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Q06194

- FA8_MOUSE

UniProt

Q06194 - FA8_MOUSE

Protein

Coagulation factor VIII

Gene

F8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei391 – 3922Cleavage; by thrombinBy similarity
    Sitei759 – 7602Cleavage; by thrombinBy similarity
    Sitei1324 – 13252Cleavage (activation)By similarity
    Sitei1640 – 16412Cleavage (activation)By similarity
    Sitei1678 – 16792Cleavage; by thrombinBy similarity

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. oxidoreductase activity Source: InterPro
    3. serine-type endopeptidase activity Source: Ensembl

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. blood coagulation, intrinsic pathway Source: Ensembl
    3. cell adhesion Source: InterPro
    4. platelet activation Source: InterPro

    Keywords - Biological processi

    Acute phase, Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Coagulation factor VIII
    Alternative name(s):
    Procoagulant component
    Gene namesi
    Name:F8
    Synonyms:Cf8, F8c
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:88383. F8.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 23192300Coagulation factor VIIIPRO_0000002972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi173 ↔ 199Curated
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
    Modified residuei367 – 3671SulfotyrosineBy similarity
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi547 ↔ 573Curated
    Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
    Modified residuei737 – 7371SulfotyrosineBy similarity
    Modified residuei738 – 7381SulfotyrosineBy similarity
    Modified residuei742 – 7421SulfotyrosineBy similarity
    Glycosylationi880 – 8801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi958 – 9581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1015 – 10151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1026 – 10261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1044 – 10441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1076 – 10761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1087 – 10871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1136 – 11361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1161 – 11611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1192 – 11921N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1268 – 12681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1273 – 12731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1302 – 13021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1316 – 13161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1378 – 13781N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1669 – 16691SulfotyrosineBy similarity
    Modified residuei1687 – 16871SulfotyrosineBy similarity
    Glycosylationi1797 – 17971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1819 ↔ 1845Curated
    Disulfide bondi2008 ↔ 2156PROSITE-ProRule annotation
    Glycosylationi2105 – 21051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2161 ↔ 2313PROSITE-ProRule annotation

    Post-translational modificationi

    The binding of vWF and activation depend on the sulfation of Tyr-1669.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Sulfation

    Proteomic databases

    PaxDbiQ06194.
    PRIDEiQ06194.

    PTM databases

    PhosphoSiteiQ06194.

    Expressioni

    Tissue specificityi

    Found in most tissues.

    Gene expression databases

    ArrayExpressiQ06194.
    BgeeiQ06194.
    CleanExiMM_F8.
    GenevestigatoriQ06194.

    Interactioni

    Subunit structurei

    Interacts with vWF. vWF binding is essential for the stabilization of F8 in circulation By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ06194.
    SMRiQ06194. Positions 20-744, 1678-2319.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 349330F5/8 type A 1Add
    BLAST
    Domaini20 – 199180Plastocyanin-like 1Add
    BLAST
    Domaini207 – 349143Plastocyanin-like 2Add
    BLAST
    Domaini399 – 730332F5/8 type A 2Add
    BLAST
    Domaini399 – 573175Plastocyanin-like 3Add
    BLAST
    Domaini583 – 730148Plastocyanin-like 4Add
    BLAST
    Domaini1683 – 2008326F5/8 type A 3Add
    BLAST
    Domaini1683 – 1845163Plastocyanin-like 5Add
    BLAST
    Domaini1855 – 2008154Plastocyanin-like 6Add
    BLAST
    Domaini2008 – 2156149F5/8 type C 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2161 – 2313153F5/8 type C 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni760 – 1640881BAdd
    BLAST

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 3 F5/8 type A domains.Curated
    Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
    Contains 6 plastocyanin-like domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG151351.
    GeneTreeiENSGT00740000114988.
    HOGENOMiHOG000231686.
    HOVERGENiHBG106657.
    InParanoidiA2AN88.
    KOiK03899.
    OMAiWHVIGMG.
    OrthoDBiEOG7ZWD1D.
    TreeFamiTF329807.

    Family and domain databases

    Gene3Di2.60.120.260. 2 hits.
    2.60.40.420. 6 hits.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR024715. Factor_5/8.
    IPR014707. Factor_8.
    IPR008979. Galactose-bd-like.
    [Graphical view]
    PANTHERiPTHR10127:SF50. PTHR10127:SF50. 1 hit.
    PfamiPF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 2 hits.
    PF00754. F5_F8_type_C. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000354. Factors_V_VIII. 1 hit.
    SMARTiSM00231. FA58C. 2 hits.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 6 hits.
    SSF49785. SSF49785. 2 hits.
    PROSITEiPS01285. FA58C_1. 2 hits.
    PS01286. FA58C_2. 2 hits.
    PS50022. FA58C_3. 2 hits.
    PS00079. MULTICOPPER_OXIDASE1. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06194-1 [UniParc]FASTAAdd to Basket

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    MQIALFACFF LSLFNFCSSA IRRYYLGAVE LSWNYIQSDL LSVLHTDSRF     50
    LPRMSTSFPF NTSIMYKKTV FVEYKDQLFN IAKPRPPWMG LLGPTIWTEV 100
    HDTVVITLKN MASHPVSLHA VGVSYWKASE GDEYEDQTSQ MEKEDDKVFP 150
    GESHTYVWQV LKENGPMASD PPCLTYSYMS HVDLVKDLNS GLIGALLVCK 200
    EGSLSKERTQ MLYQFVLLFA VFDEGKSWHS ETNDSYTQSM DSASARDWPK 250
    MHTVNGYVNR SLPGLIGCHR KSVYWHVIGM GTTPEIHSIF LEGHTFFVRN 300
    HRQASLEISP ITFLTAQTLL IDLGQFLLFC HISSHKHDGM EAYVKVDSCP 350
    EESQWQKKNN NEEMEDYDDD LYSEMDMFTL DYDSSPFIQI RSVAKKYPKT 400
    WIHYISAEEE DWDYAPSVPT SDNGSYKSQY LSNGPHRIGR KYKKVRFIAY 450
    TDETFKTRET IQHESGLLGP LLYGEVGDTL LIIFKNQASR PYNIYPHGIT 500
    DVSPLHARRL PRGIKHVKDL PIHPGEIFKY KWTVTVEDGP TKSDPRCLTR 550
    YYSSFINPER DLASGLIGPL LICYKESVDQ RGNQMMSDKR NVILFSIFDE 600
    NQSWYITENM QRFLPNAAKT QPQDPGFQAS NIMHSINGYV FDSLELTVCL 650
    HEVAYWHILS VGAQTDFLSI FFSGYTFKHK MVYEDTLTLF PFSGETVFMS 700
    MENPGLWVLG CHNSDFRKRG MTALLKVSSC DKSTSDYYEE IYEDIPTQLV 750
    NENNVIDPRS FFQNTNHPNT RKKKFKDSTI PKNDMEKIEP QFEEIAEMLK 800
    VQSVSVSDML MLLGQSHPTP HGLFLSDGQE AIYEAIHDDH SPNAIDSNEG 850
    PSKVTQLRPE SHHSEKIVFT PQPGLQLRSN KSLETTIEVK WKKLGLQVSS 900
    LPSNLMTTTI LSDNLKATFE KTDSSGFPDM PVHSSSKLST TAFGKKAYSL 950
    VGSHVPLNVS EENSDSNILD STLMYSQESL PRDNILSMEN DRLLREKRFH 1000
    GIALLTKDNT LFKDNVSLMK TNKTYNHSTT NEKLHTESPT SIENSTTDLQ 1050
    DAILKVNSEI QEVTALIHDG TLLGKNSTYL RLNHMLNRTT STKNKDIFHR 1100
    KDEDPIPQDE ENTIMPFSKM LFLSESSNWF KKTNGNNSLN SEQEHSPKQL 1150
    VYLMFKKYVK NQSFLSEKNK VTVEQDGFTK NIGLKDMAFP HNMSIFLTTL 1200
    SNVHENGRHN QEKNIQEEIE KEALIEEKVV LPQVHEATGS KNFLKDILIL 1250
    GTRQNISLYE VHVPVLQNIT SINNSTNTVQ IHMEHFFKRR KDKETNSEGL 1300
    VNKTREMVKN YPSQKNITTQ RSKRALGQFR LSTQWLKTIN CSTQCIIKQI 1350
    DHSKEMKKFI TKSSLSDSSV IKSTTQTNSS DSHIVKTSAF PPIDLKRSPF 1400
    QNKFSHVQAS SYIYDFKTKS SRIQESNNFL KETKINNPSL AILPWNMFID 1450
    QGKFTSPGKS NTNSVTYKKR ENIIFLKPTL PEESGKIELL PQVSIQEEEI 1500
    LPTETSHGSP GHLNLMKEVF LQKIQGPTKW NKAKRHGESI KGKTESSKNT 1550
    RSKLLNHHAW DYHYAAQIPK DMWKSKEKSP EIISIKQEDT ILSLRPHGNS 1600
    HSIGANEKQN WPQRETTWVK QGQTQRTCSQ IPPVLKRHQR ELSAFQSEQE 1650
    ATDYDDAITI ETIEDFDIYS EDIKQGPRSF QQKTRHYFIA AVERLWDYGM 1700
    STSHVLRNRY QSDNVPQFKK VVFQEFTDGS FSQPLYRGEL NEHLGLLGPY 1750
    IRAEVEDNIM VTFKNQASRP YSFYSSLISY KEDQRGEEPR RNFVKPNETK 1800
    IYFWKVQHHM APTEDEFDCK AWAYFSDVDL ERDMHSGLIG PLLICHANTL 1850
    NPAHGRQVSV QEFALLFTIF DETKSWYFTE NVKRNCKTPC NFQMEDPTLK 1900
    ENYRFHAING YVMDTLPGLV MAQDQRIRWY LLSMGNNENI QSIHFSGHVF 1950
    TVRKKEEYKM AVYNLYPGVF ETLEMIPSRA GIWRVECLIG EHLQAGMSTL 2000
    FLVYSKQCQI PLGMASGSIR DFQITASGHY GQWAPNLARL HYSGSINAWS 2050
    TKEPFSWIKV DLLAPMIVHG IKTQGARQKF SSLYISQFII MYSLDGKKWL 2100
    SYQGNSTGTL MVFFGNVDSS GIKHNSFNPP IIARYIRLHP THSSIRSTLR 2150
    MELMGCDLNS CSIPLGMESK VISDTQITAS SYFTNMFATW SPSQARLHLQ 2200
    GRTNAWRPQV NDPKQWLQVD LQKTMKVTGI ITQGVKSLFT SMFVKEFLIS 2250
    SSQDGHHWTQ ILYNGKVKVF QGNQDSSTPM MNSLDPPLLT RYLRIHPQIW 2300
    EHQIALRLEI LGCEAQQQY 2319
    Length:2,319
    Mass (Da):266,196
    Last modified:July 27, 2011 - v2
    Checksum:i09CAC4CFBCCECA57
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti959 – 9591V → A in AAA37385. (PubMed:8314577)Curated
    Sequence conflicti988 – 9881M → I in AAA37385. (PubMed:8314577)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05573 mRNA. Translation: AAA37385.1.
    AL731844, AL808110 Genomic DNA. Translation: CAM15581.1.
    AL808110, AL731844 Genomic DNA. Translation: CAM26492.1.
    CH466576 Genomic DNA. Translation: EDL29229.1.
    CCDSiCCDS30238.1.
    PIRiA47004.
    RefSeqiNP_032003.2. NM_007977.2.
    UniGeneiMm.1805.

    Genome annotation databases

    EnsembliENSMUST00000033539; ENSMUSP00000033539; ENSMUSG00000031196.
    GeneIDi14069.
    KEGGimmu:14069.
    UCSCiuc009tpt.3. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05573 mRNA. Translation: AAA37385.1 .
    AL731844 , AL808110 Genomic DNA. Translation: CAM15581.1 .
    AL808110 , AL731844 Genomic DNA. Translation: CAM26492.1 .
    CH466576 Genomic DNA. Translation: EDL29229.1 .
    CCDSi CCDS30238.1.
    PIRi A47004.
    RefSeqi NP_032003.2. NM_007977.2.
    UniGenei Mm.1805.

    3D structure databases

    ProteinModelPortali Q06194.
    SMRi Q06194. Positions 20-744, 1678-2319.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q06194.

    Proteomic databases

    PaxDbi Q06194.
    PRIDEi Q06194.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033539 ; ENSMUSP00000033539 ; ENSMUSG00000031196 .
    GeneIDi 14069.
    KEGGi mmu:14069.
    UCSCi uc009tpt.3. mouse.

    Organism-specific databases

    CTDi 2157.
    MGIi MGI:88383. F8.

    Phylogenomic databases

    eggNOGi NOG151351.
    GeneTreei ENSGT00740000114988.
    HOGENOMi HOG000231686.
    HOVERGENi HBG106657.
    InParanoidi A2AN88.
    KOi K03899.
    OMAi WHVIGMG.
    OrthoDBi EOG7ZWD1D.
    TreeFami TF329807.

    Miscellaneous databases

    NextBioi 285060.
    PROi Q06194.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06194.
    Bgeei Q06194.
    CleanExi MM_F8.
    Genevestigatori Q06194.

    Family and domain databases

    Gene3Di 2.60.120.260. 2 hits.
    2.60.40.420. 6 hits.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR024715. Factor_5/8.
    IPR014707. Factor_8.
    IPR008979. Galactose-bd-like.
    [Graphical view ]
    PANTHERi PTHR10127:SF50. PTHR10127:SF50. 1 hit.
    Pfami PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 2 hits.
    PF00754. F5_F8_type_C. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000354. Factors_V_VIII. 1 hit.
    SMARTi SM00231. FA58C. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 6 hits.
    SSF49785. SSF49785. 2 hits.
    PROSITEi PS01285. FA58C_1. 2 hits.
    PS01286. FA58C_2. 2 hits.
    PS50022. FA58C_3. 2 hits.
    PS00079. MULTICOPPER_OXIDASE1. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the murine factor VIII cDNA."
      Elder B., Lakich D., Gitschier J.
      Genomics 16:374-379(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiFA8_MOUSE
    AccessioniPrimary (citable) accession number: Q06194
    Secondary accession number(s): A2AN88
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3