GDF8_BUBBU
ID GDF8_BUBBU Reviewed; 375 AA.
AC Q6X5V1; Q4JH08;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Growth/differentiation factor 8;
DE Short=GDF-8;
DE AltName: Full=Myostatin;
DE Flags: Precursor;
GN Name=MSTN; Synonyms=GDF8;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mota L.S.L.S., Curi R.A., Palmieri D.A., Braga G.U.L., Borges A.S.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Murrah;
RA Vijh R.K., Bharani Kumar S.T., Mishra B., Tantia M.S.;
RT "Myostatin exon 3 in Murrah buffaloes.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Vijh R.K., Bharani Kumar S.T., Mishra B., Tantia M.S.;
RT "Myostatin (GDF8) gene of Bubalus bubalis.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Mishra B., Vijh R.K., Tantia M.S., Bharani Kumar S.T.;
RT "Myostatin mRNA of Bubalus bubalis.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC growth. {ECO:0000250|UniProtKB:O08689}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with WFIKKN2, leading
CC to inhibit its activity. Interacts with FSTL3.
CC {ECO:0000250|UniProtKB:O08689}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
CC -!- PTM: Synthesized as large precursor molecule that undergoes proteolytic
CC cleavage to generate an N-terminal propeptide and a disulfide linked C-
CC terminal dimer, which is the biologically active molecule. The
CC circulating form consists of a latent complex of the C-terminal dimer
CC and other proteins, including its propeptide, which maintain the C-
CC terminal dimer in a latent, inactive state. Ligand activation requires
CC additional cleavage of the prodomain by a tolloid-like
CC metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; AY254098; AAQ98602.1; -; Genomic_DNA.
DR EMBL; AY363177; AAQ98602.1; JOINED; Genomic_DNA.
DR EMBL; AY363178; AAQ98602.1; JOINED; Genomic_DNA.
DR EMBL; AY854497; AAW50584.1; -; Genomic_DNA.
DR EMBL; AY854495; AAW50584.1; JOINED; Genomic_DNA.
DR EMBL; AY854496; AAW50584.1; JOINED; Genomic_DNA.
DR EMBL; DQ091762; AAY98351.1; -; Genomic_DNA.
DR EMBL; DQ159987; AAZ86073.1; -; mRNA.
DR RefSeq; NP_001277896.1; NM_001290967.1.
DR AlphaFoldDB; Q6X5V1; -.
DR SMR; Q6X5V1; -.
DR GeneID; 102414042; -.
DR KEGG; bbub:102414042; -.
DR CTD; 2660; -.
DR OrthoDB; 892873at2759; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISS:UniProtKB.
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; Heparin-binding; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..266
FT /evidence="ECO:0000255"
FT /id="PRO_0000033938"
FT CHAIN 267..375
FT /note="Growth/differentiation factor 8"
FT /id="PRO_0000033939"
FT SITE 98..99
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O08689"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..282
FT /evidence="ECO:0000250|UniProtKB:O14793"
FT DISULFID 281..340
FT /evidence="ECO:0000250|UniProtKB:O14793"
FT DISULFID 309..372
FT /evidence="ECO:0000250|UniProtKB:O14793"
FT DISULFID 313..374
FT /evidence="ECO:0000250|UniProtKB:O14793"
FT DISULFID 339
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:O14793"
SQ SEQUENCE 375 AA; 42496 MW; B1285708CFD1B221 CRC64;
MQKLQISVYI YLFMLIVAGP VDLNENSEQK ENVEKEGLCN ACLWRENTTS SRLEAIKIQI
LSKLRLETAP NISKDAIRQL LPKAPPLLEL IDQFDVQRDA GSDGSLEDDD YHARTDAVIT
MPTESDLLTQ VEGKPKCCFF QFSSKIQYNK LVKAQLWIYL RPVKTPATVF VQILRLIKPM
KDGTRYTGIR SLKLDMNPGT GIWQSIDVKT VLQNWLKQPE SNLGIEIKAL DENGHDLAVT
FPEPGEDGLT PFLEVKVTDT PKRSRRDFGL DCDERSTESR CCRYPLTVDF EAFGWDWIIA
PKRYKANYCS GECEFVFLQK YPHTHLVHQA NPRGSAGPCC TPTKMSPINM LYFNGEGQII
YGKIPAMVVD RCGCS
