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Q8K0E8

- FIBB_MOUSE

UniProt

Q8K0E8 - FIBB_MOUSE

Protein

Fibrinogen beta chain

Gene

Fgb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei34 – 352Cleavage; by thrombin; to release fibrinopeptide BBy similarity

    GO - Biological processi

    1. cellular response to interleukin-1 Source: Ensembl
    2. cellular response to leptin stimulus Source: Ensembl
    3. platelet activation Source: InterPro
    4. protein polymerization Source: InterPro
    5. response to calcium ion Source: Ensembl
    6. signal transduction Source: InterPro

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibrinogen beta chain
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Fgb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:99501. Fgb.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: Ensembl
    2. cell cortex Source: MGI
    3. external side of plasma membrane Source: Ensembl
    4. fibrinogen complex Source: InterPro
    5. platelet alpha granule Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Peptidei20 – 3415Fibrinopeptide BBy similarityPRO_0000009078Add
    BLAST
    Chaini35 – 481447Fibrinogen beta chainPRO_0000009077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi213 – 213Interchain (with alpha chain)PROSITE-ProRule annotation
    Disulfide bondi217 – 217Interchain (with gamma chain)PROSITE-ProRule annotation
    Disulfide bondi221 ↔ 306PROSITE-ProRule annotation
    Disulfide bondi231 ↔ 260PROSITE-ProRule annotation
    Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi414 ↔ 427PROSITE-ProRule annotation

    Post-translational modificationi

    Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8K0E8.
    PaxDbiQ8K0E8.
    PRIDEiQ8K0E8.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00279079.
    Q8K0E8.

    PTM databases

    PhosphoSiteiQ8K0E8.

    Expressioni

    Gene expression databases

    BgeeiQ8K0E8.
    CleanExiMM_FGB.
    GenevestigatoriQ8K0E8.

    Interactioni

    Subunit structurei

    Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ8K0E8. 5 interactions.
    MINTiMINT-1863241.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8K0E8.
    SMRiQ8K0E8. Positions 78-479.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini222 – 478257Fibrinogen C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 373Beta-chain polymerization, binding distal domain of another fibrinBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili149 – 21365Sequence AnalysisAdd
    BLAST

    Domaini

    A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure By similarity.By similarity

    Sequence similaritiesi

    Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal

    Phylogenomic databases

    eggNOGiNOG277105.
    GeneTreeiENSGT00750000117251.
    HOGENOMiHOG000059561.
    HOVERGENiHBG005707.
    InParanoidiQ8K0E8.
    KOiK03904.
    OMAiTIHNGMF.
    OrthoDBiEOG7X9G60.
    PhylomeDBiQ8K0E8.
    TreeFamiTF336658.

    Family and domain databases

    Gene3Di3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProiIPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR012290. Fibrinogen_a/b/g_coil_dom.
    IPR020837. Fibrinogen_CS.
    [Graphical view]
    PfamiPF08702. Fib_alpha. 1 hit.
    PF00147. Fibrinogen_C. 1 hit.
    [Graphical view]
    SMARTiSM00186. FBG. 1 hit.
    [Graphical view]
    SUPFAMiSSF56496. SSF56496. 1 hit.
    PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8K0E8-1 [UniParc]FASTAAdd to Basket

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    MRHLWLLLLL CVFSVQTQAA DDDYDEPTDS LDARGHRPVD RRKEEPPSLR    50
    PAPPPISGGG YRARPAKATA NQKKVERRPP DAGGCLHADT DMGVLCPTGC 100
    TLQQTLLNQE RPIKSSIAEL NNNIQSVSDT SSVTFQYLTL LKDMWKKKQA 150
    QVKENENVIN EYSSILEDQR LYIDETVNDN IPLNLRVLRS ILEDLRSKIQ 200
    KLESDISAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD 250
    TSIKPYRVYC DMKTENGGWT VIQNRQDGSV DFGRKWDPYK KGFGNIATNE 300
    DAKKYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT 350
    VQNEASKYQV SVNKYKGTAG NALMDGASQL VGENRTMTIH NGMFFSTYDR 400
    DNDGWVTTDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG LYSWDMSKHG 450
    TDDGVVWMNW KGSWYSMRRM SMKIRPFFPQ Q 481
    Length:481
    Mass (Da):54,753
    Last modified:October 1, 2002 - v1
    Checksum:i9902830CF708A155
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC031715 mRNA. Translation: AAH31715.1.
    AF413205 mRNA. Translation: AAL02225.1.
    CCDSiCCDS17432.1.
    RefSeqiNP_862897.1. NM_181849.2.
    UniGeneiMm.30063.

    Genome annotation databases

    EnsembliENSMUST00000048246; ENSMUSP00000039472; ENSMUSG00000033831.
    GeneIDi110135.
    KEGGimmu:110135.
    UCSCiuc008pph.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC031715 mRNA. Translation: AAH31715.1 .
    AF413205 mRNA. Translation: AAL02225.1 .
    CCDSi CCDS17432.1.
    RefSeqi NP_862897.1. NM_181849.2.
    UniGenei Mm.30063.

    3D structure databases

    ProteinModelPortali Q8K0E8.
    SMRi Q8K0E8. Positions 78-479.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8K0E8. 5 interactions.
    MINTi MINT-1863241.

    PTM databases

    PhosphoSitei Q8K0E8.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00279079.
    Q8K0E8.

    Proteomic databases

    MaxQBi Q8K0E8.
    PaxDbi Q8K0E8.
    PRIDEi Q8K0E8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000048246 ; ENSMUSP00000039472 ; ENSMUSG00000033831 .
    GeneIDi 110135.
    KEGGi mmu:110135.
    UCSCi uc008pph.1. mouse.

    Organism-specific databases

    CTDi 2244.
    MGIi MGI:99501. Fgb.

    Phylogenomic databases

    eggNOGi NOG277105.
    GeneTreei ENSGT00750000117251.
    HOGENOMi HOG000059561.
    HOVERGENi HBG005707.
    InParanoidi Q8K0E8.
    KOi K03904.
    OMAi TIHNGMF.
    OrthoDBi EOG7X9G60.
    PhylomeDBi Q8K0E8.
    TreeFami TF336658.

    Enzyme and pathway databases

    Reactomei REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi FGB. mouse.
    NextBioi 363391.
    PROi Q8K0E8.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8K0E8.
    CleanExi MM_FGB.
    Genevestigatori Q8K0E8.

    Family and domain databases

    Gene3Di 3.90.215.10. 1 hit.
    4.10.530.10. 1 hit.
    InterProi IPR014716. Fibrinogen_a/b/g_C_1.
    IPR014715. Fibrinogen_a/b/g_C_2.
    IPR002181. Fibrinogen_a/b/g_C_dom.
    IPR012290. Fibrinogen_a/b/g_coil_dom.
    IPR020837. Fibrinogen_CS.
    [Graphical view ]
    Pfami PF08702. Fib_alpha. 1 hit.
    PF00147. Fibrinogen_C. 1 hit.
    [Graphical view ]
    SMARTi SM00186. FBG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56496. SSF56496. 1 hit.
    PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
    PS51406. FIBRINOGEN_C_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Liver.
    2. "Mouse fibrinogen B-beta-chain."
      Murakawa M., Freeman M.W.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 234-469.

    Entry informationi

    Entry nameiFIBB_MOUSE
    AccessioniPrimary (citable) accession number: Q8K0E8
    Secondary accession number(s): Q91ZP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 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