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O08689

- GDF8_MOUSE

UniProt

O08689 - GDF8_MOUSE

Protein

Growth/differentiation factor 8

Gene

Mstn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Acts specifically as a negative regulator of skeletal muscle growth.

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. receptor binding Source: MGI

    GO - Biological processi

    1. cellular response to dexamethasone stimulus Source: MGI
    2. negative regulation of muscle hypertrophy Source: Ensembl
    3. negative regulation of skeletal muscle tissue growth Source: Ensembl
    4. ovulation cycle process Source: Ensembl
    5. positive regulation of transcription, DNA-templated Source: Ensembl
    6. response to electrical stimulus Source: Ensembl
    7. response to estrogen Source: Ensembl
    8. response to ethanol Source: Ensembl
    9. response to gravity Source: Ensembl
    10. response to heat Source: Ensembl
    11. response to muscle activity Source: Ensembl
    12. response to testosterone Source: Ensembl
    13. skeletal muscle atrophy Source: Ensembl
    14. skeletal muscle tissue regeneration Source: Ensembl
    15. transforming growth factor beta receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Cytokine, Growth factor

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Growth/differentiation factor 8
    Short name:
    GDF-8
    Alternative name(s):
    Myostatin
    Gene namesi
    Name:Mstn
    Synonyms:Gdf8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:95691. Mstn.

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular space Source: UniProtKB-KW

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mutant animals exhibit muscle hypertrophy.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 267243Sequence AnalysisPRO_0000033956Add
    BLAST
    Chaini268 – 376109Growth/differentiation factor 8PRO_0000033957Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi72 – 721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi282 ↔ 341
    Disulfide bondi310 ↔ 373
    Disulfide bondi314 ↔ 375
    Disulfide bondi340 – 340Interchain

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO08689.
    PRIDEiO08689.

    PTM databases

    PhosphoSiteiO08689.

    Expressioni

    Tissue specificityi

    Expressed specifically in developing and adult skeletal muscle. Weak expression in adipose tissue.

    Developmental stagei

    First detected 9.5 dpc in one-third of developing somites. At 10.5 dpc, expressed in the myotome compartment of somites. At later stages of development, detected in a wide range of developing muscles. Expression continues in adulthood.

    Gene expression databases

    ArrayExpressiO08689.
    BgeeiO08689.
    CleanExiMM_MSTN.
    GenevestigatoriO08689.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked By similarity. Interacts with WFIKKN2, leading to inhibit its activity. Interacts with FST3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201535. 1 interaction.
    IntActiO08689. 4 interactions.
    MINTiMINT-7914794.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi281 – 2855
    Beta strandi288 – 2903
    Helixi291 – 2944
    Beta strandi299 – 3013
    Beta strandi303 – 3064
    Beta strandi309 – 3113
    Turni316 – 3194
    Helixi324 – 3318
    Beta strandi340 – 35415
    Beta strandi360 – 37617

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3HH2X-ray2.15A/B268-376[»]
    3SEKX-ray2.40B268-376[»]
    ProteinModelPortaliO08689.
    SMRiO08689. Positions 50-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08689.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TGF-beta family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG310007.
    HOGENOMiHOG000006566.
    HOVERGENiHBG000217.
    InParanoidiO08689.
    KOiK05497.
    OMAiNPFLEVR.
    OrthoDBiEOG74R1Q4.
    PhylomeDBiO08689.
    TreeFamiTF318514.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR029034. Cystine-knot_cytokine.
    IPR015616. GDF_8.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view]
    PANTHERiPTHR11848. PTHR11848. 1 hit.
    PTHR11848:SF13. PTHR11848:SF13. 1 hit.
    PfamiPF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view]
    SMARTiSM00204. TGFB. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O08689-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMQKLQMYVY IYLFMLIAAG PVDLNEGSER EENVEKEGLC NACAWRQNTR    50
    YSRIEAIKIQ ILSKLRLETA PNISKDAIRQ LLPRAPPLRE LIDQYDVQRD 100
    DSSDGSLEDD DYHATTETII TMPTESDFLM QADGKPKCCF FKFSSKIQYN 150
    KVVKAQLWIY LRPVKTPTTV FVQILRLIKP MKDGTRYTGI RSLKLDMSPG 200
    TGIWQSIDVK TVLQNWLKQP ESNLGIEIKA LDENGHDLAV TFPGPGEDGL 250
    NPFLEVKVTD TPKRSRRDFG LDCDEHSTES RCCRYPLTVD FEAFGWDWII 300
    APKRYKANYC SGECEFVFLQ KYPHTHLVHQ ANPRGSAGPC CTPTKMSPIN 350
    MLYFNGKEQI IYGKIPAMVV DRCGCS 376
    Length:376
    Mass (Da):42,921
    Last modified:July 1, 1997 - v1
    Checksum:i3E19814DD62C08BE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U84005 mRNA. Translation: AAC53167.1.
    CCDSiCCDS14950.1.
    RefSeqiNP_034964.1. NM_010834.2.
    UniGeneiMm.3514.

    Genome annotation databases

    EnsembliENSMUST00000027269; ENSMUSP00000027269; ENSMUSG00000026100.
    GeneIDi17700.
    KEGGimmu:17700.
    UCSCiuc007ayt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U84005 mRNA. Translation: AAC53167.1 .
    CCDSi CCDS14950.1.
    RefSeqi NP_034964.1. NM_010834.2.
    UniGenei Mm.3514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HH2 X-ray 2.15 A/B 268-376 [» ]
    3SEK X-ray 2.40 B 268-376 [» ]
    ProteinModelPortali O08689.
    SMRi O08689. Positions 50-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201535. 1 interaction.
    IntActi O08689. 4 interactions.
    MINTi MINT-7914794.

    PTM databases

    PhosphoSitei O08689.

    Proteomic databases

    PaxDbi O08689.
    PRIDEi O08689.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027269 ; ENSMUSP00000027269 ; ENSMUSG00000026100 .
    GeneIDi 17700.
    KEGGi mmu:17700.
    UCSCi uc007ayt.1. mouse.

    Organism-specific databases

    CTDi 2660.
    MGIi MGI:95691. Mstn.

    Phylogenomic databases

    eggNOGi NOG310007.
    HOGENOMi HOG000006566.
    HOVERGENi HBG000217.
    InParanoidi O08689.
    KOi K05497.
    OMAi NPFLEVR.
    OrthoDBi EOG74R1Q4.
    PhylomeDBi O08689.
    TreeFami TF318514.

    Miscellaneous databases

    EvolutionaryTracei O08689.
    NextBioi 292290.
    PROi O08689.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08689.
    Bgeei O08689.
    CleanExi MM_MSTN.
    Genevestigatori O08689.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR029034. Cystine-knot_cytokine.
    IPR015616. GDF_8.
    IPR001839. TGF-b_C.
    IPR001111. TGF-b_N.
    IPR015615. TGF-beta-rel.
    IPR017948. TGFb_CS.
    [Graphical view ]
    PANTHERi PTHR11848. PTHR11848. 1 hit.
    PTHR11848:SF13. PTHR11848:SF13. 1 hit.
    Pfami PF00019. TGF_beta. 1 hit.
    PF00688. TGFb_propeptide. 1 hit.
    [Graphical view ]
    SMARTi SM00204. TGFB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00250. TGF_BETA_1. 1 hit.
    PS51362. TGF_BETA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member."
      McPherron A.C., Lawler A.M., Lee S.-J.
      Nature 387:83-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: CD-1.
      Tissue: Skeletal muscle.
    2. "Regulation of myostatin in vivo by growth and differentiation factor-associated serum protein-1: a novel protein with protease inhibitor and follistatin domains."
      Hill J.J., Qiu Y., Hewick R.M., Wolfman N.M.
      Mol. Endocrinol. 17:1144-1154(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WFIKKN2.
    3. Cited for: DISRUPTION PHENOTYPE.
    4. "The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding."
      Cash J.N., Rejon C.A., McPherron A.C., Bernard D.J., Thompson T.B.
      EMBO J. 28:2662-2676(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 268-376 IN COMPLEX WITH HUMAN FOLLISTATIN, HEPARIN-BINDING, DISULFIDE BONDS.
    5. "Structure of myostatin.follistatin-like 3: N-terminal domains of follistatin-type molecules exhibit alternate modes of binding."
      Cash J.N., Angerman E.B., Kattamuri C., Nolan K., Zhao H., Sidis Y., Keutmann H.T., Thompson T.B.
      J. Biol. Chem. 287:1043-1053(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 268-376 IN COMPLEX WITH HUMAN FSTL3, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGDF8_MOUSE
    AccessioniPrimary (citable) accession number: O08689
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 107 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3