FA9_RABIT
ID FA9_RABIT Reviewed; 275 AA.
AC P16292;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Coagulation factor IX;
DE EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740};
DE AltName: Full=Christmas factor;
DE Flags: Fragment;
GN Name=F9;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 of
RT 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+) ions,
CC phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740};
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain; disulfide-
CC linked. Interacts with SERPINC1. {ECO:0000250|UniProtKB:P00740}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
CC -!- PTM: Activated by factor XIa, which excises the activation peptide. The
CC propeptide can also be removed by snake venom protease.
CC {ECO:0000250|UniProtKB:P00740}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; M26234; AAA31251.1; -; mRNA.
DR PIR; I46712; I46712.
DR AlphaFoldDB; P16292; -.
DR SMR; P16292; -.
DR STRING; 9986.ENSOCUP00000004537; -.
DR MEROPS; S01.214; -.
DR PRIDE; P16292; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR InParanoid; P16292; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR035694; Coagulation_factor_IX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 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; Hemostasis;
KW Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome;
KW Secreted; Serine protease; Sulfation.
FT CHAIN <1..>275
FT /note="Coagulation factor IX"
FT /id="PRO_0000088684"
FT DOMAIN 49..>275
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 89
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 233
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 13..14
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT SITE 48..49
FT /note="Cleavage; by factor XIa"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 23
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT MOD_RES 27
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 74..90
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 204..218
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 229..257
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT NON_TER 1
FT NON_TER 275
SQ SEQUENCE 275 AA; 30777 MW; FE364489AC76BE87 CRC64;
GVSVSHASKK ITRATTIFSN TEYENFTEAE TIRGNVTQRS QSSDDFTRIV GGENAKPGQF
PWQVLLNGKV EAFCGGSIIN EKWVVTAAHC IKPDDNITVV AGEYNIQETE NTEQKRNVIR
IIPYHKYNAT INKYNHDIAL LELDKPLTLN SYVTPICIAN REYTNIFLNF GSGYVSGWGR
VFNRGRQASI LQYLRVPFVD RATCLRSTKF TIYNNMFCAG FDVGGKDSCE GDSGGPHVTE
VEGTSFLTGI ISWGEECAIK GKYGVYTRVS WYVNW
