(data stored in ACNUC19913 zone)

HOGENOM: MOUSE8_PE164

ID   MOUSE8_PE164                         STANDARD;      PRT;   481 AA.
AC   MOUSE8_PE164; O88947; O54740; Q99L32;
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; (MOUSE8.PE164).
GN   Name=F10;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE8.PE164.
CC       Mus musculus chromosome 8 NCBIM37  sequence 1..131738871 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA10_MOUSE
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma; synthesized in the liver.
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 (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   -!- 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:Mus_musculus;ENSMUSG00000031444;ENSMUST00000063820;ENSMUSP00000068389.
DR   EMBL; AC127308; - ;
DR   EMBL; AF087644; - ;
DR   EMBL; AF211347; - ;
DR   EMBL; AJ222677; - ;
DR   EMBL; AK154100; - ;
DR   EMBL; AK171096; - ;
DR   EMBL; BC003877; - ;
DR   EMBL; CH466566; - ;
DR   EMBL; CT010325; - ;
DR   UniProtKB/Swiss-Prot; O88947; O54740; Q99L32; -.
DR   EMBL; AF087644; AAC36345.1; -; mRNA.
DR   EMBL; AJ222677; CAA10933.1; -; mRNA.
DR   EMBL; AF211347; AAF22980.1; -; Genomic_DNA.
DR   EMBL; BC003877; AAH03877.1; -; mRNA.
DR   IPI; IPI00331551; -.
DR   RefSeq; NP_031998.3; NM_007972.4.
DR   UniGene; Mm.262589; -.
DR   ProteinModelPortal; O88947; -.
DR   SMR; O88947; 41-464.
DR   IntAct; O88947; 2.
DR   STRING; O88947; -.
DR   MEROPS; S01.216; -.
DR   PRIDE; O88947; -.
DR   Ensembl; ENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
DR   GeneID; 14058; -.
DR   KEGG; mmu:14058; -.
DR   CTD; 2159; -.
DR   MGI; MGI:103107; F10.
DR   eggNOG; roNOG11613; -.
DR   InParanoid; O88947; -.
DR   OMA; PACLPQK; -.
DR   PhylomeDB; O88947; -.
DR   NextBio; 285020; -.
DR   ArrayExpress; O88947; -.
DR   Bgee; O88947; -.
DR   CleanEx; MM_F10; -.
DR   Genevestigator; O88947; -.
DR   GermOnline; ENSMUSG00000031444; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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; MOUSE8.PE164; -.
KW   ENSMUSG000000314445old_1320000031; ENSMUSP000000683891old_1320000031;
KW   D3Z7R3_MOUSE; Q3TBR2_MOUSE; Q4FJS7_MOUSE; AC127308; AF087644; AF211347;
KW   AK154100; AK171096; BC003877; CH466566; CT010325;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW   Signal; Zymogen.
SQ   SEQUENCE   481 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK GNLERECMEE
     ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA CRDGIGGYTC TCSEGFEGKN
     CELFVRKLCR LDNGDCDQFC REEQNSVVCS CASGYFLGND GKSCISTAPF PCGKITTGRR
     KRSVALNTSD SELDLEDALL DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD
     GECPWQALLI NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH
     EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL MTQKTGIVSG
     FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF CAGYEAKLED ACQGDSGGPH
     VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT KVTTFLKWID RSMKARVGPT AETPRTAGPP
     N
//

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