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O08689 (GDF8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth/differentiation factor 8

Short name=GDF-8
Alternative name(s):
Myostatin
Gene names
Name:Mstn
Synonyms:Gdf8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts specifically as a negative regulator of skeletal muscle growth.

Subunit structure

Homodimer; disulfide-linked By similarity. Interacts with WFIKKN2, leading to inhibit its activity. Interacts with FST3 By similarity. Ref.2 Ref.4 Ref.5

Subcellular location

Secreted By similarity.

Tissue specificity

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

Developmental stage

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.

Disruption phenotype

Mutant animals exhibit muscle hypertrophy.

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandHeparin-binding
   Molecular functionCytokine
Growth factor
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle tissue growth

Inferred from electronic annotation. Source: Ensembl

ovulation cycle process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to gravity

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to muscle activity

Inferred from electronic annotation. Source: Ensembl

response to testosterone

Inferred from electronic annotation. Source: Ensembl

skeletal muscle atrophy

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue regeneration

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.2. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor binding

Inferred from physical interaction PubMed 11459935. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 267243 Potential
PRO_0000033956
Chain268 – 376109Growth/differentiation factor 8
PRO_0000033957

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Disulfide bond282 ↔ 341 Ref.4 Ref.5
Disulfide bond310 ↔ 373 Ref.4 Ref.5
Disulfide bond314 ↔ 375 Ref.4 Ref.5
Disulfide bond340Interchain Ref.4 Ref.5

Secondary structure

................... 376
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O08689 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 3E19814DD62C08BE

FASTA37642,921
        10         20         30         40         50         60 
MMQKLQMYVY IYLFMLIAAG PVDLNEGSER EENVEKEGLC NACAWRQNTR YSRIEAIKIQ 

        70         80         90        100        110        120 
ILSKLRLETA PNISKDAIRQ LLPRAPPLRE LIDQYDVQRD DSSDGSLEDD DYHATTETII 

       130        140        150        160        170        180 
TMPTESDFLM QADGKPKCCF FKFSSKIQYN KVVKAQLWIY LRPVKTPTTV FVQILRLIKP 

       190        200        210        220        230        240 
MKDGTRYTGI RSLKLDMSPG TGIWQSIDVK TVLQNWLKQP ESNLGIEIKA LDENGHDLAV 

       250        260        270        280        290        300 
TFPGPGEDGL NPFLEVKVTD TPKRSRRDFG LDCDEHSTES RCCRYPLTVD FEAFGWDWII 

       310        320        330        340        350        360 
APKRYKANYC SGECEFVFLQ KYPHTHLVHQ ANPRGSAGPC CTPTKMSPIN MLYFNGKEQI 

       370 
IYGKIPAMVV DRCGCS 

« Hide

References

[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]"BMP signaling controls muscle mass."
Sartori R., Schirwis E., Blaauw B., Bortolanza S., Zhao J., Enzo E., Stantzou A., Mouisel E., Toniolo L., Ferry A., Stricker S., Goldberg A.L., Dupont S., Piccolo S., Amthor H., Sandri M.
Nat. Genet. 45:1309-1318(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U84005 mRNA. Translation: AAC53167.1.
RefSeqNP_034964.1. NM_010834.2.
UniGeneMm.3514.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HH2X-ray2.15A/B268-376[»]
3SEKX-ray2.40B268-376[»]
ProteinModelPortalO08689.
SMRO08689. Positions 50-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201535. 1 interaction.
IntActO08689. 4 interactions.
MINTMINT-7914794.

PTM databases

PhosphoSiteO08689.

Proteomic databases

PaxDbO08689.
PRIDEO08689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027269; ENSMUSP00000027269; ENSMUSG00000026100.
GeneID17700.
KEGGmmu:17700.
UCSCuc007ayt.1. mouse.

Organism-specific databases

CTD2660.
MGIMGI:95691. Mstn.

Phylogenomic databases

eggNOGNOG310007.
HOGENOMHOG000006566.
HOVERGENHBG000217.
InParanoidO08689.
KOK05497.
OMADLLMQVE.
OrthoDBEOG74R1Q4.
PhylomeDBO08689.
TreeFamTF318514.

Gene expression databases

ArrayExpressO08689.
BgeeO08689.
CleanExMM_MSTN.
GenevestigatorO08689.

Family and domain databases

InterProIPR015616. GDF_8.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PTHR11848:SF13. PTHR11848:SF13. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO08689.
NextBio292290.
PROO08689.
SOURCESearch...

Entry information

Entry nameGDF8_MOUSE
AccessionPrimary (citable) accession number: O08689
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot