(data stored in ACNUC19913 zone)

HOGENOM: BOVINX_14_PE1

ID   BOVINX_14_PE1                        STANDARD;      PRT;   462 AA.
AC   BOVINX_14_PE1; P00741;
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; Fragment; (BOVINX_14.PE1).
GN   Name=F9;
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 BOVINX_14.PE1.
CC       Bos taurus chromosome X Btau_4.0 partial sequence 12956216..13956215
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_BOVIN
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   -!- 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;ENSBTAG00000004003;ENSBTAT00000005227;ENSBTAP00000005227.
DR   EMBL; AF394598; - ;
DR   EMBL; J00007; - ;
DR   UniProtKB/Swiss-Prot; P00741; -.
DR   EMBL; J00007; AAA30520.1; -; mRNA.
DR   IPI; IPI00905351; -.
DR   PIR; A14757; KFBO.
DR   UniGene; Bt.13106; -.
DR   PDB; 1J34; X-ray; 1.55 A; C=1-46.
DR   PDB; 1J35; X-ray; 1.80 A; C=1-46.
DR   PDBsum; 1J34; -.
DR   PDBsum; 1J35; -.
DR   ProteinModelPortal; P00741; -.
DR   SMR; P00741; 1-146, 182-416.
DR   STRING; P00741; -.
DR   MEROPS; S01.214; -.
DR   GlycoSuiteDB; P00741; -.
DR   PRIDE; P00741; -.
DR   eggNOG; maNOG10212; -.
DR   InParanoid; P00741; -.
DR   OrthoDB; EOG4THVTF; -.
DR   PMAP-CutDB; P00741; -.
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; BOVINX_14.PE1; -.
KW   ENSBTAG00000004003fold_1320000031; ENSBTAP00000005227fold_1320000031;
KW   Q95ME8_BOVIN; AF394598; J00007;
KW   3D-structure; Blood coagulation; Calcium; Complete proteome;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia; Hydrolase;
KW   Hydroxylation; Protease; Reference proteome; Secreted;
KW   Serine protease; Zymogen.
SQ   SEQUENCE   462 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MWCLNMIMAE SPGLVTICLL GYLLSAECTV FLDRENATKI LHRPKRYNSG KLEEFVRGNL
     ERECKEEKCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGMCKD DINSYECWCQ
     AGFEGTNCEL DATCSIKNGR CKQFCKRDTD NKVVCSCTDG YRLAEDQKSC EPAVPFPCGR
     VSVSHISKKL TRAETIFSNT NYENSSEAEI IWDNVTQSNQ SFDEFSRVVG GEDAERGQFP
     WQVLLHGEIA AFCGGSIVNE KWVVTAAHCI KPGVKITVVA GEHNTEKPEP TEQKRNVIRA
     IPYHSYNASI NKYSHDIALL ELDEPLELNS YVTPICIADR DYTNIFLKFG YGYVSGWGKV
     FNRGRSASIL QYLKVPLVDR ATCLRSTKFS IYSHMFCAGY HEGGKDSCQG DSGGPHVTEV
     EGTSFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT
//

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