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}.
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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
//