SOMA_ICTPU
ID SOMA_ICTPU Reviewed; 200 AA.
AC P34745;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=gh;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Pituitary;
RX PubMed=8293072;
RA Tang Y., Lin C.M., Chen T.T., Kawauchi H., Dunham R.A., Powers D.A.;
RT "Structure of the channel catfish (Ictalurus punctatus) growth hormone gene
RT and its evolutionary implications.";
RL Mol. Mar. Biol. Biotechnol. 2:198-206(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chen T.T.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 23-200.
RC TISSUE=Pituitary;
RX PubMed=1308206;
RA Watanabe K., Igarashi A., Noso T., Chen T.T., Dunham R.A., Kawauchi H.;
RT "Chemical identification of catfish growth hormone and prolactin.";
RL Mol. Mar. Biol. Biotechnol. 1:239-249(1992).
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; S69215; AAC60745.1; -; Genomic_DNA.
DR EMBL; AF267989; AAF78944.1; -; Genomic_DNA.
DR AlphaFoldDB; P34745; -.
DR SMR; P34745; -.
DR STRING; 7998.ENSIPUP00000027839; -.
DR OMA; QTAFCFS; -.
DR Proteomes; UP000221080; Genome assembly.
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; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0042538; P:hyperosmotic salinity response; IDA:AgBase.
DR GO; GO:0050996; P:positive regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:1903576; P:response to L-arginine; IDA:AgBase.
DR GO; GO:0043434; P:response to peptide hormone; IDA:AgBase.
DR GO; GO:0042594; P:response to starvation; 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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hormone; Metal-binding;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:1308206"
FT CHAIN 23..200
FT /note="Somatotropin"
FT /id="PRO_0000033027"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT DISULFID 71..173
FT /evidence="ECO:0000250"
FT DISULFID 190..198
FT /evidence="ECO:0000250"
FT CONFLICT 145
FT /note="N -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 22469 MW; 4DE6BB4DAF5860FA CRC64;
MARVLVLLSV VVASLLFSQG ATFESQRLFN NAVIRVQHLH QLAAKMMDDF EEALLPEERK
QLSKIFPLSF CNSDSIEAPA GKDEAQKSSV LKLLHTSYRL IESWEFPSRN LGNPNHISEK
LADLKMGIGV LIEGCVDGQT GLDENDSLAP PFEDFYQTLS EGNLRKSFRL LSCFKKDMHK
VETYLSVAKC RRSLDSNCTL