(data stored in ACNUC19913 zone)

HOGENOM: MOUSEX_PE709

ID   MOUSEX_PE709                         STANDARD;      PRT;   471 AA.
AC   MOUSEX_PE709; P16294; Q3UES1;
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 IX; EC=3.4.21 22;AltName: Full=Christmas
DE   factor;Contains: RecName: Full=Coagulation factor IXa light
DE   chain;Contains: RecName: Full=Coagulation factor IXa heavy chain;Flags:
DE   Precursor; (MOUSEX.PE709).
GN   Name=F9; Synonyms=Cf9;
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 MOUSEX.PE709.
CC       Mus musculus chromosome X NCBIM37  sequence 1..166650296 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_MOUSE
CC   -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
CC       participates in the intrinsic pathway of blood coagulation by
CC       converting factor X to its active form in the presence of Ca(2+)
CC       ions, phospholipids, and factor VIIIa.
CC   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
CC       X to form factor Xa.
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized primarily in the liver and
CC       secreted in plasma.
CC   -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
CC       residues and, with stronger affinity, to another site, beyond the
CC       Gla domain.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide.
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   -!- 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;ENSMUSG00000031138;ENSMUST00000033477;ENSMUSP00000033477.
DR   EMBL; AK149372; - ;
DR   EMBL; AL671984; - ;
DR   EMBL; BC125617; - ;
DR   EMBL; BC132393; - ;
DR   EMBL; CH466583; - ;
DR   EMBL; M23109; - ;
DR   EMBL; M26236; - ;
DR   UniProtKB/Swiss-Prot; P16294; Q3UES1; -.
DR   EMBL; AK149372; BAE28840.1; -; mRNA.
DR   EMBL; M23109; AAA37629.1; -; mRNA.
DR   EMBL; M26236; AAA37630.1; -; mRNA.
DR   IPI; IPI00348266; -.
DR   PIR; JQ0419; JQ0419.
DR   RefSeq; NP_032005.1; NM_007979.1.
DR   UniGene; Mm.391283; -.
DR   ProteinModelPortal; P16294; -.
DR   SMR; P16294; 47-192, 237-470.
DR   STRING; P16294; -.
DR   MEROPS; S01.214; -.
DR   PhosphoSite; P16294; -.
DR   PRIDE; P16294; -.
DR   Ensembl; ENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
DR   GeneID; 14071; -.
DR   KEGG; mmu:14071; -.
DR   NMPDR; fig|10090.3.peg.21591; -.
DR   CTD; 2158; -.
DR   MGI; MGI:88384; F9.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P16294; -.
DR   OMA; KYSHDIA; -.
DR   OrthoDB; EOG4THVTF; -.
DR   NextBio; 285068; -.
DR   ArrayExpress; P16294; -.
DR   Bgee; P16294; -.
DR   CleanEx; MM_F9; -.
DR   Genevestigator; P16294; -.
DR   GermOnline; ENSMUSG00000031138; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
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; MOUSEX.PE709; -.
KW   ENSMUSG000000311385old_1320000031; ENSMUSP000000334771old_1320000031;
KW   A0JLY3_MOUSE; A2AEU0_MOUSE; AK149372; AL671984; BC125617; BC132393;
KW   M23109; M26236;
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   Phosphoprotein; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Sulfation; Zymogen.
SQ   SEQUENCE   471 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG KLEEFVRGNL
     ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD DISSYECWCQ
     VGFEGRNCEL DATCNIKNGR CKQFCKNSPD NKVICSCTEG YQLAEDQKSC EPTVPFPCGR
     ASISYSSKKI TRAETVFSNM DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG
     ENAKPGQIPW QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT
     EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE YTNIFLKFGS
     GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI YNNMFCAGYR EGGKDSCEGD
     SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
//

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