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P16294

- FA9_MOUSE

UniProt

P16294 - FA9_MOUSE

Protein

Coagulation factor IX

Gene

F9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 3 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.

    Catalytic activityi

    Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei192 – 1932Cleavage; by factor XIaBy similarity
    Sitei236 – 2372Cleavage; by factor XIaBy similarity
    Active sitei277 – 2771Charge relay systemBy similarity
    Active sitei325 – 3251Charge relay systemBy similarity
    Active sitei421 – 4211Charge relay systemBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. peptidase activity Source: MGI
    3. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Protein family/group databases

    MEROPSiS01.214.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coagulation factor IX (EC:3.4.21.22)
    Alternative name(s):
    Christmas factor
    Cleaved into the following 2 chains:
    Gene namesi
    Name:F9
    Synonyms:Cf9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:88384. F9.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Propeptidei29 – 4618By similarityPRO_0000027760Add
    BLAST
    Chaini47 – 471425Coagulation factor IXPRO_0000027761Add
    BLAST
    Chaini47 – 192146Coagulation factor IXa light chainPRO_0000027762Add
    BLAST
    Propeptidei193 – 23644Activation peptideBy similarityPRO_0000027763Add
    BLAST
    Chaini237 – 471235Coagulation factor IXa heavy chainPRO_0000027764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei53 – 5314-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei63 – 6314-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi64 ↔ 69By similarity
    Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei82 – 8214-carboxyglutamatePROSITE-ProRule annotation
    Modified residuei86 – 8614-carboxyglutamatePROSITE-ProRule annotation
    Disulfide bondi97 ↔ 108By similarity
    Glycosylationi99 – 991O-linked (Glc...); alternateBy similarity
    Glycosylationi99 – 991O-linked (Xyl...); alternateBy similarity
    Disulfide bondi102 ↔ 117By similarity
    Modified residuei110 – 1101(3R)-3-hydroxyaspartateBy similarity
    Modified residuei114 – 1141PhosphoserineBy similarity
    Disulfide bondi119 ↔ 128By similarity
    Disulfide bondi134 ↔ 145By similarity
    Disulfide bondi141 ↔ 155By similarity
    Disulfide bondi157 ↔ 170By similarity
    Disulfide bondi178 ↔ 345By similarity
    Modified residuei202 – 2021SulfotyrosineBy similarity
    Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
    Modified residuei205 – 2051PhosphoserineBy similarity
    Glycosylationi206 – 2061O-linked (GalNAc...)By similarity
    Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi225 – 2251O-linked (GalNAc...)By similarity
    Disulfide bondi262 ↔ 278By similarity
    Disulfide bondi392 ↔ 406By similarity
    Disulfide bondi417 ↔ 445By similarity

    Post-translational modificationi

    Activated by factor XIa, which excises the activation peptide.
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
    Predominantly O-glucosylated at Ser-99 by POGLUT1.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

    Proteomic databases

    MaxQBiP16294.
    PaxDbiP16294.
    PRIDEiP16294.

    PTM databases

    PhosphoSiteiP16294.

    Expressioni

    Tissue specificityi

    Synthesized primarily in the liver and secreted in plasma.

    Gene expression databases

    ArrayExpressiP16294.
    BgeeiP16294.
    CleanExiMM_F9.
    GenevestigatoriP16294.

    Interactioni

    Subunit structurei

    Heterodimer of a light chain and a heavy chain; disulfide-linked.

    Structurei

    3D structure databases

    ProteinModelPortaliP16294.
    SMRiP16294. Positions 47-192, 237-470.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 9246GlaPROSITE-ProRule annotationAdd
    BLAST
    Domaini93 – 12937EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini130 – 17142EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 469233Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00750000117249.
    HOGENOMiHOG000251821.
    HOVERGENiHBG013304.
    InParanoidiP16294.
    KOiK01321.
    OMAiSAECTVF.
    OrthoDBiEOG75B84T.
    PhylomeDBiP16294.
    TreeFamiTF327329.

    Family and domain databases

    Gene3Di4.10.740.10. 1 hit.
    InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR012224. Pept_S1A_FX.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00008. EGF. 1 hit.
    PF00594. Gla. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001143. Factor_X. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    SMARTiSM00181. EGF. 1 hit.
    SM00179. EGF_CA. 1 hit.
    SM00069. GLA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 1 hit.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16294-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG    50
    KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN 100
    PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD 150
    NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM 200
    DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW 250
    QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT 300
    EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE 350
    YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI 400
    YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK 450
    YGIYTKVSRY VNWIKEKTKL T 471
    Length:471
    Mass (Da):52,978
    Last modified:January 9, 2007 - v3
    Checksum:i05E08E86622397E2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti375 – 3751Q → H in AAA37629. (PubMed:2323576)Curated
    Sequence conflicti400 – 4001I → T in AAA37629. (PubMed:2323576)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK149372 mRNA. Translation: BAE28840.1.
    M23109 mRNA. Translation: AAA37629.1.
    M26236 mRNA. Translation: AAA37630.1.
    CCDSiCCDS30158.1.
    PIRiJQ0419.
    RefSeqiNP_032005.1. NM_007979.1.
    UniGeneiMm.391283.

    Genome annotation databases

    EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
    GeneIDi14071.
    KEGGimmu:14071.
    UCSCiuc009thw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK149372 mRNA. Translation: BAE28840.1 .
    M23109 mRNA. Translation: AAA37629.1 .
    M26236 mRNA. Translation: AAA37630.1 .
    CCDSi CCDS30158.1.
    PIRi JQ0419.
    RefSeqi NP_032005.1. NM_007979.1.
    UniGenei Mm.391283.

    3D structure databases

    ProteinModelPortali P16294.
    SMRi P16294. Positions 47-192, 237-470.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S01.214.

    PTM databases

    PhosphoSitei P16294.

    Proteomic databases

    MaxQBi P16294.
    PaxDbi P16294.
    PRIDEi P16294.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033477 ; ENSMUSP00000033477 ; ENSMUSG00000031138 .
    GeneIDi 14071.
    KEGGi mmu:14071.
    UCSCi uc009thw.1. mouse.

    Organism-specific databases

    CTDi 2158.
    MGIi MGI:88384. F9.

    Phylogenomic databases

    eggNOGi COG5640.
    GeneTreei ENSGT00750000117249.
    HOGENOMi HOG000251821.
    HOVERGENi HBG013304.
    InParanoidi P16294.
    KOi K01321.
    OMAi SAECTVF.
    OrthoDBi EOG75B84T.
    PhylomeDBi P16294.
    TreeFami TF327329.

    Miscellaneous databases

    NextBioi 285068.
    PROi P16294.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16294.
    Bgeei P16294.
    CleanExi MM_F9.
    Genevestigatori P16294.

    Family and domain databases

    Gene3Di 4.10.740.10. 1 hit.
    InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR000294. GLA_domain.
    IPR012224. Pept_S1A_FX.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF00594. Gla. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001143. Factor_X. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    PR00001. GLABLOOD.
    SMARTi SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 1 hit.
    SM00069. GLA. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57630. SSF57630. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 1 hit.
    PS01187. EGF_CA. 1 hit.
    PS00011. GLA_1. 1 hit.
    PS50998. GLA_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    2. "Deduced amino acid sequence of mouse blood-coagulation factor IX."
      Wu S.-M., Stafford D.W., Ware J.
      Gene 86:275-278(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-471.
    3. "Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species."
      Sarkar G., Koeberl D.D., Sommer S.S.
      Genomics 6:133-143(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 180-463.

    Entry informationi

    Entry nameiFA9_MOUSE
    AccessioniPrimary (citable) accession number: P16294
    Secondary accession number(s): Q3UES1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 163 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3