SOMA_CANLF
ID SOMA_CANLF Reviewed; 216 AA.
AC P33711; Q9TQT6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=GH1; Synonyms=GH;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8206387; DOI=10.1016/0378-1119(94)90110-4;
RA Ascacio-Martinez J.A., Barrera-Saldana H.A.;
RT "A dog growth hormone cDNA codes for a mature protein identical to pig
RT growth hormone.";
RL Gene 143:277-280(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA van Leeuwen I.S., Teske E., van Garderen E., Rutteman G.R., Mol J.A.;
RT "Extrapituitary growth hormone expression in the dog is initiated at the
RT normal pituitary transcription start site in the mammary gland and at
RT multiple upstream sites in lymphoid cells.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=10411306; DOI=10.1016/s0303-7207(99)00010-6;
RA Lantinga-van Leeuwen I.S., Oudshoorn M., Mol J.A.;
RT "Canine mammary growth hormone gene transcription initiates at the
RT pituitary-specific start site in the absence of Pit-1.";
RL Mol. Cell. Endocrinol. 150:121-128(1999).
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; Z23067; CAA80601.1; -; mRNA.
DR EMBL; U92533; AAF21502.1; -; Genomic_DNA.
DR EMBL; AF069071; AAD43366.1; -; mRNA.
DR PIR; I46145; I46145.
DR RefSeq; NP_001003168.1; NM_001003168.1.
DR RefSeq; XP_005624232.1; XM_005624175.2.
DR AlphaFoldDB; P33711; -.
DR SMR; P33711; -.
DR STRING; 9612.ENSCAFP00000018659; -.
DR PaxDb; P33711; -.
DR Ensembl; ENSCAFT00030026701; ENSCAFP00030023307; ENSCAFG00030014381.
DR Ensembl; ENSCAFT00040032741; ENSCAFP00040028484; ENSCAFG00040017587.
DR Ensembl; ENSCAFT00845037520; ENSCAFP00845029397; ENSCAFG00845021230.
DR GeneID; 403795; -.
DR KEGG; cfa:403795; -.
DR CTD; 2688; -.
DR VEuPathDB; HostDB:ENSCAFG00845021230; -.
DR eggNOG; ENOG502R5GJ; Eukaryota.
DR GeneTree; ENSGT00950000182818; -.
DR HOGENOM; CLU_088274_2_1_1; -.
DR InParanoid; P33711; -.
DR OMA; QTAFCFS; -.
DR OrthoDB; 1190548at2759; -.
DR TreeFam; TF332592; -.
DR Reactome; R-CFA-1170546; Prolactin receptor signaling.
DR Reactome; R-CFA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Reactome; R-CFA-982772; Growth hormone receptor signaling.
DR Proteomes; UP000002254; Chromosome 9.
DR Bgee; ENSCAFG00000012681; Expressed in pituitary gland and 43 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR GO; GO:0005131; F:growth hormone receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0045927; P:positive regulation of growth; IBA:GO_Central.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central.
DR GO; GO:0032094; P:response to food; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IBA:GO_Central.
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_0000032978"
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"
FT CONFLICT 4
FT /note="S -> G (in Ref. 1; CAA80601)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="N -> T (in Ref. 1; CAA80601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24468 MW; A8AD1DD59F1DAAED CRC64;
MAASPRNSVL LAFALLCLPW PQEVGAFPAM PLSSLFANAV LRAQHLHQLA ADTYKEFERA
YIPEGQRYSI QNAQAAFCFS ETIPAPTGKD EAQQRSDVEL LRFSLLLIQS WLGPVQFLSR
VFTNSLVFGT SDRVYEKLKD LEEGIQALMR ELEDGSPRAG QILKQTYDKF DTNLRSDDAL
LKNYGLLSCF KKDLHKAETY LRVMKCRRFV ESSCAF
