ID   GDF8_OREMO              Reviewed;         376 AA.
AC   Q98TB4;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Growth/differentiation factor 8 {ECO:0000305};
DE   AltName: Full=Myostatin {ECO:0000303|PubMed:11250920};
DE            Short=MSTN {ECO:0000303|PubMed:11250920};
DE   Flags: Precursor;
GN   Name=gdf-8 {ECO:0000305};
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8127 {ECO:0000312|EMBL:AAK28706.1};
RN   [1] {ECO:0000312|EMBL:AAK28706.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND PHYLOGENETIC ANALYSIS.
RC   TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAK28706.1};
RX   PubMed=11250920; DOI=10.1210/endo.142.4.8097;
RA   Rodgers B.D., Weber G.M., Sullivan C.V., Levine M.A.;
RT   "Isolation and characterization of myostatin complementary deoxyribonucleic
RT   acid clones from two commercially important fish: Oreochromis mossambicus
RT   and Morone chrysops.";
RL   Endocrinology 142:1412-1418(2001).
CC   -!- FUNCTION: Acts specifically as a negative regulator of skeletal muscle
CC       growth. {ECO:0000250|UniProtKB:O42222}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:O08689}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC       ECO:0000269|PubMed:11250920}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in muscle. Also expressed in other
CC       tissues such as eye, gill, ovary, gut and brain. Very low level
CC       detected in testis. Not expressed in liver, kidney, stomach or heart.
CC       {ECO:0000269|PubMed:11250920}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases rapidly in whole body during
CC       embryonic and early larval development. However, the rate of expression
CC       decreases to plateau during yolk sac absorption. Expression not
CC       detected in fertilized oocytes and in prehatching larvae with eye
CC       spots. First detected in post-hatching larvae and peaks soon thereafter
CC       with the appearance of muscle activity coinciding with early
CC       myogenesis. {ECO:0000269|PubMed:11250920}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255,
CC       ECO:0000255|RuleBase:RU000354, ECO:0000305}.
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DR   EMBL; AF197193; AAK28706.1; -; mRNA.
DR   AlphaFoldDB; Q98TB4; -.
DR   SMR; Q98TB4; -.
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   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;
KW   Growth factor; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..267
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000438240"
FT   CHAIN           268..376
FT                   /note="Growth/differentiation factor 8"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004325050"
FT   DISULFID        273..283
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        282..341
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        310..373
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        314..375
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
FT   DISULFID        340
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:O08689"
SQ   SEQUENCE   376 AA;  42551 MW;  7C3469D1314B01E6 CRC64;
     MHLSQIVLYL SLLIALGPVV LSDQEAHQQP SVSTPVDTDQ CATCEVRQQI KTMRLNAIKS
     QILSKLRMKE APNISREIVK QLLPKAPPLQ QLLDQYDVLG DDNREEVLED DDEHATTETI
     VMVATEPDPA VQVDGQPKCC FFSITQKFQA SRVVRAQLWV HLRPSEEVTT VFLQISRLIP
     VTDGNRHIRS RSLKIDVNPG PASWQSIDVK QVLTVWLRQP ETNWGIEINA FDSRGNDLAV
     TSAEPGEEGL QPFMEVKISE GPRRARRDSG LDCDENSPES RCCRYPLTVD FEDFGWDWII
     APKRYKANYC SGECEYMHLQ KYPHTHLVNK ANPRGTAGPC CTPTKMSPIN MLYFNRKEQI
     IYGKIPSMVV DRCGCS