ID   FA9_RAT                 Reviewed;         282 AA.
AC   P16296;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   16-JUN-2009, entry version 81.
DE   RecName: Full=Coagulation factor IX;
DE            EC=3.4.21.22;
DE   AltName: Full=Christmas factor;
DE   Flags: Fragment;
GN   Name=F9; Synonyms=Cf9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90152675; PubMed=2303254; DOI=10.1016/0888-7543(90)90458-7;
RA   Sarkar G., Koeberl D.D., Sommer S.S.;
RT   "Direct sequencing of the activation peptide and the catalytic domain
RT   of the factor IX gene in six species.";
RL   Genomics 6:133-143(1990).
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.
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DR   EMBL; M26247; AAA41162.1; -; mRNA.
DR   IPI; IPI00765267; -.
DR   PIR; I84621; I84621.
DR   UniGene; Rn.214249; -.
DR   HSSP; P00740; 1RFN.
DR   SMR; P16296; 56-282.
DR   PRIDE; P16296; -.
DR   RGD; 2589; F9.
DR   HOVERGEN; P16296; -.
DR   BRENDA; 3.4.21.22; 248.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Disulfide bond; Glycoprotein; Hydrolase;
KW   Protease; Secreted; Serine protease.
FT   CHAIN        <1   >282       Coagulation factor IX.
FT                                /FTId=PRO_0000088685.
FT   DOMAIN       56   >282       Peptidase S1.
FT   ACT_SITE     96     96       Charge relay system.
FT   ACT_SITE    144    144       Charge relay system.
FT   ACT_SITE    240    240       Charge relay system.
FT   CARBOHYD     25     25       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     36     36       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   DISULFID     81     97       By similarity.
FT   DISULFID    211    225       By similarity.
FT   DISULFID    236    264       By similarity.
FT   NON_TER       1      1
FT   NON_TER     282    282
SQ   SEQUENCE   282 AA;  31447 MW;  88B37B0A4673BEC9 CRC64;
     RVSVAYNSKK ITRAETVFSN TDYGNSTELI LDDITNSTIL DNLTENSEPI NDFTRVVGGE
     NAKPGQIPWQ VILNGEIEAF CGGAIINEKW IVTAAHCLKP GDKIEVVAGE HNIDEKEDTE
     QRRNVIRTIP HHQYNATINK YSHDIALLEL DKPLILNSYV TPICVANKEY TNIFLKFGSG
     YVSGWGKVFN KGRQASILQY LRVPLVDRAT CLRSTKFSIY NNMFCAGYRE GGKDSCEGDS
     GGPHVTEVEG TSFLTGIISW GEECAMKGKY GIYTKVSRYV NW
//