ID   SOMA_PSEDN              Reviewed;         206 AA.
AC   P24363;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Pseudocaranx dentex (White trevally) (Caranx delicatissimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Pseudocaranx.
OX   NCBI_TaxID=349646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=2223886; DOI=10.1016/0167-4781(90)90212-k;
RA   Yamakawa M., Watahiki M., Kamioka Y., Yamamoto M., Tanaka M.,
RA   Nishiguchi Y., Nakashima K.;
RT   "Nucleotide sequence of cDNA and primary structure for hard tail growth
RT   hormone.";
RL   Biochim. Biophys. Acta 1087:247-249(1990).
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; X55176; CAA38961.1; -; mRNA.
DR   PIR; S13161; S13161.
DR   AlphaFoldDB; P24363; -.
DR   SMR; P24363; -.
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..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..206
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033016"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..179
FT                   /evidence="ECO:0000250"
FT   DISULFID        196..204
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   206 AA;  23339 MW;  3F793CDE19F2AD8B CRC64;
     MLDRVVVLLS VLCLGVSSQP IPNNQHLFSM AVSRIHHLHL RAQRLFANFE SSLQSDDQRQ
     LNKIFLQDFC NSDYIISPID KHETQRSSVL KLLLISKQLV ESWEISSHFL PGGLAERSQI
     SSRLAELREG IQMLITTNQE GAEVFSDSST LPLAPPFGNF FQTQGGDELQ RRSYELLACF
     KKDMHKVETY LTVAKCRLST EANCTL