ID   SOMA_DICLA              Reviewed;         204 AA.
AC   Q05163;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1472711; DOI=10.3109/10425179209034015;
RA   Doliana R., Bortolussi M., Colombo L.;
RT   "Cloning and sequencing of European sea bass (Dicentrarchus labrax L.)
RT   growth hormone cDNA using polymerase chain reaction and degenerate
RT   oligonucleotides.";
RL   DNA Seq. 3:185-189(1992).
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; X65716; CAA46632.1; -; mRNA.
DR   PIR; A56642; A56642.
DR   AlphaFoldDB; Q05163; -.
DR   SMR; Q05163; -.
DR   Proteomes; UP000694389; Unplaced.
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   Reference proteome; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..204
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033021"
FT   BINDING         35
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;  23017 MW;  62480D8015592A62 CRC64;
     MDRAILLLSV LSVGVSSQPI TEGQRLFSIA VERVHNLHLL AQRLFSEFES SLQTEEQRQL
     NKIFLQDFCN SDYIISPIDK HETQRSSVLK LLSISYRLIE SWEFPSRSLS VGPAARNQIS
     PKLSELKTGI LVLIGANQDG AEMFPDSSTL QLAPYGNYYQ SLGADESLRR TYELLACFKK
     DMHKVETYLT VAKCRLSPEA NCTL