(data stored in ACNUC19913 zone)

HOGENOM: RABITUN0002_4_PE1

ID   RABITUN0002_4_PE1                    STANDARD;      PRT;   462 AA.
AC   RABITUN0002_4_PE1; P16292;
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; (RABITUN0002_4.PE1).
GN   Name=F9;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABITUN0002_4.PE1.
CC       Oryctolagus cuniculus chromosome Un0002 oryCun2 partial sequence
CC       2764368..3764367 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_RABIT
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:Oryctolagus_cuniculus;ENSOCUG00000005240;ENSOCUT00000005236;ENSOCUP00000004537.
DR   EMBL; M26234; - ;
DR   UniProtKB/Swiss-Prot; P16292; -.
DR   EMBL; M26234; AAA31251.1; -; mRNA.
DR   PIR; I46712; I46712.
DR   UniGene; Ocu.1877; -.
DR   ProteinModelPortal; P16292; -.
DR   SMR; P16292; 49-275.
DR   STRING; P16292; -.
DR   MEROPS; S01.214; -.
DR   Ensembl; ENSOCUT00000005236; ENSOCUP00000004537; ENSOCUG00000005240.
DR   Ensembl; ENSOCUT00000026210; ENSOCUP00000019921; ENSOCUG00000005240.
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; RABITUN0002_4.PE1; -.
KW   ENSOCUG00000005240820036002503210000011;
KW   FA9_RABIT; Q9TRU3_RABIT; Q9TRU4_RABIT; Q9TRU5_RABIT; M26234;
KW   Blood coagulation; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease.
SQ   SEQUENCE   462 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQFLNTIMAE SPGLITICLL GYLLSAECTV FLDHENATKI LNRAKRYNSG KLEEFVSGNL
     ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGSCKD DINAYECWCQ
     YGFEGKNCEL DSTCSIKNGR CEQFCRKNRN NKIICSCTEG YRLAENQKSC EPAVPFPCGR
     VSVSHASKKI TRATTIFSNT EYENFTEAET IRGNVTQDAQ SSDDFTRIVG GENAKPGQFP
     WQVLLNGKVE AFCGGSIINE KWVVTAAHCI KPDDNITVVA GEYNIQETEN TEQKRNVIRI
     IPYHKYNATI NKYNHDIALL ELDKPLTLNS YVTPICIANR EYTNIFLNFG SGYVSGWGRV
     FNRGRQASIL QYLRVPFVDR ATCLRSTKFT IYNNMFCAGF DVGGKDSCEG DSGGPHVTEV
     EGTSFLTGII SWGEECAIKG KYGVYTRVSW YVNWIKEKTK LT
//

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