Growth/differentiation factor 8 precursor

Contribute

Send feedback

Read comments (?) or add your own

O08689 (GDF8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Growth/differentiation factor 8
Short name=GDF-8

Alternative name(s):
Myostatin

Gene names

Name:	Mstn
Synonyms:	Gdf8

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.3 Ref.4
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.
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Heparin-binding
Molecular function	Cytokine Growth factor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of muscle hypertrophy Inferred from electronic annotation. Source: Compara negative regulation of skeletal muscle tissue growth Inferred from electronic annotation. Source: Compara ovulation cycle process Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to gravity Inferred from electronic annotation. Source: Compara response to heat Inferred from electronic annotation. Source: Compara response to muscle activity Inferred from electronic annotation. Source: Compara response to testosterone stimulus Inferred from electronic annotation. Source: Compara skeletal muscle atrophy Inferred from electronic annotation. Source: Compara skeletal muscle tissue regeneration Inferred from electronic annotation. Source: Compara transforming growth factor beta receptor signaling pathway Inferred from direct assay Ref.2. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Potential

Propeptide

25 – 267

243

Potential

PRO_0000033956

Chain

268 – 376

109

Growth/differentiation factor 8

PRO_0000033957

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Interchain Ref.3 Ref.4

Secondary structure

376

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O08689 [UniParc].

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

FASTA

376

42,921

        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]	"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.
[4]	"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.

IPI

IPI00114963.

RefSeq

NP_034964.1. NM_010834.2.

UniGene

Mm.3514.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HH2	X-ray	2.15	A/B	268-376	[»]
3SEK	X-ray	2.40	B	268-376	[»]

ProteinModelPortal

O08689.

SMR

O08689. Positions 50-376.

ModBase

Search...

Protein-protein interaction databases

IntAct

O08689. 2 interactions.

PTM databases

PhosphoSite

O08689.

Proteomic databases

PaxDb

O08689.

PRIDE

O08689.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000027269; ENSMUSP00000027269; ENSMUSG00000026100.

GeneID

17700.

KEGG

mmu:17700.

Organism-specific databases

CTD

2660.

MGI

MGI:95691. Mstn.

Phylogenomic databases

eggNOG

NOG310007.

HOGENOM

HOG000006566.

HOVERGEN

HBG000217.

InParanoid

O08689.

K05497.

OMA

DLLMQVE.

OrthoDB

EOG4ZS93B.

Gene expression databases

ArrayExpress

O08689.

Bgee

O08689.

CleanEx

MM_MSTN.

Genevestigator

O08689.

GermOnline

ENSMUSG00000026100. Mus musculus.

Family and domain databases

InterPro

IPR015616. GDF_8.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR015615. TGF-beta-rel.
IPR017948. TGFb_CS.
[Graphical view]

PANTHER

PTHR11848. PTHR11848. 1 hit.
PTHR11848:SF13. PTHR11848:SF13. 1 hit.

Pfam

PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]

SMART

SM00204. TGFB. 1 hit.
[Graphical view]

PROSITE

PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O08689.

NextBio

292290.

SOURCE

Search...

Entry information

Entry name

GDF8_MOUSE

Accession

Primary (citable) accession number: O08689

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents