FA9_CAVPO
ID FA9_CAVPO Reviewed; 285 AA.
AC P16295;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 119.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26237; AAA37037.1; -; mRNA.
DR PIR; I48144; I48144.
DR AlphaFoldDB; P16295; -.
DR SMR; P16295; -.
DR STRING; 10141.ENSCPOP00000016267; -.
DR MEROPS; S01.214; -.
DR eggNOG; ENOG502QUEV; Eukaryota.
DR HOGENOM; CLU_006842_0_4_1; -.
DR InParanoid; P16295; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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..>285
FT /note="Coagulation factor IX"
FT /id="PRO_0000088683"
FT DOMAIN 59..>285
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 99
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT BINDING 123
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 58..59
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; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="O-linked (GalNAc...) threonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT CARBOHYD 45
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 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..100
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 214..228
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT DISULFID 239..267
FT /evidence="ECO:0000250|UniProtKB:P00740"
FT NON_TER 1
FT NON_TER 285
SQ SEQUENCE 285 AA; 32032 MW; 68E36DD317C11C60 CRC64;
RVSIPSVSKE HNRANAIFSR MGYVNFTDDE TIWDDNDDDE TIWDNSTEST KPSDEFFRVV
GGEDAKPGQF PWQVLLNGET EAFCGGSIVN EKWIVTAAHC ILPGIKIEVV AGKHNIEKKE
DTEQRRNVTQ IILHHSYNAS FNKYSHDIAL LELDKPLSLN SYVTPICIAN REYTNIFLKF
GAGYVSGWGK LFSQGRTASI LQYLRVPLVD RATCLRSTKF TIYNNMFCAG FHEGGRDSCQ
GDSGGPHVTE VEGTNFLTGI ISWGEECAMK GKYGIYTKVS RYVNW
