SOMA2_ONCMY
ID SOMA2_ONCMY Reviewed; 210 AA.
AC P20332;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Somatotropin-2;
DE AltName: Full=Growth hormone 2;
DE Flags: Precursor;
GN Name=gh2;
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 [GENOMIC DNA].
RX PubMed=3393535; DOI=10.1073/pnas.85.14.5136;
RA Agellon L.B., Davies S.L., Chen T.T., Powers D.A.;
RT "Structure of a fish (rainbow trout) growth hormone gene and its
RT evolutionary implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5136-5140(1988).
RN [3]
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).
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; M22732; AAA49557.1; -; mRNA.
DR EMBL; J03797; AAA49556.1; -; Genomic_DNA.
DR EMBL; M24684; AAA49554.1; -; mRNA.
DR PIR; I51340; I51340.
DR RefSeq; NP_001118162.1; NM_001124690.1.
DR AlphaFoldDB; P20332; -.
DR SMR; P20332; -.
DR GeneID; 100136734; -.
DR KEGG; omy:100136734; -.
DR CTD; 2689; -.
DR OrthoDB; 1190548at2759; -.
DR SABIO-RK; P20332; -.
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:2000844; P:negative regulation of testosterone secretion; 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:0050766; P:positive regulation of phagocytosis; ISS:AgBase.
DR GO; GO:2000833; P:positive regulation of steroid hormone secretion; 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-2"
FT /id="PRO_0000033037"
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 112
FT /note="T -> I (in Ref. 3; AAA49554)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="GV -> LA (in Ref. 3; AAA49554)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="Y -> S (in Ref. 3; AAA49554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23946 MW; 51CC693FDB14CF90 CRC64;
MGQVFLLMPV LLVSCFLGQG AAMENQRLFN IAVNRVQHLH LLAQKMFNDF EGTLLPDERR
QLNKIFLLDF CNSDSIVSPI DKQETQKSSV LKLLHISFRL IESWEYPSQT LTISNSLMVR
NSNQISEKLS DLKVGINLLI KGSQDGVLSL DDNDSQHLPP YGNYYQNLGG DGNVRRNYEL
LACFKKDMHK VETYLTVAKC RKYLEANCTL
