(data stored in ACNUC19913 zone)

HOGENOM: PANTRX_140_PE2

ID   PANTRX_140_PE2                       STANDARD;      PRT;   433 AA.
AC   PANTRX_140_PE2; Q95ND7;
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; (PANTRX_140.PE2).
GN   Name=F9;
OS   PAN TROGLODYTES.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Pan.
OX   NCBI_TaxID=9598;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PANTRX_140.PE2.
CC       Pan troglodytes chromosome X CHIMP2.1 partial sequence 138747973..13974
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_PANTR
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 (By similarity).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
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 (By similarity).
CC   -!- PTM: Activated by factor XIa, which excises the activation peptide
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   -!- 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:Pan_troglodytes;ENSPTRG00000022330;ENSPTRT00000041650;ENSPTRP00000047240.
DR   EMBL; AB062470; - ;
DR   EMBL; AB062471; - ;
DR   UniProtKB/Swiss-Prot; Q95ND7; -.
DR   EMBL; AB062470; BAB58885.1; -; Genomic_DNA.
DR   RefSeq; NP_001129063.1; NM_001135591.1.
DR   UniGene; Ptr.6102; -.
DR   ProteinModelPortal; Q95ND7; -.
DR   SMR; Q95ND7; 47-191, 227-461.
DR   STRING; Q95ND7; -.
DR   MEROPS; S01.214; -.
DR   GeneID; 465887; -.
DR   KEGG; ptr:465887; -.
DR   CTD; 2158; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; Q95ND7; -.
DR   OrthoDB; EOG4THVTF; -.
DR   PMAP-CutDB; Q95ND7; -.
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; PANTRX_140.PE2; -.
KW   ENSPTRG00000022330-2caffold_90100000011;
KW   FA9_PANTR; Q8HZD4_PANTR; Q95ND6_PANTR; AB062470; AB062471;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid;
KW   Glycoprotein; Hydrolase; Hydroxylation; Phosphoprotein; Protease;
KW   Repeat; Secreted; Serine protease; Signal; Sulfation; Zymogen.
SQ   SEQUENCE   433 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     SVFLDHENAN KILNRPKRYN SGKLEEFVQG NLERECMEEK CSFEEAREVF ENTERTTEFW
     KQYVDGDQCE SNPCLNGGSC KDDINSYECW CPFGFEGKNC ELDVTCNIKN GRCEQFCKNS
     ADNKVVCSCT EGYRLAENQK SCEPAVPFPC GRVSVSQTSK LTRAETVFPD VDYVNSTEAE
     TILDNITQST QSFNDFTRVV GGEDAKPGQF PWQVVLNGKV DAFCGGSIVN EKWIVTAAHC
     VDTGVKITVV AGEHNIEETE HTEQKRNVIR IIPHHNYNAA INKYNHDIAL LELDEPLVLN
     SYVTPICIAD KEYTNIFLKF GSGYVSGWGR VFHKGRSALV LQYLRVPLVD RATCLRSTKF
     TIYNNMFCAG FHEGGRDSCQ GDSGGPHVTE VEGTSFLTGI ISWGEECAMK GKYGIYTKVS
     RYVNWIKEKT KLT
//

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