SOMA_SALSA
ID SOMA_SALSA Reviewed; 210 AA.
AC P10814;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=gh;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2704622; DOI=10.1093/nar/17.6.2352;
RA Lorens J.B., Nerland A.H., Lossius I., Male R., Telle W., Totland G.K.;
RT "The nucleotide sequence of Atlantic salmon growth hormone cDNA.";
RL Nucleic Acids Res. 17:2352-2353(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=1562611; DOI=10.1016/0167-4781(92)90452-6;
RA Male R., Nerland A.H., Lorens J.B., Telle W., Lossius I., Totland G.K.;
RT "The complete nucleotide sequence of the Atlantic salmon growth hormone I
RT gene.";
RL Biochim. Biophys. Acta 1130:345-348(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2753360; DOI=10.1016/0378-1119(89)90079-6;
RA Johansen B., Johnsen O.C., Valla S.;
RT "The complete nucleotide sequence of the growth-hormone gene from Atlantic
RT salmon (Salmo salar).";
RL Gene 77:317-324(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; X14305; CAA32481.1; -; mRNA.
DR EMBL; M21573; AAA49558.1; -; Genomic_DNA.
DR EMBL; X61938; CAA43942.1; -; Genomic_DNA.
DR PIR; A60621; A60621.
DR PIR; JS0179; JS0179.
DR PIR; S03709; S03709.
DR RefSeq; NP_001117148.1; NM_001123676.1.
DR RefSeq; XP_014059912.1; XM_014204437.1.
DR AlphaFoldDB; P10814; -.
DR SMR; P10814; -.
DR STRING; 8030.ENSSSAP00000058473; -.
DR GeneID; 100136588; -.
DR GeneID; 106607462; -.
DR KEGG; sasa:100136588; -.
DR KEGG; sasa:106607462; -.
DR OMA; QTAFCFS; -.
DR OrthoDB; 1190548at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
DR Proteomes; UP000087266; Chromosome ssa06.
DR Bgee; ENSSSAG00000055013; Expressed in brain and 1 other tissue.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0070186; F:growth hormone activity; IEA:Ensembl.
DR GO; GO:0005131; F:growth hormone receptor binding; IPI:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; ISS:AgBase.
DR GO; GO:0042538; P:hyperosmotic salinity response; ISS:AgBase.
DR GO; GO:0042539; P:hypotonic salinity response; IDA:AgBase.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISS:AgBase.
DR GO; GO:0009648; P:photoperiodism; IDA:AgBase.
DR GO; GO:0045919; P:positive regulation of cytolysis; ISS:AgBase.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
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:0002637; P:regulation of immunoglobulin production; ISS:AgBase.
DR GO; GO:0032355; P:response to estradiol; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:0009416; P:response to light stimulus; IDA:AgBase.
DR GO; GO:0014070; P:response to organic cyclic compound; IDA:AgBase.
DR GO; GO:0042594; P:response to starvation; IDA: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_0000033051"
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 42
FT /note="M -> L (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="P -> S (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="L -> Q (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> A (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="Q -> H (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="V -> I (in Ref. 3; AAA49558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 210 AA; 23894 MW; 20A6BA82A69A6368 CRC64;
MGQVFLLMPV LLVSCFLSQG AAMENQRLFN IAVNRVQHLH LMAQKMFNDF EGTLLPDERR
QLNKIFLLDF CNSDSIVSPI DKLETQKSSV LKLLHISFRL IESWEYPSQT LTISNSLMVR
NSNQISEKLS DLKVGINLLI KGSQDGVLSL DDNDSQQLPP YGNYYQNLGG DGNVRRNYEL
LACFKKDMHK VETYLTVAKC RKSLEANCTL
