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 02-SEP-2026, entry version 127. 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 (inactive and activated) with F11 (activated) in CC calcium-dependent manner. Interacts with SERPINC1. CC {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 (By similarity). CC Activated by coagulation factor VIIa-tissue factor (F7-F3) complex in CC calcium-dependent manner (By similarity). 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 GlyCosmos; P16295; 6 sites, No reported glycans. DR eggNOG; ENOG502QUEV; Eukaryota. DR HOGENOM; CLU_006842_0_4_1; -. DR InParanoid; P16295; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; 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 FunFam; 2.40.10.10:FF:000013; Coagulation factor X; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR050127; Serine_Proteases_S1. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR24264:SF65; SRCR DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 //