(data stored in ACNUC19913 zone)

HOGENOM: CANFAX_115_PE1

ID   CANFAX_115_PE1                       STANDARD;      PRT;   459 AA.
AC   CANFAX_115_PE1; P19540;
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 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; (CANFAX_115.PE1).
GN   Name=F9;
OS   CANIS LUPUS FAMILIARIS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CANFAX_115.PE1.
CC       Canis familiaris chromosome X BROADD2 partial sequence 112370746..11336
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_CANFA
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   -!- DISEASE: Note=Defects in F9 are the cause of hemophilia B (HEMB).
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:Canis_familiaris;ENSCAFG00000018998;ENSCAFT00000030166;ENSCAFP00000028031.
DR   EMBL; M21757; - ;
DR   EMBL; M33826; - ;
DR   UniProtKB/Swiss-Prot; P19540; -.
DR   EMBL; M21757; AAA75006.1; -; mRNA.
DR   EMBL; M33826; AAA30844.1; -; mRNA.
DR   PIR; A30351; A30351.
DR   RefSeq; NP_001003323.1; NM_001003323.2.
DR   UniGene; Cfa.3857; -.
DR   ProteinModelPortal; P19540; -.
DR   SMR; P19540; 40-185, 218-452.
DR   STRING; P19540; -.
DR   MEROPS; S01.214; -.
DR   GeneID; 404015; -.
DR   KEGG; cfa:404015; -.
DR   CTD; 2158; -.
DR   eggNOG; maNOG10212; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P19540; -.
DR   OrthoDB; EOG4THVTF; -.
DR   PhylomeDB; P19540; -.
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; CANFAX_115.PE1; -.
KW   ENSCAFG00000018998fold_1320000031; ENSCAFP00000028031fold_1320000031;
KW   M21757; M33826;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disease mutation; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
SQ   SEQUENCE   459 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     RQRLNRIMAE ASGLVTVCLL GYLLSAECAV FLDRENATKI LSRPKRYNSG KLEEFVRGNL
     ERECIEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNDGVCKD DINSYECWCR
     AGFEGKNCEL DVTCNIKNGR CKQFCKLGPD NKVVCSCTTG YQLAEDQRSC EPAVPFPCGR
     VSVPHISMTR TRAETLFSNM DYENSTEVEK ILDNVTQPLN DFTRVVGGKD AKPGQFPWQV
     LLNGKVDAFC GGSIINEKWV VTAAHCIEPD VKITIVAGEH NTEKREHTEQ KRNVIRTILH
     HSYNATINKY NHDIALLELD EPLTLNSYVT PICIADREYS NIFLKFGSGY VSGWGRVFNK
     GRSASILQYL KVPLVDRATC LRSTKFTIYN NMFCAGFHEG GKDSCQGDSG GPHVTEVEGI
     SFLTGIISWG EECAMKGKYG IYTKVSRYVN WIKEKTKLT
//

If you have problems or comments...

PBIL Back to PBIL home page