ID   Q5FVW1_XENTR            Unreviewed;       607 AA.
AC   Q5FVW1;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   08-MAY-2019, entry version 127.
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:
CC       Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to
CC         form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
CC         Evidence={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}.
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DR   EMBL; BC089747; AAH89747.1; -; mRNA.
DR   RefSeq; NP_001015797.1; NM_001015797.1.
DR   MEROPS; S01.217; -.
DR   GeneID; 548514; -.
DR   KEGG; xtr:548514; -.
DR   CTD; 2147; -.
DR   Xenbase; XB-GENE-481539; f2.
DR   eggNOG; ENOG410IKPN; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251824; -.
DR   KO; K01313; -.
DR   OrthoDB; 1314811at2759; -.
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; cd00108; KR; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
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; 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|PIRNR:PIRNR001149};
KW   Blood coagulation {ECO:0000256|PIRNR:PIRNR001149};
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:SAAS00144621};
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
//