SOMA_NEOVI
ID SOMA_NEOVI Reviewed; 216 AA.
AC P19795;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=GH1; Synonyms=GH;
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Neogale.
OX NCBI_TaxID=452646;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=2243786; DOI=10.1093/nar/18.21.6424;
RA Shoji K., Ohara E., Watahiki M., Yoneda Y.;
RT "Cloning and nucleotide sequence of a cDNA encoding the mink growth
RT hormone.";
RL Nucleic Acids Res. 18:6424-6424(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-216.
RA Perelygina L.M., Baricheva E.M., Sebeleva T.E., Kokoza V.A.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-216.
RX PubMed=2268323; DOI=10.1016/s0006-291x(05)80913-1;
RA Harada Y., Tatsumi H., Nakano E., Umezu M.;
RT "Cloning and sequence analysis of mink growth hormone cDNA.";
RL Biochem. Biophys. Res. Commun. 173:1200-1204(1990).
CC -!- FUNCTION: Plays an important role in growth control. Its major role in
CC stimulating body growth is to stimulate the liver and other tissues to
CC secrete IGF-1. It stimulates both the differentiation and proliferation
CC of myoblasts. It also stimulates amino acid uptake and protein
CC synthesis in muscle and other tissues.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000305}.
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DR EMBL; X56120; CAA39585.1; -; mRNA.
DR EMBL; X59786; CAA42448.2; -; mRNA.
DR EMBL; M62901; AAA30964.1; -; mRNA.
DR PIR; S12128; A37782.
DR AlphaFoldDB; P19795; -.
DR SMR; P19795; -.
DR Ensembl; ENSNVIT00000035564; ENSNVIP00000030700; ENSNVIG00000023639.
DR GeneTree; ENSGT00950000182818; -.
DR Proteomes; UP000694425; Unplaced.
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 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; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..216
FT /note="Somatotropin"
FT /id="PRO_0000032993"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01241"
FT DISULFID 78..189
FT /evidence="ECO:0000250"
FT DISULFID 206..214
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 24469 MW; A75B96AC94EC257F CRC64;
MAAGPRNSML LVFALLSLPW PQEVGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKDFERA
YIPEGQRYSI QNAQAAFCFS ETIPAPTGKD EAQQRSDMEL LRFSLLLIQS WLGPVQFLSR
VFTNSLVFGT SDRVYEKLKD LEEGIQALMR ELEDGSPRAG PILKQTYDKF DTNLRSDDAL
LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF