(data stored in ACNUC19913 zone)

HOGENOM: BOVIN12_87_PE4

ID   BOVIN12_87_PE4                       STANDARD;      PRT;   492 AA.
AC   BOVIN12_87_PE4; P00743;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Coagulation factor X; EC=3.4.21 6;AltName: Full=Stuart
DE   factor;Contains: RecName: Full=Factor X light chain;Contains: RecName:
DE   Full=Factor X heavy chain;Contains: RecName: Full=Activated factor Xa
DE   heavy chain;Flags: Precursor; (BOVIN12_87.PE4).
GN   Name=F10;
OS   BOS TAURUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BOVIN12_87.PE4.
CC       Bos taurus chromosome 12 Btau_4.0 partial sequence 84460455..85358539
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA10_BOVIN
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting.
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then
CC       Arg-|-Ile bonds in prothrombin to form thrombin.
CC   -!- SUBUNIT: The two chains are formed from a single-chain precursor
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: N- and O-glycosylated.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to
CC       another site, beyond the GLA domain.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Bos_taurus;ENSBTAG00000016385;ENSBTAT00000021789;ENSBTAP00000021789.
DR   EMBL; BC104607; - ;
DR   EMBL; X00673; - ;
DR   UniProtKB/Swiss-Prot; P00743; -.
DR   EMBL; X00673; CAA25286.1; -; mRNA.
DR   IPI; IPI00685993; -.
DR   PIR; A22867; EXBO.
DR   RefSeq; NP_001073682.1; NM_001080213.1.
DR   UniGene; Bt.13151; -.
DR   PDB; 1APO; NMR; -; A=85-126.
DR   PDB; 1CCF; NMR; -; A=85-126.
DR   PDB; 1IOD; X-ray; 2.30 A; G=41-84.
DR   PDB; 1KIG; X-ray; 3.00 A; H=234-474, L=129-179.
DR   PDB; 1WHE; NMR; -; A=41-126.
DR   PDB; 1WHF; NMR; -; A=41-126.
DR   PDBsum; 1APO; -.
DR   PDBsum; 1CCF; -.
DR   PDBsum; 1IOD; -.
DR   PDBsum; 1KIG; -.
DR   PDBsum; 1WHE; -.
DR   PDBsum; 1WHF; -.
DR   ProteinModelPortal; P00743; -.
DR   SMR; P00743; 42-126, 129-179, 234-474.
DR   STRING; P00743; -.
DR   MEROPS; S01.216; -.
DR   GlycoSuiteDB; P00743; -.
DR   PRIDE; P00743; -.
DR   Ensembl; ENSBTAT00000021789; ENSBTAP00000021789; ENSBTAG00000016385.
DR   GeneID; 280787; -.
DR   KEGG; bta:280787; -.
DR   CTD; 2159; -.
DR   eggNOG; maNOG12280; -.
DR   InParanoid; P00743; -.
DR   OMA; LIRICCT; -.
DR   OrthoDB; EOG447FTB; -.
DR   PhylomeDB; P00743; -.
DR   PMAP-CutDB; P00743; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   HOGENOMDNA; BOVIN12_87.PE4; -.
KW   ENSBTAG00000016385fold_1320000031; ENSBTAP00000021789fold_1320000031;
KW   Q3MHW2_BOVIN; BC104607; X00673;
KW   3D-structure; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal; Sulfation; Zymogen.
SQ   SEQUENCE   492 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ GNLERECLEE
     ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH CKDGIGDYTC TCAEGFEGKN
     CEFSTREICS LDNGGCDQFC REERSEVRCS CAHGYVLGDD SKSCVSTERF PCGKFTQGRS
     RRWAIHTSED ALDASELEHY DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC
     AEGECPWQAL LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
     AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA TLMTQKTGIV
     SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN MFCAGYDTQP EDACQGDSGG
     PHVTRFKDTY FVTGIVSWGE GCARKGKFGV YTKVSNFLKW IDKIMKARAG AAGSRGHSEA
     PATWTVPPPL PL
//

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