ID   SOMA_THUTH              Reviewed;         204 AA.
AC   P09113;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Thunnus thynnus (Atlantic bluefin tuna) (Scomber thynnus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Pelagiaria; Scombriformes; Scombridae; Thunnus.
OX   NCBI_TaxID=8237;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Pituitary;
RX   PubMed=3334850; DOI=10.1016/0167-4781(88)90051-6;
RA   Sato N., Watanabe K., Murata K., Sakaguchi M., Kariya Y., Kimura S.,
RA   Nonaka M., Kimura A.;
RT   "Molecular cloning and nucleotide sequence of tuna growth hormone cDNA.";
RL   Biochim. Biophys. Acta 949:35-42(1988).
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; X06735; CAA29914.1; -; mRNA.
DR   PIR; S01746; S01746.
DR   AlphaFoldDB; P09113; -.
DR   SMR; P09113; -.
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   Pyrrolidone carboxylic acid; Secreted; Signal; Zinc.
FT   SIGNAL          1..17
FT   CHAIN           18..204
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033058"
FT   BINDING         36
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|UniProtKB:P34747"
FT   DISULFID        69..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        194..202
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23138 MW;  F68D0F2AA7AB2D96 CRC64;
     MDRVFLLLSV LSLGVSSQPI TDSQRLFSIA VSRVQHLHLL AQRLFSDFES SLQTEEQRQL
     NKIFLQDFCN SDYIISPIDK HETQRSSVLK LLSISYRLVE SWEFPSRSLS GGSAPRNQIS
     PKLSELKTGI HLLIRANQDG DEMFADSSAL QLAPYGNYYQ SLGADESLRR SYELLACFKK
     DMHKVETYLT VAKCRLSPEA NCTL