SOMA_CORAU
ID SOMA_CORAU Reviewed; 210 AA.
AC P45655;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=gh;
OS Coregonus autumnalis (Arctic cisco) (Salmo autumnalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Coregoninae; Coregonus.
OX NCBI_TaxID=27773;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=7990828;
RA Trofimova I.N., Iakhnenko V.M.;
RT "Primary structure of DNA, complementary for mRNA for the Baikal omul
RT growth hormone.";
RL Mol. Biol. (Mosk.) 28:1057-1060(1994).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X77245; CAA54461.1; -; mRNA.
DR PIR; I50118; I50118.
DR AlphaFoldDB; P45655; -.
DR SMR; P45655; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005131; F:growth hormone receptor binding; IEA:InterPro.
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:0045919; P:positive regulation of cytolysis; ISS: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: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; Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..210
FT /note="Somatotropin"
FT /id="PRO_0000033017"
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; 23908 MW; 7972AA807459B265 CRC64;
MGQVFLLMPV LLVSGFLSQG AAMENQRLFN IAVNRVQHLH LMAQKMFNDF EGTLLPDERR
QLNKIFLLDF CNSDSIVSPI DKLETQKSSV LKLLHISFRL IESWEYPSQT LTISNSLMVR
NSNQISEKLS DLKVGINLLI KGSQDGVLSL DDNDFQQLPP YGNYYQNLGG DGNVRRNYEL
LACFKKDMHK VETYLTVAKC RKSLEANCTL