ID Q5FVW1_XENTR Unreviewed; 607 AA. AC Q5FVW1; DT 01-MAR-2005, integrated into UniProtKB/TrEMBL. DT 01-MAR-2005, sequence version 1. DT 27-SEP-2017, entry version 119. DE RecName: Full=Prothrombin {ECO:0000256|PIRNR:PIRNR001149}; DE EC=3.4.21.5 {ECO:0000256|PIRNR:PIRNR001149}; DE AltName: Full=Coagulation factor II {ECO:0000256|PIRNR:PIRNR001149}; GN Name=f2 {ECO:0000313|EMBL:AAH89747.1, GN ECO:0000313|Xenbase:XB-GENE-481539}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH89747.1}; RN [1] {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. 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 {ECO:0000256|PIRNR:PIRNR001149}. CC -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in CC fibrinogen to form fibrin and release fibrinopeptides A and B. CC {ECO:0000256|PIRNR:PIRNR001149}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000256|PIRNR:PIRNR001149, ECO:0000256|SAAS:SAAS00559343}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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 UniGene; Str.8528; -. DR ProteinModelPortal; Q5FVW1; -. DR MEROPS; S01.217; -. DR PaxDb; Q5FVW1; -. DR GeneID; 548514; -. DR CTD; 2147; -. DR Xenbase; XB-GENE-481539; f2. DR eggNOG; ENOG410IKPN; Eukaryota. DR eggNOG; COG5640; LUCA. DR HOGENOM; HOG000251824; -. DR HOVERGEN; HBG108381; -. 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:InterPro. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. DR CDD; cd00190; Tryp_SPc; 1. 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; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR003966; Prothrombin/thrombin. DR InterPro; IPR018992; Thrombin_light_chain. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24254:SF13; PTHR24254:SF13; 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|PIRNR:PIRNR001149}; KW Blood coagulation {ECO:0000256|PIRNR:PIRNR001149}; KW Calcium {ECO:0000256|SAAS:SAAS00738281}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001149-4, ECO:0000256|PROSITE- KW ProRule:PRU00121, ECO:0000256|SAAS:SAAS00037407}; KW Hemostasis {ECO:0000256|PIRNR:PIRNR001149}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001149, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745942}; KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121, KW ECO:0000256|SAAS:SAAS00045973}; KW Protease {ECO:0000256|PIRNR:PIRNR001149, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745964}; KW Serine protease {ECO:0000256|PIRNR:PIRNR001149, KW ECO:0000256|RuleBase:RU363034, ECO:0000256|SAAS:SAAS00745848}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 607 Prothrombin. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004255933. FT DOMAIN 41 87 Gla. {ECO:0000259|PROSITE:PS50998}. FT DOMAIN 107 184 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 207 285 Kringle. {ECO:0000259|PROSITE:PS50070}. FT DOMAIN 350 603 Peptidase S1. {ECO:0000259|PROSITE: FT PS50240}. FT ACT_SITE 392 392 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001149-1}. FT ACT_SITE 448 448 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001149-1}. FT ACT_SITE 553 553 Charge relay system. {ECO:0000256|PIRSR: FT PIRSR001149-1}. FT DISULFID 58 63 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 88 101 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 108 184 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 129 167 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 155 179 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 208 285 {ECO:0000256|PIRSR:PIRSR001149-4, FT ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 229 268 {ECO:0000256|PIRSR:PIRSR001149-4, FT ECO:0000256|PROSITE-ProRule:PRU00121}. FT DISULFID 256 280 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 322 468 Interchain (between light and heavy FT chains). {ECO:0000256|PIRSR:PIRSR001149- FT 4}. FT DISULFID 377 393 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 521 535 {ECO:0000256|PIRSR:PIRSR001149-4}. FT DISULFID 549 579 {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 //