(data stored in ACNUC19913 zone)

HOGENOM: CAVPO79_3_PE6

ID   CAVPO79_3_PE6                        STANDARD;      PRT;   472 AA.
AC   CAVPO79_3_PE6; P16295;
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;Flags: Fragment; (CAVPO79_3.PE6).
GN   Name=F9;
OS   CAVIA PORCELLUS.
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; Hystricognathi; Caviidae; Cavia.
OX   NCBI_TaxID=10141;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAVPO79_3.PE6.
CC       Cavia porcellus scaffold scaffold_79 cavPor3 partial sequence
CC       2000001..3000000 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_CAVPO
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   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Cavia_porcellus;ENSCPOG00000025563;ENSCPOT00000020110;ENSCPOP00000016267.
DR   EMBL; M26237; - ;
DR   UniProtKB/Swiss-Prot; P16295; -.
DR   EMBL; M26237; AAA37037.1; -; mRNA.
DR   PIR; I48144; I48144.
DR   ProteinModelPortal; P16295; -.
DR   SMR; P16295; 59-285.
DR   MEROPS; S01.214; -.
DR   Ensembl; ENSCPOT00000020110; ENSCPOP00000016267; ENSCPOG00000025563.
DR   Ensembl; ENSCPOT00000026462; ENSCPOP00000018277; ENSCPOG00000025563.
DR   eggNOG; roNOG11613; -.
DR   GeneTree; ENSGT00560000076714; -.
DR   InParanoid; P16295; -.
DR   OrthoDB; EOG4THVTF; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
DR   HOGENOMDNA; CAVPO79_3.PE6; -.
KW   ENSCPOG00000025563fold_1320000031; ENSCPOP00000016267fold_1320000031;
KW   M26237;
KW   Blood coagulation; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease.
SQ   SEQUENCE   472 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     TQLLNMIMAE SWGLITIYLF GYLLNAECTV FLDHENATKI LNRPKRFNSG KLEEFIRGNL
     ERECLEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD SIDAYECWCQ
     LGFEGRNCEL DASCNIKNGR CKQFCKTDAK NKVICSCTEG YQLAEDQKSC EPAVPFPCGR
     VSIPSVSKEH NRANAIFSRM GYVNFTDDET IWDDNDDDET IWDNSTESTK PSDEFFRVVG
     GEDAKPGQFP WQVLLNGETE AFCGGSIVNE KWIVTAAHCI LPGIKIEVVA GKHNIEKKED
     TEQRRNVTQI ILHHSYNASF NKYSHDIALL ELDKPLSLNS YVTPICIANR EYTNIFLKFG
     AGYVSGWGKL FSQGRTASIL QYLRVPLVDR ATCLRSTKFT IYNNMFCAGF HEGGRDSCQG
     DSGGPHVTEV EGTNFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKQKTK LT
//

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