SOMA_LITCT
ID SOMA_LITCT Reviewed; 215 AA.
AC P10813;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Somatotropin;
DE AltName: Full=Growth hormone;
DE Flags: Precursor;
GN Name=GH;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=3260110; DOI=10.1016/0167-4781(88)90017-6;
RA Pan F.-M., Chang W.-C.;
RT "Cloning and sequencing of bullfrog growth hormone complementary DNA.";
RL Biochim. Biophys. Acta 950:238-242(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RX PubMed=1476615; DOI=10.1677/jme.0.0090283;
RA Takahashi N., Kikuyama S., Gen K., Maruyama O., Kato Y.;
RT "Cloning of a bullfrog growth hormone cDNA: expression of growth hormone
RT mRNA in larval and adult bullfrog pituitaries.";
RL J. Mol. Endocrinol. 9:283-289(1992).
RN [3]
RP PROTEIN SEQUENCE OF 26-215.
RC TISSUE=Pituitary;
RX PubMed=1859828; DOI=10.1016/0167-4838(91)90160-2;
RA Kobayashi T., Yasuda A., Yamaguchi K., Kawauchi H., Kikuyama S.;
RT "The complete amino acid sequence of growth hormone of the bullfrog (Rana
RT catesbeiana).";
RL Biochim. Biophys. Acta 1078:383-387(1991).
CC -!- FUNCTION: Growth hormone plays an important role in growth control.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Levels increase as metamorphosis progresses, reach
CC maxima in juveniles and decrease as adulthood approaches.
CC -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC {ECO:0000305}.
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DR EMBL; X12520; CAA31038.1; -; mRNA.
DR EMBL; S52027; AAB24792.1; -; mRNA.
DR PIR; I51188; I51188.
DR PIR; JS0037; JS0037.
DR AlphaFoldDB; P10813; -.
DR SMR; P10813; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hormone; Metal-binding;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:1859828"
FT CHAIN 26..215
FT /note="Somatotropin"
FT /id="PRO_0000033008"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT DISULFID 77..188
FT /evidence="ECO:0000250"
FT DISULFID 205..213
FT /evidence="ECO:0000250"
FT CONFLICT 68..73
FT /note="SNKHSY -> KQTLLI (in Ref. 1; CAA31038)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="D -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="T -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 215 AA; 24975 MW; 3C08D5840EFF102A CRC64;
MASGLGSSLV LLVVICLQSP QGFNAFPQMS LSNLFTNAVI RAQHLHQMVA DTYRDYERTY
IPEDQRFSNK HSYSVYCYSE TIPAPTDKDN THQKSDIDLL RFSLTLLQSW MTPIQIVNRV
FGNNQVFGNI DRVYDRLRDL DEGLHILIRE LDDGNVRNYG VLTFTYDKFD VNLRSEEGRA
KNYGLLSCFK KDMHKVETYL KVMKCRRFVE SNCTF