ID   Q5FVW1_XENTR            Unreviewed;       607 AA.
AC   Q5FVW1;
DT   01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2005, sequence version 1.
DT   14-MAY-2014, entry version 87.
DE   RecName: Full=Prothrombin;
DE            EC=3.4.21.5;
DE   AltName: Full=Coagulation factor II;
GN   Name=f2;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole body;
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Gly bonds in
CC       fibrinogen to form fibrin and release fibrinopeptides A and B.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains peptidase S1 domain.
CC   -!- SIMILARITY: Contains peptidase Sdomain.
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DR   EMBL; BC089747; AAH89747.1; -; mRNA.
DR   RefSeq; NP_001015797.1; NM_001015797.1.
DR   UniGene; Str.8528; -.
DR   ProteinModelPortal; Q5FVW1; -.
DR   SMR; Q5FVW1; 314-606.
DR   STRING; 8364.ENSXETP00000004244; -.
DR   MEROPS; S01.217; -.
DR   GeneID; 548514; -.
DR   KEGG; xtr:548514; -.
DR   CTD; 2147; -.
DR   Xenbase; XB-GENE-481539; f2.
DR   eggNOG; COG5640; -.
DR   HOGENOM; HOG000251824; -.
DR   HOVERGEN; HBG108381; -.
DR   InParanoid; Q5FVW1; -.
DR   KO; K01313; -.
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:0007596; P:blood coagulation; IEA:InterPro.
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; 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; Blood coagulation; Calcium; Disulfide bond; Hemostasis;
KW   Hydrolase; Kringle; Protease; Serine protease.
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
//