ID   SOMA_MORSA              Reviewed;         204 AA.
AC   P48248;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Morone saxatilis (Striped bass) (Perca saxatilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Morone.
OX   NCBI_TaxID=34816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=7758842; DOI=10.1016/0303-7207(94)03458-6;
RA   Cheng C.M., Lin C.M., Shamblott M., Gonzalez-Villasenor L.I., Powers D.A.,
RA   Woods C., Chen T.T.;
RT   "Production of a biologically active recombinant teleostean growth hormone
RT   in E. coli cells.";
RL   Mol. Cell. Endocrinol. 108:75-85(1995).
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; S78253; AAB34389.1; -; mRNA.
DR   PIR; I51289; I51289.
DR   AlphaFoldDB; P48248; -.
DR   SMR; P48248; -.
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; Pyrrolidone carboxylic acid;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000250"
FT   CHAIN           18..204
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033032"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         18
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        69..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23045 MW;  F4186DC5FF696115 CRC64;
     MDRAVLLLSV LSLGVSSQPI TEGQRLFSIA VERVHNLHLL AQRLFTEFES SLQTEEQRQL
     NKIFLQDFCN SDYIISPIDK HETQRSSVLK LLSISYRLIE SWEFPSRSLS VGPAARNQIS
     PKLSELKTGI LLLIGANQDG AEMFPDSSTL QLAPYGNYYQ SLGADESLRR TYELLACFKK
     DMHKVETYLT VAKCRLSPEA NCTL