SOMA1_ONCMY
ID SOMA1_ONCMY Reviewed; 210 AA.
AC P09538;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Somatotropin-1;
DE AltName: Full=Growth hormone 1;
DE Flags: Precursor;
GN Name=gh1;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2908440; DOI=10.1002/mrd.1080010104;
RA Agellon L.B., Davies S.L., Lin C.M., Chen T.T., Powers D.A.;
RT "Rainbow trout has two genes for growth hormone.";
RL Mol. Reprod. Dev. 1:11-17(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2647438; DOI=10.1089/dna.1.1989.8.109;
RA Rentier-Delrue F., Swennen D., Mercier L., Lion M., Benrubi O.,
RA Martial J.A.;
RT "Molecular cloning and characterization of two forms of trout growth
RT hormone cDNA: expression and secretion of tGH-II by Escherichia coli.";
RL DNA 8:109-117(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 23-210.
RX PubMed=3545720; DOI=10.1089/dna.1.1986.5.463;
RA Agellon L.B., Chen T.T.;
RT "Rainbow trout growth hormone: molecular cloning of cDNA and expression in
RT Escherichia coli.";
RL DNA 5:463-471(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; M22731; AAA49555.1; -; mRNA.
DR EMBL; M24683; AAA49553.1; -; mRNA.
DR PIR; A25791; A25791.
DR PIR; A31363; A31363.
DR RefSeq; NP_001118161.1; NM_001124689.1.
DR AlphaFoldDB; P09538; -.
DR SMR; P09538; -.
DR GeneID; 100136733; -.
DR KEGG; omy:100136733; -.
DR CTD; 2688; -.
DR OrthoDB; 1190548at2759; -.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005131; F:growth hormone receptor binding; IDA: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:0055064; P:chloride ion homeostasis; IDA:AgBase.
DR GO; GO:0042538; P:hyperosmotic salinity response; IDA:AgBase.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:AgBase.
DR GO; GO:0045919; P:positive regulation of cytolysis; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR GO; GO:2000376; P:positive regulation of oxygen metabolic process; IDA:AgBase.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IDA:AgBase.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:AgBase.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:AgBase.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:AgBase.
DR GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IMP:AgBase.
DR GO; GO:0009306; P:protein secretion; IDA:AgBase.
DR GO; GO:0002637; P:regulation of immunoglobulin production; ISS:AgBase.
DR GO; GO:1903350; P:response to dopamine; IDA:AgBase.
DR GO; GO:0043207; P:response to external biotic stimulus; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:0009749; P:response to glucose; IDA:AgBase.
DR GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:0042594; P:response to starvation; IDA:AgBase.
DR GO; GO:0009266; P:response to temperature stimulus; IDA:AgBase.
DR GO; GO:0055078; P:sodium ion homeostasis; IDA: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; Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..210
FT /note="Somatotropin-1"
FT /id="PRO_0000033036"
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"
FT CONFLICT 143
FT /note="S -> N (in Ref. 2; AAA49553)"
FT /evidence="ECO:0000305"
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
