ID   SOMA_ONCKE              Reviewed;         210 AA.
AC   P07064;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Oncorhynchus keta (Chum salmon) (Salmo keta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8018;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16593578; DOI=10.1073/pnas.82.13.4306;
RA   Sekine S., Mizukami T., Nishi T., Kuwana Y., Saito A., Sato M., Itoh S.,
RA   Kawauchi H.;
RT   "Cloning and expression of cDNA for salmon growth hormone in Escherichia
RT   coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:4306-4310(1985).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3947079; DOI=10.1016/0003-9861(86)90622-3;
RA   Kawauchi H., Moriyama S., Yasuda A., Yamaguchi K., Shirahata K., Kubota J.,
RA   Hirano T.;
RT   "Isolation and characterization of chum salmon growth hormone.";
RL   Arch. Biochem. Biophys. 244:542-552(1986).
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; K03050; AAA49403.1; -; mRNA.
DR   PIR; A23154; A23154.
DR   AlphaFoldDB; P07064; -.
DR   SMR; P07064; -.
DR   GO; GO:0005829; C:cytosol; ISS:AgBase.
DR   GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR   GO; GO:0005131; F:growth hormone receptor binding; ISS: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; IMP:AgBase.
DR   GO; GO:0055064; P:chloride ion homeostasis; ISS:AgBase.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IMP:AgBase.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IMP:AgBase.
DR   GO; GO:0045919; P:positive regulation of cytolysis; IMP:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR   GO; GO:2000376; P:positive regulation of oxygen metabolic process; ISS:AgBase.
DR   GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; ISS:AgBase.
DR   GO; GO:0090277; P:positive regulation of peptide hormone secretion; ISS:AgBase.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:AgBase.
DR   GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISS:AgBase.
DR   GO; GO:0009306; P:protein secretion; ISS:AgBase.
DR   GO; GO:0002637; P:regulation of immunoglobulin production; IMP:AgBase.
DR   GO; GO:1903350; P:response to dopamine; ISS:AgBase.
DR   GO; GO:0060416; P:response to growth hormone; ISS:AgBase.
DR   GO; GO:0042594; P:response to starvation; ISS:AgBase.
DR   GO; GO:0009266; P:response to temperature stimulus; ISS:AgBase.
DR   GO; GO:0055078; P:sodium ion homeostasis; IMP: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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hormone; Metal-binding;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT   CHAIN           23..210
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033033"
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;  23795 MW;  69D0E57CD18C5515 CRC64;
     MGQVFLLMPV LLVSCFLSQG AAIENQRLFN IAVSRVQHLH LLAQKMFNDF DGTLLPDERR
     QLNKIFLLDF CNSDSIVSPV DKHETQKSSV LKLLHISFRL IESWEYPSQT LIISNSLMVR
     NANQISEKLS DLKVGINLLI TGSQDGVLSL DDNDSQQLPP YGNYYQNLGG DGNVRRNYEL
     LACFKKDMHK VETYLTVAKC RKSLEANCTL