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Protein

Growth/differentiation factor 8

Gene

mstnb

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Acts specifically as a negative regulator of skeletal muscle growth. May down-regulate muscle-specific transcription factors such as myod and myog.3 Publications

GO - Molecular functioni

  • growth factor activity Source: UniProtKB

GO - Biological processi

  • growth Source: InterPro
  • muscle organ development Source: ZFIN
  • negative regulation of growth Source: UniProtKB
  • negative regulation of growth rate Source: ZFIN
  • negative regulation of striated muscle tissue development Source: UniProtKB
  • skeletal muscle tissue development Source: ZFIN
  • transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Growth factor

Names & Taxonomyi

Protein namesi
Recommended name:
Growth/differentiation factor 8
Short name:
GDF-8
Alternative name(s):
Myostatin
Myostatin-1
Short name:
zfMSTN-1
Myostatin-B
Gene namesi
Name:mstnb
Synonyms:gdf8, mstn, mstn-1
ORF Names:si:ch211-3o3.2
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Chromosome 9

Organism-specific databases

ZFINiZDB-GENE-990415-165. mstnb.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Defects produce a giant phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 265243Sequence analysisPRO_0000033976Add
BLAST
Chaini266 – 374109Growth/differentiation factor 8PRO_0000033977Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi280 ↔ 339By similarity
Disulfide bondi308 ↔ 371By similarity
Disulfide bondi312 ↔ 373By similarity
Disulfide bondi338 – 338InterchainBy similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO42222.
PRIDEiO42222.

Expressioni

Tissue specificityi

Predominantly expressed in muscle. At hatching, expression is strongest in the skin epithelium, and is also found in the retina and brain. From day 28, expressed in skeletal muscle. In the adult, highest expression is seen in the gastrointestinal tract, brain, muscle, heart and testis. Also expressed in the adult pharynx, kidney, spleen, liver, gill, eyes, skin, swim bladder and ovary.3 Publications

Developmental stagei

Expressed both maternally and zygotically. Weakly expressed ubiquitously in early stage embryos. Present transiently in the blastula with levels dropping almost completely during gastrulation. Expression peaks during late somitogenesis, decreases at the end of somitogenesis, and then rises again at and after hatching. Strongly expressed in swimming larvae, juveniles and adults.5 Publications

Inductioni

Repressed in adult muscle, and stimulated in adult spleen, when fish are grown in overcrowded conditions.2 Publications

Gene expression databases

BgeeiO42222.
ExpressionAtlasiO42222. differential.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

GO - Molecular functioni

  • growth factor activity Source: UniProtKB

Protein-protein interaction databases

BioGridi663041. 2 interactions.
STRINGi7955.ENSDARP00000091159.

Structurei

3D structure databases

ProteinModelPortaliO42222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TGF-beta family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000006566.
HOVERGENiHBG000217.
InParanoidiO42222.
KOiK05497.
OMAiFMEVKIS.
OrthoDBiEOG74R1Q4.
PhylomeDBiO42222.
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:SF150. PTHR11848:SF150. 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.

O42222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHFTQVLISL SVLIACGPVG YGDITAHQQP STATEESEQC STCEFRQHSK
60 70 80 90 100
LMRLHAIKSQ ILSKLRLKQA PNISRDVVKQ LLPKAPPLQQ LLDQYDVLGD
110 120 130 140 150
DSKDGAVEED DEHATTETIM TMATEPDPIV QVDRKPKCCF FSFSPKIQAN
160 170 180 190 200
RIVRAQLWVH LRPAEEATTV FLQISRLMPV KDGGRHRIRS LKIDVNAGVT
210 220 230 240 250
SWQSIDVKQV LTVWLKQPET NRGIEINAYD AKGNDLAVTS TETGEDGLLP
260 270 280 290 300
FMEVKISEGP KRIRRDSGLD CDENSSESRC CRYPLTVDFE DFGWDWIIAP
310 320 330 340 350
KRYKANYCSG ECDYMYLQKY PHTHLVNKAS PRGTAGPCCT PTKMSPINML
360 370
YFNGKEQIIY GKIPSMVVDR CGCS
Length:374
Mass (Da):42,075
Last modified:November 24, 2009 - v2
Checksum:i6E3B87A48E6E2172
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391Q → L in AAB86693 (PubMed:9356471).Curated
Sequence conflicti39 – 391Q → L in AAP85526 (PubMed:14555747).Curated
Sequence conflicti39 – 391Q → L in AAQ11222 (Ref. 3) Curated
Sequence conflicti39 – 391Q → L in AAP13068 (Ref. 4) Curated
Sequence conflicti204 – 2041S → G in AAP85526 (PubMed:14555747).Curated
Sequence conflicti330 – 3301S → G in AAP85526 (PubMed:14555747).Curated
Sequence conflicti367 – 3671Missing in AAP85526 (PubMed:14555747).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019626 mRNA. Translation: AAB86693.1.
AY323521 Genomic DNA. Translation: AAP85526.1.
AF540956 mRNA. Translation: AAQ11222.1.
AY258034 mRNA. Translation: AAP13068.1.
AL672217 Genomic DNA. Translation: CAD43439.1.
BX323586 Genomic DNA. Translation: CAQ13470.1.
AJ318758 mRNA. Translation: CAC86466.1.
RefSeqiNP_571094.1. NM_131019.4.
UniGeneiDr.75782.

Genome annotation databases

EnsembliENSDART00000100386; ENSDARP00000091159; ENSDARG00000069133.
GeneIDi798441.
KEGGidre:798441.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019626 mRNA. Translation: AAB86693.1.
AY323521 Genomic DNA. Translation: AAP85526.1.
AF540956 mRNA. Translation: AAQ11222.1.
AY258034 mRNA. Translation: AAP13068.1.
AL672217 Genomic DNA. Translation: CAD43439.1.
BX323586 Genomic DNA. Translation: CAQ13470.1.
AJ318758 mRNA. Translation: CAC86466.1.
RefSeqiNP_571094.1. NM_131019.4.
UniGeneiDr.75782.

3D structure databases

ProteinModelPortaliO42222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi663041. 2 interactions.
STRINGi7955.ENSDARP00000091159.

Proteomic databases

PaxDbiO42222.
PRIDEiO42222.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000100386; ENSDARP00000091159; ENSDARG00000069133.
GeneIDi798441.
KEGGidre:798441.

Organism-specific databases

CTDi798441.
ZFINiZDB-GENE-990415-165. mstnb.

Phylogenomic databases

eggNOGiKOG3900. Eukaryota.
ENOG410XT8Z. LUCA.
GeneTreeiENSGT00760000119112.
HOGENOMiHOG000006566.
HOVERGENiHBG000217.
InParanoidiO42222.
KOiK05497.
OMAiFMEVKIS.
OrthoDBiEOG74R1Q4.
PhylomeDBiO42222.
TreeFamiTF318514.

Miscellaneous databases

NextBioi20933414.
PROiO42222.

Gene expression databases

BgeeiO42222.
ExpressionAtlasiO42222. differential.

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:SF150. PTHR11848:SF150. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Double muscling in cattle due to mutations in the myostatin gene."
    McPherron A.C., Lee S.-J.
    Proc. Natl. Acad. Sci. U.S.A. 94:12457-12461(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Analysis of myostatin gene structure, expression and function in zebrafish."
    Xu C., Wu G., Zohar Y., Du S.-J.
    J. Exp. Biol. 206:4067-4079(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
  3. "Molecular cloning and characterization of myostatin (double muscle gene) in various aquatic organisms."
    Ko Y.-L., Lu J.-K., Wu J.-L.
    Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Pattern and tissue distribution of myostatin-1 in zebrafish embryo."
    Amali A.A., Lin C.J.-F., Gong H.-Y., Ko Y.-L., Lu J.-K., Wu J.-L.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The zebrafish reference genome sequence and its relationship to the human genome."
    Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.
    , White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G., Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.
    Nature 496:498-503(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuebingen.
  6. "Myostatin expression during development and chronic stress in zebrafish (Danio rerio)."
    Vianello S., Brazzoduro L., Dalla Valle L., Belvedere P., Colombo L.
    J. Endocrinol. 176:47-59(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-33, DEVELOPMENTAL STAGE, INDUCTION.
    Tissue: Liver.
  7. "Myostatin precursor is present in several tissues in teleost fish: a comparative immunolocalization study."
    Radaelli G., Rowlerson A., Mascarello F., Patruno M., Funkenstein B.
    Cell Tissue Res. 311:239-250(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Up-regulation of muscle-specific transcription factors during embryonic somitogenesis of zebrafish (Danio rerio) by knock-down of myostatin-1."
    Amali A.A., Lin C.J.-F., Chen Y.-H., Wang W.-L., Gong H.-Y., Lee C.-Y., Ko Y.-L., Lu J.-K., Her G.M., Chen T.T., Wu J.-L.
    Dev. Dyn. 229:847-856(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "Phylogenetic analysis of the myostatin gene sub-family and the differential expression of a novel member in zebrafish."
    Kerr T., Roalson E.H., Rodgers B.D.
    Evol. Dev. 7:390-400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  10. "Myostatin gene silenced by RNAi show a zebrafish giant phenotype."
    Acosta J., Carpio Y., Borroto I., Gonzalez O., Estrada M.P.
    J. Biotechnol. 119:324-331(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "Embryonic and tissue-specific regulation of myostatin-1 and -2 gene expression in zebrafish."
    Helterline D.L.I., Garikipati D., Stenkamp D.L., Rodgers B.D.
    Gen. Comp. Endocrinol. 151:90-97(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.

Entry informationi

Entry nameiGDF8_DANRE
AccessioniPrimary (citable) accession number: O42222
Secondary accession number(s): B0S643
, Q7T1K5, Q8JFS0, Q8UUR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 24, 2009
Last modified: May 11, 2016
This is version 117 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.