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GDF8_DANRE
ID   GDF8_DANRE              Reviewed;         374 AA.
AC   O42222; B0S643; Q7T1K5; Q8JFS0; Q8UUR8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Growth/differentiation factor 8;
DE            Short=GDF-8;
DE   AltName: Full=Myostatin;
DE   AltName: Full=Myostatin-1;
DE            Short=zfMSTN-1;
DE   AltName: Full=Myostatin-B;
DE   Flags: Precursor;
GN   Name=mstnb; Synonyms=gdf8, mstn, mstn-1; ORFNames=si:ch211-3o3.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=9356471; DOI=10.1073/pnas.94.23.12457;
RA   McPherron A.C., Lee S.-J.;
RT   "Double muscling in cattle due to mutations in the myostatin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:12457-12461(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=14555747; DOI=10.1242/jeb.00635;
RA   Xu C., Wu G., Zohar Y., Du S.-J.;
RT   "Analysis of myostatin gene structure, expression and function in
RT   zebrafish.";
RL   J. Exp. Biol. 206:4067-4079(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ko Y.-L., Lu J.-K., Wu J.-L.;
RT   "Molecular cloning and characterization of myostatin (double muscle gene)
RT   in various aquatic organisms.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Amali A.A., Lin C.J.-F., Gong H.-Y., Ko Y.-L., Lu J.-K., Wu J.-L.;
RT   "Pattern and tissue distribution of myostatin-1 in zebrafish embryo.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-33, DEVELOPMENTAL STAGE, AND INDUCTION.
RC   TISSUE=Liver;
RX   PubMed=12525249; DOI=10.1677/joe.0.1760047;
RA   Vianello S., Brazzoduro L., Dalla Valle L., Belvedere P., Colombo L.;
RT   "Myostatin expression during development and chronic stress in zebrafish
RT   (Danio rerio).";
RL   J. Endocrinol. 176:47-59(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=12596043; DOI=10.1007/s00441-002-0668-y;
RA   Radaelli G., Rowlerson A., Mascarello F., Patruno M., Funkenstein B.;
RT   "Myostatin precursor is present in several tissues in teleost fish: a
RT   comparative immunolocalization study.";
RL   Cell Tissue Res. 311:239-250(2003).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15042708; DOI=10.1002/dvdy.10454;
RA   Amali A.A., Lin C.J.-F., Chen Y.-H., Wang W.-L., Gong H.-Y., Lee C.-Y.,
RA   Ko Y.-L., Lu J.-K., Her G.M., Chen T.T., Wu J.-L.;
RT   "Up-regulation of muscle-specific transcription factors during embryonic
RT   somitogenesis of zebrafish (Danio rerio) by knock-down of myostatin-1.";
RL   Dev. Dyn. 229:847-856(2004).
RN   [9]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16174033; DOI=10.1111/j.1525-142x.2005.05044.x;
RA   Kerr T., Roalson E.H., Rodgers B.D.;
RT   "Phylogenetic analysis of the myostatin gene sub-family and the
RT   differential expression of a novel member in zebrafish.";
RL   Evol. Dev. 7:390-400(2005).
RN   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16005092; DOI=10.1016/j.jbiotec.2005.04.023;
RA   Acosta J., Carpio Y., Borroto I., Gonzalez O., Estrada M.P.;
RT   "Myostatin gene silenced by RNAi show a zebrafish giant phenotype.";
RL   J. Biotechnol. 119:324-331(2005).
RN   [11]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=17289047; DOI=10.1016/j.ygcen.2006.12.023;
RA   Helterline D.L.I., Garikipati D., Stenkamp D.L., Rodgers B.D.;
RT   "Embryonic and tissue-specific regulation of myostatin-1 and -2 gene
RT   expression in zebrafish.";
RL   Gen. Comp. Endocrinol. 151:90-97(2007).
CC   -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC       growth. May down-regulate muscle-specific transcription factors such as
CC       myod and myog. {ECO:0000269|PubMed:14555747,
CC       ECO:0000269|PubMed:15042708, ECO:0000269|PubMed:16005092}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in muscle. At hatching,
CC       expression is strongest in the skin epithelium, and is also found in
CC       the retina and brain. From day 28, expressed in skeletal muscle. In the
CC       adult, highest expression is seen in the gastrointestinal tract, brain,
CC       muscle, heart and testis. Also expressed in the adult pharynx, kidney,
CC       spleen, liver, gill, eyes, skin, swim bladder and ovary.
CC       {ECO:0000269|PubMed:12596043, ECO:0000269|PubMed:15042708,
CC       ECO:0000269|PubMed:17289047}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Weakly
CC       expressed ubiquitously in early stage embryos. Present transiently in
CC       the blastula with levels dropping almost completely during
CC       gastrulation. Expression peaks during late somitogenesis, decreases at
CC       the end of somitogenesis, and then rises again at and after hatching.
CC       Strongly expressed in swimming larvae, juveniles and adults.
CC       {ECO:0000269|PubMed:12525249, ECO:0000269|PubMed:14555747,
CC       ECO:0000269|PubMed:15042708, ECO:0000269|PubMed:16174033,
CC       ECO:0000269|PubMed:17289047}.
CC   -!- INDUCTION: Repressed in adult muscle, and stimulated in adult spleen,
CC       when fish are grown in overcrowded conditions.
CC       {ECO:0000269|PubMed:12525249, ECO:0000269|PubMed:17289047}.
CC   -!- DISRUPTION PHENOTYPE: Defects produce a giant phenotype.
CC       {ECO:0000269|PubMed:16005092}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; AF019626; AAB86693.1; -; mRNA.
DR   EMBL; AY323521; AAP85526.1; -; Genomic_DNA.
DR   EMBL; AF540956; AAQ11222.1; -; mRNA.
DR   EMBL; AY258034; AAP13068.1; -; mRNA.
DR   EMBL; AL672217; CAD43439.1; -; Genomic_DNA.
DR   EMBL; BX323586; CAQ13470.1; -; Genomic_DNA.
DR   EMBL; AJ318758; CAC86466.1; -; mRNA.
DR   RefSeq; NP_571094.2; NM_131019.5.
DR   AlphaFoldDB; O42222; -.
DR   SMR; O42222; -.
DR   BioGRID; 663041; 2.
DR   STRING; 7955.ENSDARP00000091159; -.
DR   PaxDb; O42222; -.
DR   Ensembl; ENSDART00000100386; ENSDARP00000091159; ENSDARG00000069133.
DR   GeneID; 798441; -.
DR   KEGG; dre:798441; -.
DR   CTD; 798441; -.
DR   ZFIN; ZDB-GENE-990415-165; mstnb.
DR   eggNOG; KOG3900; Eukaryota.
DR   GeneTree; ENSGT00940000165813; -.
DR   HOGENOM; CLU_020515_6_1_1; -.
DR   InParanoid; O42222; -.
DR   OMA; TDQCATC; -.
DR   OrthoDB; 892873at2759; -.
DR   PhylomeDB; O42222; -.
DR   TreeFam; TF318514; -.
DR   PRO; PR:O42222; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 9.
DR   Bgee; ENSDARG00000069133; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IDA:ZFIN.
DR   GO; GO:0110021; P:cardiac muscle myoblast proliferation; IMP:ZFIN.
DR   GO; GO:0006955; P:immune response; IMP:ZFIN.
DR   GO; GO:0007517; P:muscle organ development; IDA:ZFIN.
DR   GO; GO:0110023; P:negative regulation of cardiac muscle myoblast proliferation; IMP:ZFIN.
DR   GO; GO:0045926; P:negative regulation of growth; IDA:UniProtKB.
DR   GO; GO:0045967; P:negative regulation of growth rate; IDA:ZFIN.
DR   GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IMP:ZFIN.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; IDA:UniProtKB.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0014738; P:regulation of muscle hyperplasia; IMP:ZFIN.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IDA:ZFIN.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:ZFIN.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR015616; GDF_8.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   PANTHER; PTHR11848:SF150; PTHR11848:SF150; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 1.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..265
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000033976"
FT   CHAIN           266..374
FT                   /note="Growth/differentiation factor 8"
FT                   /id="PRO_0000033977"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        274
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        271..281
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        280..339
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..371
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..373
FT                   /evidence="ECO:0000250"
FT   DISULFID        338
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="Q -> L (in Ref. 1; AAB86693, 2; AAP85526, 3;
FT                   AAQ11222 and 4; AAP13068)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        204
FT                   /note="S -> G (in Ref. 2; AAP85526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="S -> G (in Ref. 2; AAP85526)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        367
FT                   /note="Missing (in Ref. 2; AAP85526)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42075 MW;  6E3B87A48E6E2172 CRC64;
     MHFTQVLISL SVLIACGPVG YGDITAHQQP STATEESEQC STCEFRQHSK LMRLHAIKSQ
     ILSKLRLKQA PNISRDVVKQ LLPKAPPLQQ LLDQYDVLGD DSKDGAVEED DEHATTETIM
     TMATEPDPIV QVDRKPKCCF FSFSPKIQAN RIVRAQLWVH LRPAEEATTV FLQISRLMPV
     KDGGRHRIRS LKIDVNAGVT SWQSIDVKQV LTVWLKQPET NRGIEINAYD AKGNDLAVTS
     TETGEDGLLP FMEVKISEGP KRIRRDSGLD CDENSSESRC CRYPLTVDFE DFGWDWIIAP
     KRYKANYCSG ECDYMYLQKY PHTHLVNKAS PRGTAGPCCT PTKMSPINML YFNGKEQIIY
     GKIPSMVVDR CGCS
 
 
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