(data stored in ACNUC19913 zone)

HOGENOM: HSX_PE2478

ID   HSX_PE2478                           STANDARD;      PRT;   461 AA.
AC   HSX_PE2478; P00740; A8K9N4; Q5JYJ8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Coagulation factor IX; EC=3.4.21 22;AltName: Full=Christmas
DE   factor;AltName: Full=Plasma thromboplastin component; Short=PTC;Contains:
DE   RecName: Full=Coagulation factor IXa light chain;Contains: RecName:
DE   Full=Coagulation factor IXa heavy chain;Flags: Precursor; (HSX.PE2478).
GN   Name=F9;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HSX.PE2478.
CC       Homo sapiens chromosome X GRCh37  sequence 1..155260560 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:FA9_HUMAN
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   -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
CC       X to form factor Xa.
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized primarily in the liver and
CC       secreted in plasma.
CC   -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
CC       residues and, with stronger affinity, to another site, beyond the
CC       Gla domain.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC   -!- DISEASE: Defects in F9 are the cause of recessive X-linked
CC       hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease.
CC   -!- DISEASE: Note=Mutations in position 43 (Oxford-3, San Dimas) and
CC       46 (Cambridge) prevents cleavage of the propeptide, mutation in
CC       position 93 (Alabama) probably fails to bind to cell membranes,
CC       mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya
CC       OR Hilo) prevent cleavage of the activation peptide.
CC   -!- DISEASE: Defects in F9 are the cause of thrombophilia due to
CC       factor IX defect (THR-FIX) [MIM:300807]. A hemostatic disorder
CC       characterized by a tendency to thrombosis.
CC   -!- PHARMACEUTICAL: Available under the name BeneFix (Baxter and
CC       American Home Products). Used to treat hemophilia B.
CC   -!- MISCELLANEOUS: In 1952, one of the earliest researchers of the
CC       disease, Dr. R.G. Macfarlane used the patient's surname,
CC       Christmas, to refer to the disease and also to refer to the
CC       clotting factor which he called the 'Christmas Factor' At the time
CC       Stephen Christmas was a 5-year-old boy. He died in 1993 at the age
CC       of 46 from acquired immunodeficiency syndrome contracted through
CC       treatment with blood products.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Factor IX entry;
CC       URL="http://en.wikipedia.org/wiki/Factor_IX";
CC   -!- WEB RESOURCE: Name=HAEMB; Note=Hemophilia B mutation database;
CC       URL="http://www.kcl.ac.uk/ip/petergreen/haemBdatabase.html";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/F9";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/f9/";
CC   -!- WEB RESOURCE: Name=BeneFix; Note=Clinical information on BeneFix;
CC       URL="http://www.wyeth.com/products/benefix.asp";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The Christmas Factor -
CC       Issue 41 of December 2003;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt041.shtml";
CC   -!- GENE_FAMILY: HOG000251821 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000101981;ENST00000394090;ENSP00000377650.
DR   EMBL; AF536327; - ;
DR   EMBL; AK292749; - ;
DR   EMBL; AL033403; - ;
DR   EMBL; AY226143; - ;
DR   EMBL; AY269424; - ;
DR   EMBL; AY269425; - ;
DR   EMBL; BC109214; - ;
DR   EMBL; BC109215; - ;
DR   EMBL; CH471150; - ;
DR   EMBL; DQ431774; - ;
DR   EMBL; DQ431775; - ;
DR   EMBL; DQ431776; - ;
DR   EMBL; DQ431777; - ;
DR   EMBL; DQ431778; - ;
DR   EMBL; DQ431779; - ;
DR   EMBL; DQ431780; - ;
DR   EMBL; DQ431781; - ;
DR   EMBL; DQ431782; - ;
DR   EMBL; DQ431783; - ;
DR   EMBL; DQ431784; - ;
DR   EMBL; DQ431785; - ;
DR   EMBL; DQ431786; - ;
DR   EMBL; DQ431787; - ;
DR   EMBL; DQ431788; - ;
DR   EMBL; DQ431789; - ;
DR   EMBL; DQ431790; - ;
DR   EMBL; DQ431791; - ;
DR   EMBL; DQ431792; - ;
DR   EMBL; DQ431793; - ;
DR   EMBL; DQ431794; - ;
DR   EMBL; DQ431795; - ;
DR   EMBL; DQ431796; - ;
DR   EMBL; DQ431797; - ;
DR   EMBL; DQ431798; - ;
DR   EMBL; DQ431801; - ;
DR   EMBL; DQ431803; - ;
DR   EMBL; DQ431804; - ;
DR   EMBL; DQ431805; - ;
DR   EMBL; DQ431806; - ;
DR   EMBL; DQ431807; - ;
DR   EMBL; DQ431808; - ;
DR   EMBL; DQ431809; - ;
DR   EMBL; DQ431810; - ;
DR   EMBL; DQ431811; - ;
DR   EMBL; DQ431816; - ;
DR   EMBL; DQ431817; - ;
DR   EMBL; DQ431818; - ;
DR   EMBL; DQ431819; - ;
DR   EMBL; DQ431820; - ;
DR   EMBL; DQ431821; - ;
DR   EMBL; DQ431822; - ;
DR   EMBL; DQ431823; - ;
DR   EMBL; DQ431824; - ;
DR   EMBL; DQ431825; - ;
DR   EMBL; DQ431826; - ;
DR   EMBL; DQ431827; - ;
DR   EMBL; DQ431828; - ;
DR   EMBL; DQ431829; - ;
DR   EMBL; DQ431830; - ;
DR   EMBL; DQ431831; - ;
DR   EMBL; DQ431832; - ;
DR   EMBL; DQ431833; - ;
DR   EMBL; DQ431834; - ;
DR   EMBL; DQ431835; - ;
DR   EMBL; DQ431836; - ;
DR   EMBL; DQ431837; - ;
DR   EMBL; DQ431838; - ;
DR   EMBL; DQ431839; - ;
DR   EMBL; DQ431840; - ;
DR   EMBL; J00136; - ;
DR   EMBL; J00137; - ;
DR   EMBL; K02048; - ;
DR   EMBL; K02049; - ;
DR   EMBL; K02051; - ;
DR   EMBL; K02052; - ;
DR   EMBL; K02053; - ;
DR   EMBL; K02402; - ;
DR   EMBL; M11309; - ;
DR   EMBL; M19063; - ;
DR   EMBL; M35672; - ;
DR   EMBL; S66752; - ;
DR   EMBL; S68634; - ;
DR   UniProtKB/Swiss-Prot; P00740; A8K9N4; Q5JYJ8; -.
DR   EMBL; J00136; AAA98726.1; -; mRNA.
DR   EMBL; J00137; AAA52763.1; -; mRNA.
DR   EMBL; K02053; AAA56822.1; -; Genomic_DNA.
DR   EMBL; K02048; AAA56822.1; JOINED; Genomic_DNA.
DR   EMBL; K02049; AAA56822.1; JOINED; Genomic_DNA.
DR   EMBL; K02051; AAA56822.1; JOINED; Genomic_DNA.
DR   EMBL; K02052; AAA56822.1; JOINED; Genomic_DNA.
DR   EMBL; K02402; AAB59620.1; -; Genomic_DNA.
DR   EMBL; M11309; AAA52023.1; -; mRNA.
DR   EMBL; AL033403; CAI42103.1; -; Genomic_DNA.
DR   EMBL; AF536327; AAM96188.1; -; Genomic_DNA.
DR   EMBL; AK292749; BAF85438.1; -; mRNA.
DR   EMBL; CH471150; EAW88433.1; -; Genomic_DNA.
DR   EMBL; BC109214; AAI09215.1; -; mRNA.
DR   EMBL; BC109215; AAI09216.1; -; mRNA.
DR   EMBL; S68634; AAB29758.1; -; Genomic_DNA.
DR   EMBL; M35672; AAA51981.1; -; mRNA.
DR   EMBL; M19063; AAA52456.1; -; Genomic_DNA.
DR   EMBL; S66752; AAB28588.1; -; Genomic_DNA.
DR   IPI; IPI00296176; -.
DR   PIR; A00922; KFHU.
DR   RefSeq; NP_000124.1; NM_000133.3.
DR   UniGene; Hs.522798; -.
DR   PDB; 1CFH; NMR; -; A=47-93.
DR   PDB; 1CFI; NMR; -; A=47-93.
DR   PDB; 1EDM; X-ray; 1.50 A; B/C=92-130.
DR   PDB; 1IXA; NMR; -; A=92-130.
DR   PDB; 1MGX; NMR; -; A=47-93.
DR   PDB; 1NL0; X-ray; 2.20 A; G=47-91.
DR   PDB; 1RFN; X-ray; 2.80 A; A=227-461, B=133-188.
DR   PDB; 2WPH; X-ray; 1.50 A; E=133-191, S=227-461.
DR   PDB; 2WPI; X-ray; 1.99 A; E=133-191, S=227-461.
DR   PDB; 2WPJ; X-ray; 1.60 A; E=133-191, S=227-461.
DR   PDB; 2WPK; X-ray; 2.21 A; E=133-191, S=227-461.
DR   PDB; 2WPL; X-ray; 1.82 A; E=133-191, S=227-461.
DR   PDB; 2WPM; X-ray; 2.00 A; E=133-191, S=227-461.
DR   PDB; 3KCG; X-ray; 1.70 A; H=227-461, L=131-188.
DR   PDB; 3LC3; X-ray; 1.90 A; A/C=227-461, B/D=133-188.
DR   PDB; 3LC5; X-ray; 2.62 A; A=227-461, B=133-188.
DR   PDBsum; 1CFH; -.
DR   PDBsum; 1CFI; -.
DR   PDBsum; 1EDM; -.
DR   PDBsum; 1IXA; -.
DR   PDBsum; 1MGX; -.
DR   PDBsum; 1NL0; -.
DR   PDBsum; 1RFN; -.
DR   PDBsum; 2WPH; -.
DR   PDBsum; 2WPI; -.
DR   PDBsum; 2WPJ; -.
DR   PDBsum; 2WPK; -.
DR   PDBsum; 2WPL; -.
DR   PDBsum; 2WPM; -.
DR   PDBsum; 3KCG; -.
DR   PDBsum; 3LC3; -.
DR   PDBsum; 3LC5; -.
DR   ProteinModelPortal; P00740; -.
DR   SMR; P00740; 47-191, 227-461.
DR   DIP; DIP-58520N; -.
DR   STRING; P00740; -.
DR   MEROPS; S01.214; -.
DR   GlycoSuiteDB; P00740; -.
DR   PhosphoSite; P00740; -.
DR   PeptideAtlas; P00740; -.
DR   PRIDE; P00740; -.
DR   Ensembl; ENST00000218099; ENSP00000218099; ENSG00000101981.
DR   Ensembl; ENST00000394090; ENSP00000377650; ENSG00000101981.
DR   GeneID; 2158; -.
DR   KEGG; hsa:2158; -.
DR   NMPDR; fig|9606.3.peg.33470; -.
DR   UCSC; uc004fas.1; human.
DR   CTD; 2158; -.
DR   GeneCards; GC0XP127880; -.
DR   H-InvDB; HIX0056112; -.
DR   HGNC; HGNC:3551; F9.
DR   HPA; HPA000254; -.
DR   MIM; 300746; gene.
DR   MIM; 300807; phenotype.
DR   MIM; 306900; phenotype.
DR   neXtProt; NX_P00740; -.
DR   Orphanet; 169799; Mild hemophilia B.
DR   Orphanet; 169796; Moderately severe hemophilia B.
DR   Orphanet; 169793; Severe hemophilia B.
DR   Orphanet; 177929; Symptomatic form of hemophilia B in female carriers.
DR   PharmGKB; PA27954; -.
DR   eggNOG; prNOG06113; -.
DR   InParanoid; P00740; -.
DR   OMA; KYSHDIA; -.
DR   OrthoDB; EOG4THVTF; -.
DR   PhylomeDB; P00740; -.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   Reactome; REACT_604; Hemostasis.
DR   BindingDB; P00740; -.
DR   DrugBank; DB00025; Antihemophilic Factor.
DR   DrugBank; DB00100; Coagulation Factor IX.
DR   DrugBank; DB01109; Heparin.
DR   DrugBank; DB00170; Menadione.
DR   NextBio; 8719; -.
DR   PMAP-CutDB; P00740; -.
DR   ArrayExpress; P00740; -.
DR   Bgee; P00740; -.
DR   CleanEx; HS_F9; -.
DR   Genevestigator; P00740; -.
DR   GermOnline; ENSG00000101981; Homo sapiens.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0007598; P:blood coagulation, extrinsic pathway; EXP:Reactome.
DR   GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
DR   GO; GO:0017187; P:peptidyl-glutamic acid carboxylation; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; TAS:Reactome.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Pept_cys/ser_Trypsin-like.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Gene3D; G3DSA:4.10.740.10; Coagulation_factor_Gla; 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; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; Pept_Ser_Cys; 1.
DR   SUPFAM; SSF57630; VitK_dep_GLA; 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.
DR   HOGENOMDNA; HSX.PE2478; -.
KW   ENSG000001019811755old_1320000031; ENSP000003776507901old_1320000031;
KW   Q19UG1_HUMAN; Q19UG2_HUMAN; Q19UG3_HUMAN; Q19UG4_HUMAN; Q19UG5_HUMAN;
KW   Q19UG8_HUMAN; Q19UG9_HUMAN; Q19UH5_HUMAN; Q19UH6_HUMAN; Q19UH8_HUMAN;
KW   Q19UI1_HUMAN; Q19UI2_HUMAN; Q19UI3_HUMAN; Q19UI4_HUMAN; Q19UI5_HUMAN;
KW   Q19UJ1_HUMAN; Q19UJ4_HUMAN; Q19UJ5_HUMAN; Q19UJ6_HUMAN; Q19UJ7_HUMAN;
KW   Q19UK3_HUMAN; Q19UK4_HUMAN; Q19UK5_HUMAN; Q19UK6_HUMAN; Q19UK7_HUMAN;
KW   Q19UK9_HUMAN; Q19UL0_HUMAN; Q19UL1_HUMAN; Q19UL3_HUMAN; Q19UL5_HUMAN;
KW   Q19UL8_HUMAN; Q19UM0_HUMAN; Q19UM1_HUMAN; Q19UM2_HUMAN; Q7Z7N0_HUMAN;
KW   Q86XR9_HUMAN; AF536327; AK292749; AL033403; AY226143; AY269424; AY269425;
KW   BC109215; CH471150; DQ431774; DQ431775; DQ431776; DQ431777; DQ431778;
KW   DQ431780; DQ431781; DQ431782; DQ431783; DQ431784; DQ431785; DQ431786;
KW   DQ431788; DQ431789; DQ431790; DQ431791; DQ431792; DQ431793; DQ431794;
KW   DQ431796; DQ431797; DQ431798; DQ431801; DQ431803; DQ431804; DQ431805;
KW   DQ431807; DQ431808; DQ431809; DQ431810; DQ431811; DQ431816; DQ431817;
KW   DQ431819; DQ431820; DQ431821; DQ431822; DQ431823; DQ431824; DQ431825;
KW   DQ431827; DQ431828; DQ431829; DQ431830; DQ431831; DQ431832; DQ431833;
KW   DQ431835; DQ431836; DQ431837; DQ431838; DQ431839; DQ431840; J00136;
KW   K02048; K02049; K02051; K02052; K02053; K02402; M11309; M19063; M35672;
KW   S68634;
KW   3D-structure; Blood coagulation; Calcium;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemophilia;
KW   Hydrolase; Hydroxylation; Pharmaceutical; Phosphoprotein;
KW   Polymorphism; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Sulfation; Thrombophilia; Zymogen.
SQ   SEQUENCE   461 AA;  UNKNOWN MW;  UNKNOWN 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 WIVTAAHCVE TGVKITVVAG EHNIEETEHT EQKRNVIRII
     PHHNYNAAIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF
     HKGRSALVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE
     GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
//

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