(data stored in ACNUC19913 zone)

HOGENOM: RABITUN1197_PE2

ID   RABITUN1197_PE2                      STANDARD;      PRT;   494 AA.
AC   RABITUN1197_PE2; O19045;
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   Flags: Fragments;
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; (RABITUN1197.PE2).
GN   Name=F10;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABITUN1197.PE2.
CC       Oryctolagus cuniculus chromosome Un1197 oryCun2 full sequence 1..25213
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA10_RABIT
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 (By similarity).
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium (By
CC       similarity).
CC   -!- PTM: N- and O-glycosylated (By similarity).
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway)
CC       (By similarity).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains
CC       (By similarity).
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:Oryctolagus_cuniculus;ENSOCUG00000022738;ENSOCUT00000026250;ENSOCUP00000025032.
DR   EMBL; AF003200; - ;
DR   UniProtKB/Swiss-Prot; O19045; -.
DR   EMBL; AF003200; AAB62542.1; -; mRNA.
DR   RefSeq; NP_001075485.1; NM_001082016.1.
DR   UniGene; Ocu.2157; -.
DR   ProteinModelPortal; O19045; -.
DR   SMR; O19045; 42-86, 233-473.
DR   STRING; O19045; -.
DR   MEROPS; S01.216; -.
DR   Ensembl; ENSOCUT00000026250; ENSOCUP00000025032; ENSOCUG00000022738.
DR   GeneID; 100008647; -.
DR   CTD; 2159; -.
DR   eggNOG; maNOG10212; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   OrthoDB; EOG447FTB; -.
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; RABITUN1197.PE2; -.
KW   ENSOCUG00000022738820036002503210000011;
KW   FA10_RABIT; AF003200;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
SQ   SEQUENCE   494 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     TEGTGASVLR HTMANPLHLV LLGAALAGLL LSGSSVFISR RRANDVLART RRANSFLEEL
     KKGNLERECM EENCSYEEAL EVFEDREKTN EFWNKYVDGD QCESNPCQNQ GTCKDGLGMY
     TCSCVEGYEG QDCELFTRKL CSLDNGGCDQ FCKEEENSVL CSCASGYTLG DNGKSCISTE
     LFPCGKVTLG RWRRSPATNS SEGPPEAPGP EQQDDGNLTA TENPFNLLDS PEPPPEDDSS
     SLVRIVGGQD CRDGECPWQA LLVNEENEGF CGGTILSEYH VLTAAHCLHQ AKRFKVRVGD
     RDTEHEEGNE ETHEVEVVVK HNRFVKETYD FDIAVLRLKT PITFRRNVAP ACLPQKDWAE
     STLMAQKTGI VSGFGRTHEM GRLSTTLKML EVPYVDRNSC KLSSSFTITQ NMFCAGYDAR
     PEDACQGDSG GPHVTRFRDT YFVTGIVSWG EGCARKGKFG VYTKVSNFLK WIEKSMRARA
     VPVAEAAGTP GPTQ
//

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