ID   SOMA2_XENLA             Reviewed;         208 AA.
AC   P12856; Q9PTI2;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Somatotropin-B;
DE   AltName: Full=Growth hormone B;
DE            Short=GH-B;
DE   Flags: Precursor;
GN   Name=gh-b; Synonyms=ghb;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10618393; DOI=10.1073/pnas.97.1.190;
RA   Huang H., Brown D.D.;
RT   "Overexpression of Xenopus laevis growth hormone stimulates growth of
RT   tadpoles and frogs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:190-194(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 124-208.
RC   TISSUE=Pituitary;
RX   PubMed=2734108; DOI=10.1093/nar/17.10.3974;
RA   Martens G.J.M., Groenen P.J.T.A., Braks A.A.M., Bussemakers M.J.G.;
RT   "Expression of two growth hormone genes in the Xenopus pituitary gland.";
RL   Nucleic Acids Res. 17:3974-3974(1989).
CC   -!- FUNCTION: Growth hormone plays an important role in growth control.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatotropin/prolactin family.
CC       {ECO:0000305}.
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DR   EMBL; AF193798; AAF05774.1; -; mRNA.
DR   EMBL; X14602; CAA32747.1; -; mRNA.
DR   PIR; S04354; S04354.
DR   RefSeq; NP_001079084.1; NM_001085615.2.
DR   AlphaFoldDB; P12856; -.
DR   SMR; P12856; -.
DR   GeneID; 373617; -.
DR   KEGG; xla:373617; -.
DR   CTD; 373617; -.
DR   Xenbase; XB-GENE-5872068; gh2.S.
DR   OrthoDB; 1190548at2759; -.
DR   Proteomes; UP000186698; Chromosome 4S.
DR   Bgee; 373617; Expressed in brain and 1 other tissue.
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; Reference proteome; Secreted;
KW   Signal; Zinc.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..208
FT                   /note="Somatotropin-B"
FT                   /id="PRO_0000033010"
FT   BINDING         44
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..181
FT                   /evidence="ECO:0000250"
FT   DISULFID        198..206
FT                   /evidence="ECO:0000250"
FT   CONFLICT        148
FT                   /note="N -> S (in Ref. 2; CAA32747)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  24074 MW;  3D6D54D2EB522292 CRC64;
     MVPGSCSSFG LLVILSFQNV PDVGGFPNVP LFSLFTNAVN RAQHLHMLAA DIYKDYERTY
     ITDDVRRSSK NSQVVSCYSE NIPAPTDKDN THLKSDMDLL RFSLTLIQSW LNPVQALHRL
     FRNSDVYERL KYLEEGIQSL IRELEDGNLR SYSFMRTPYE RLDINMRTDD GLLKVYGLLS
     CFKKDMHKVE TYMKVIKCRH FAESKCVI