ID A0A099Z2H8_TINGU Unreviewed; 440 AA.
AC A0A099Z2H8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Coagulation factor IX {ECO:0000256|ARBA:ARBA00019454};
DE EC=3.4.21.22 {ECO:0000256|ARBA:ARBA00012066};
DE AltName: Full=Christmas factor {ECO:0000256|ARBA:ARBA00031357};
DE Flags: Fragment;
GN ORFNames=N309_00492 {ECO:0000313|EMBL:KGL75323.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL75323.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL75323.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL75323.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002741}.
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:0000256|ARBA:ARBA00001368};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KL887884; KGL75323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099Z2H8; -.
DR STRING; 94827.A0A099Z2H8; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
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; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF31; COAGULATION FACTOR IX; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Gamma-carboxyglutamic acid {ECO:0000256|ARBA:ARBA00022479};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641};
KW Serine protease {ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 19..65
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 65..101
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 211..440
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 300
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT ACT_SITE 396
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001143-1"
FT DISULFID 91..100
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL75323.1"
FT NON_TER 440
FT /evidence="ECO:0000313|EMBL:KGL75323.1"
SQ SEQUENCE 440 AA; 49036 MW; AC5C4373B0624664 CRC64;
AVFLENREAS AILQRQRRAN SNRLEEVIAG NLERECIEEK CSYEEAREVF ENTEKTMEFW
KMYIDGDQCD PNPCKNGAIC KDGVGSYVCW CPAGYEGRNC EIDFTCSIKN GGCKHFCRHD
PPHKVVCSCA AGYKLHEDGK SCEPAVPYPC GRITAPEAKS KLTRAINTLE NWNTTYDDLD
DVSDEDLDNI TETTTAATTR IVPIVKTGTR VVGGSDSMRG EVPWQVYLVN SHNVGFCGGS
IINERWVVTA AHCLQPGDNV TAVAGEYNTR VEDATEQRRR VVRIVPHPTY NATLHKHHND
IALLELEETL HFNSYVTPIC LGSRDFTAKL LKYGMGTVSG WGSLFYRGRE SIILQVLRVP
FVDRPTCLKS TSITIELNMF CAGYSAGGRD TCEGDSGGPF ATEFEGTWFL TGVTSWGEEC
AKPGKYGIYT KVSKYIKWIK
//
