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Database: UniProt
Entry: Q95ND7
LinkDB: Q95ND7
Original site: Q95ND7 
ID   FA9_PANTR               Reviewed;         461 AA.
AC   Q95ND7;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JAN-2019, entry version 135.
DE   RecName: Full=Coagulation factor IX;
DE            EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740};
DE   AltName: Full=Christmas factor;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa light chain;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa heavy chain;
DE   Flags: Precursor;
GN   Name=F9;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate 504;
RX   PubMed=11569499; DOI=10.1266/ggs.76.159;
RA   Satta Y.;
RT   "Comparison of DNA and protein polymorphisms between humans and
RT   chimpanzees.";
RL   Genes Genet. Syst. 76:159-168(2001).
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       {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;
CC         Evidence={ECO:0000250|UniProtKB:P00740};
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked. Interacts with SERPINC1.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
CC   -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
CC       residues in the Gla domain. Calcium can also bind, with stronger
CC       affinity, to another site beyond the Gla domain. Under
CC       physiological ion concentrations, Ca(2+) is displaced by Mg(2+)
CC       from some of the gammaglutamate residues in the N-terminal Gla
CC       domain. This leads to a subtle conformation change that may affect
CC       the interaction with its binding protein.
CC       {ECO:0000250|UniProtKB:P00741}.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide. The propeptide can also be removed by snake venom
CC       protease. {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AB062470; BAB58885.1; -; Genomic_DNA.
DR   RefSeq; NP_001129063.1; NM_001135591.1.
DR   UniGene; Ptr.6102; -.
DR   ProteinModelPortal; Q95ND7; -.
DR   SMR; Q95ND7; -.
DR   STRING; 9598.ENSPTRP00000047240; -.
DR   MEROPS; S01.214; -.
DR   PaxDb; Q95ND7; -.
DR   PRIDE; Q95ND7; -.
DR   Ensembl; ENSPTRT00000085797; ENSPTRP00000079315; ENSPTRG00000022330.
DR   GeneID; 465887; -.
DR   KEGG; ptr:465887; -.
DR   CTD; 2158; -.
DR   VGNC; VGNC:1389; F9.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000159516; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; Q95ND7; -.
DR   KO; K01321; -.
DR   OMA; SYECWCQ; -.
DR   OrthoDB; 1314811at2759; -.
DR   PMAP-CutDB; Q95ND7; -.
DR   Proteomes; UP000002277; Chromosome X.
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:InterPro.
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; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR035694; Coagulation_factor_IX.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR44064:SF4; PTHR44064:SF4; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
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; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
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   3: Inferred from homology;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Magnesium; Metal-binding; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Sulfation; Zymogen.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   PROPEP       29     46       {ECO:0000250|UniProtKB:P00740}.
FT                                /FTId=PRO_0000027765.
FT   CHAIN        47    461       Coagulation factor IX.
FT                                /FTId=PRO_0000027766.
FT   CHAIN        47    191       Coagulation factor IXa light chain.
FT                                /FTId=PRO_0000027767.
FT   PROPEP      192    226       Activation peptide.
FT                                /FTId=PRO_0000027768.
FT   CHAIN       227    461       Coagulation factor IXa heavy chain.
FT                                /FTId=PRO_0000027769.
FT   DOMAIN       47     92       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       93    129       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      130    171       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      227    459       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    267    267       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    315    315       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    411    411       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        47     47       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        48     48       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        53     53       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        53     53       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        54     54       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        54     54       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        61     61       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        66     66       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        67     67       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        72     72       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        73     73       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        73     73       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        76     76       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        76     76       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        82     82       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        86     86       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        93     93       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        94     94       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        96     96       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       110    110       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       111    111       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       281    281       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       283    283       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       286    286       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       288    288       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       291    291       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        191    192       Cleavage; by factor XIa.
FT   SITE        226    227       Cleavage; by factor XIa.
FT   MOD_RES      53     53       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      54     54       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      63     63       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      72     72       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      73     73       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      79     79       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      82     82       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      86     86       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     110    110       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     201    201       Sulfotyrosine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     204    204       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     205    205       Phosphothreonine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     85     85       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     99     99       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     99     99       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    107    107       O-linked (Fuc...) serine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    205    205       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    213    213       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    215    215       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    225    225       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID     64     69       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID     97    108       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    102    117       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    119    128       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    134    145       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    141    155       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    157    170       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    178    335       Interchain (between light and heavy
FT                                chains). {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    252    268       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    382    396       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    407    435       {ECO:0000250|UniProtKB:P00740}.
SQ   SEQUENCE   461 AA;  51764 MW;  30C2F857C0F77F45 CRC64;
     MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL
     ERECMEEKCS FEEAREVFEN TERTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP
     FGFEGKNCEL DVTCNIKNGR CEQFCKNSAD NKVVCSCTEG YRLAENQKSC EPAVPFPCGR
     VSVSQTSKLT RAETVFPDVD YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW
     QVVLNGKVDA FCGGSIVNEK WIVTAAHCVD TGVKITVVAG EHNIEETEHT EQKRNVIRII
     PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF
     HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE
     GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
//
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