ID   SOMA_ACABU              Reviewed;         204 AA.
AC   Q01282;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Acanthopagrus butcheri (Australian black bream) (Mylio butcheri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Acanthopagrus.
OX   NCBI_TaxID=8179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=1777674; DOI=10.3109/10425179109039680;
RA   Knibb W., Robins A., Crocker L., Rizzon J., Heyward A., Wells J.;
RT   "Molecular cloning and sequencing of Australian black bream Acanthopagrus
RT   butcheri and barramundi Lates calcarifer fish growth hormone cDNA using
RT   polymerase chain reaction.";
RL   DNA Seq. 2:121-123(1991).
CC   -!- FUNCTION: Growth hormone plays an important role in growth control and
CC       is involved in the regulation of several anabolic processes. Implicated
CC       as an osmoregulatory substance important for seawater adaptation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; X59377; CAA42021.1; -; mRNA.
DR   PIR; S30491; S30491.
DR   AlphaFoldDB; Q01282; -.
DR   SMR; Q01282; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005131; F:growth hormone receptor binding; IEA:InterPro.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR034975; Somatotropin.
DR   InterPro; IPR001400; Somatotropin/Prolactin.
DR   InterPro; IPR018116; Somatotropin_CS.
DR   PANTHER; PTHR11417; PTHR11417; 1.
DR   PANTHER; PTHR11417:SF2; PTHR11417:SF2; 1.
DR   Pfam; PF00103; Hormone_1; 1.
DR   PRINTS; PR00836; SOMATOTROPIN.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00266; SOMATOTROPIN_1; 1.
DR   PROSITE; PS00338; SOMATOTROPIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hormone; Metal-binding; Pyrrolidone carboxylic acid;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..204
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033011"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23065 MW;  22F90A8C7DAE59AE CRC64;
     MDRVVLMLSV LSLGVSSQPI TDGQRLFSIA VSRVQHLHLL AQRLFSDFES SLQTEEQRQL
     NKIFLQDFCN SDYIISPIDK HETQRSSVLK LLSISYRLVE SWEFPSRSLA GGSAPRNQIS
     PKLSELKTGI HLLIRANEDG AELFPDSSAL QLAPYGDYYH SPGTDESLRR TYELLACFKK
     DMHKVETYLT VAKCRLSPEA NCTL