -; mRNA. DR RefSeq; NP_001015797.1; NM_001015797.1. DR STRING; 8364.ENSXETP00000060492; -. DR MEROPS; S01.217; -. DR Ensembl; ENSXETT00000064408; ENSXETP00000060492; ENSXETG00000001982. DR GeneID; 548514; -. DR KEGG; xtr:548514; -. DR CTD; 2147; -. DR Xenbase; XB-GENE-481539; f2. DR OrthoDB; 1314811at2759; -. DR Proteomes; UP000008143; Chromosome 4. DR Bgee; ENSXETG00000001982; Expressed in liver and 10 other tissues. DR GO; GO:0005576; C:extracellular region; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd00108; KR; 2. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; -; 2. DR Gene3D; 2.40.20.10; -; 2. DR Gene3D; 4.10.140.10; -; 1. DR Gene3D; 4.10.740.10; -; 1. DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom. DR InterPro; IPR035972; GLA-like_dom_SF. DR InterPro; IPR000294; GLA_domain. DR InterPro; IPR000001; Kringle. DR InterPro; IPR013806; Kringle-like. DR InterPro; IPR018056; Kringle_CS. DR InterPro; IPR038178; Kringle_sf. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR003966; Prothrombin/thrombin. DR InterPro; IPR018992; Thrombin_light_chain. DR InterPro; IPR037111; Thrombin_light_chain_sf. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24254:SF10; PTHR24254:SF10; 1. DR Pfam; PF00594; Gla; 1. DR Pfam; PF00051; Kringle; 2. DR Pfam; PF09396; Thrombin_light; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001149; Thrombin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00001; GLABLOOD. DR PRINTS; PR01505; PROTHROMBIN. DR SMART; SM00069; GLA; 1. DR SMART; SM00130; KR; 2. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR SUPFAM; SSF57440; SSF57440; 2. DR SUPFAM; SSF57630; SSF57630; 1. DR PROSITE; PS00011; GLA_1; 1. DR PROSITE; PS50998; GLA_2; 1. DR PROSITE; PS00021; KRINGLE_1; 2. DR PROSITE; PS50070; KRINGLE_2; 2. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Acute phase {ECO:0000256|ARBA:ARBA00022486, ECO:0000256|PIRNR:PIRNR001149}; KW Blood coagulation {ECO:0000256|PIRNR:PIRNR001149}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR001149-4}; KW Hemostasis {ECO:0000256|PIRNR:PIRNR001149}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001149, ECO:0000256|RuleBase:RU363034}; KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE- KW ProRule:PRU00121}; KW Protease {ECO:0000256|PIRNR:PIRNR001149, ECO:0000256|RuleBase:RU363034}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Serine protease {ECO:0000256|PIRNR:PIRNR001149, KW ECO:0000256|RuleBase:RU363034}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..607 FT /note="Prothrombin" FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_001015797.1" FT /id="PRO_5033206171" FT DOMAIN 41..87 FT /note="Gla" FT /evidence="ECO:0000259|PROSITE:PS50998" FT DOMAIN 107..184 FT /note="Kringle" FT /evidence="ECO:0000259|PROSITE:PS50070" FT DOMAIN 207..285 FT /note="Kringle" FT /evidence="ECO:0000259|PROSITE:PS50070" FT DOMAIN 350..603 FT /note="Peptidase S1" FT /evidence="ECO:0000259|PROSITE:PS50240" FT ACT_SITE 392 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1" FT ACT_SITE 448 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1" FT ACT_SITE 553 FT /note="Charge relay system" FT /evidence="ECO:0000256|PIRSR:PIRSR001149-1" FT DISULFID 58..63 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 88..101 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 108..184 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 129..167 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 155..179 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 208..285 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4, FT ECO:0000256|PROSITE-ProRule:PRU00121" FT DISULFID 229..268 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4, FT ECO:0000256|PROSITE-ProRule:PRU00121" FT DISULFID 256..280 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 322..468 FT /note="Interchain (between light and heavy chains)" FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 377..393 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 521..535 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" FT DISULFID 549..579 FT /evidence="ECO:0000256|PIRSR:PIRSR001149-4" SQ SEQUENCE 607 AA; 69503 MW; 681C15339E41947A CRC64; MQPRDHIIGG LLLAATLSLV HCQNVFLNSK EAMSVLKRSR RANSYLEEIR QGNMERECIE EICSYEELRE IKESKVETDI FWAKYKDCEP EKKTRNDRED CLKGTSTCAE GTGTHYRGNV SVTRSGRECQ YWISNYPHKT KFNPTTNPSL VKNYCRNPND NPTGPWCYTK DPQKQWEECV IPLCGTNKTT VEPLIQKVPD QSVKKEPCER EFGLHYEGKL AVTISGLPCL PWDSPSVQQH SRKDFIKEVK LQENYCRNPD NDGEGLWCYV SHPNLTYDYC PMNYCDSPID EEVLNRPAGR TTTEEHQTFF DEKSFGSGEA VCGLRPLFEQ KSVEDKGEKE LLESYMQGRI VKGETAEPGS APWQVMLFKK SPQELLCGAS LLSDRWVLSA AHCIFYPPWD KNYTTDDILV RIGKHFRTKY ERATERIAQL ERIIVHPKYN WKENLDRDIA LIQLKRPVAF SNYIHPVCLP TKDTVVKLLA AGYKGRVTGW GNLQETWTSG AQNLPQALQQ INLPIVDQET CKSSTNIKVT DNMFCAGYNP EDSKRGDACE GDSGGPFVMK DPDTGRWVQL GIVSWGEGCD RDNKYGFYVH VHRMRKWIMK TVEKFGS //