ID   SOMA_ONCTS              Reviewed;         210 AA.
AC   Q07221;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Oncorhynchus tshawytscha (Chinook salmon) (Salmo tshawytscha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=74940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1466911;
RA   Song S., Trinh K.T., Hew C.-L.;
RT   "Cloning and sequence analysis of salmon growth hormone cDNA.";
RL   Yi Chuan Xue Bao 19:308-315(1992).
RN   [2]
RP   ERRATUM OF PUBMED:1466911.
RA   Song S., Trinh K.T., Hew C.-L.;
RL   Yi Chuan Xue Bao 20:380-380(1993).
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; S50867; AAB24612.2; -; mRNA.
DR   PIR; I51186; I51186.
DR   AlphaFoldDB; Q07221; -.
DR   SMR; Q07221; -.
DR   Proteomes; UP000694402; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0005131; F:growth hormone receptor binding; IMP:AgBase.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISS:AgBase.
DR   GO; GO:0042538; P:hyperosmotic salinity response; ISS:AgBase.
DR   GO; GO:0010960; P:magnesium ion homeostasis; ISS:AgBase.
DR   GO; GO:2000844; P:negative regulation of testosterone secretion; IMP:AgBase.
DR   GO; GO:0045919; P:positive regulation of cytolysis; ISS:AgBase.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:AgBase.
DR   GO; GO:2000833; P:positive regulation of steroid hormone secretion; IMP:AgBase.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:AgBase.
DR   GO; GO:0002637; P:regulation of immunoglobulin production; ISS:AgBase.
DR   GO; GO:0055078; P:sodium ion homeostasis; ISS:AgBase.
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; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..210
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033040"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..183
FT                   /evidence="ECO:0000250"
FT   DISULFID        200..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23892 MW;  65E4FD50E42C541B CRC64;
     MGQVFLLMPV LLVSCFLSQG AAIENQRLFN IAVSRVQHLH LLAQKMFNDF DGTLLPDERR
     QLNKIFLLDF CNSDSIVSPV DKHETQKSSV LKLLHISFRL IESWEYPSQT LIISNSLMVR
     NANQISEKLS DLKVGINLLI TGSQDAYMSL DDNDSQQLPP YGNYYQNLGG DGNVRRNYEL
     LACFKKDMHK VETYLTVAKC RKSLEANCTL