ID   SOMA_HETFO              Reviewed;         200 AA.
AC   Q9W6R8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Heteropneustes fossilis (Stinging catfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Heteropneustidae; Heteropneustes.
OX   NCBI_TaxID=93621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RA   Anathy V., Pandian T.J., Mathavan S.;
RT   "Heteropneustes fossilis growth hormone mRNA.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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; AF147792; AAD33070.1; -; mRNA.
DR   AlphaFoldDB; Q9W6R8; -.
DR   SMR; Q9W6R8; -.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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   GO; GO:0042538; P:hyperosmotic salinity response; ISS:UniProtKB.
DR   GO; GO:1903576; P:response to L-arginine; ISS:UniProtKB.
DR   GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR   GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
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; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..200
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033024"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..173
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..198
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  22538 MW;  4D766AA94405D9E2 CRC64;
     MARVLVVLSV VVASLFFSQG ATFENQRLFN NAVIRVQHLH QLAAKMMDDF EEALLPEERK
     QLSKIFPLSF CNSDSIEAPA GKDETQKSSV LKLLHTSYRL IESWEFPSKN LGNPNHISEK
     LADLKMGIGV LIEGCVDGQT SLDENDAFAP PFEDFYQTLS EGNLKKSFRL LSCFKKDMHK
     VETYLSVAKC RRSLDSNCTL