ID   SOMA_HYPNO              Reviewed;         210 AA.
AC   P69160; P20390; Q00220; Q00221;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Somatotropin;
DE   AltName: Full=Growth hormone;
DE   Flags: Precursor;
GN   Name=gh;
OS   Hypophthalmichthys nobilis (Bighead carp) (Aristichthys nobilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Hypophthalmichthys.
OX   NCBI_TaxID=7965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=1426941; DOI=10.1016/0016-6480(92)90045-l;
RA   Chang Y.S., Liu C.S., Huang F.-L., Lo T.B.;
RT   "The primary structures of growth hormones of three cyprinid species:
RT   bighead carp, silver carp, and grass carp.";
RL   Gen. Comp. Endocrinol. 87:385-393(1992).
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; X60473; CAA43006.1; -; mRNA.
DR   PIR; I50763; I50763.
DR   AlphaFoldDB; P69160; -.
DR   SMR; P69160; -.
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; Secreted; Signal; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..210
FT                   /note="Somatotropin"
FT                   /id="PRO_0000033026"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..183
FT                   /evidence="ECO:0000250"
FT   DISULFID        200..208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23580 MW;  98A8B3FECD52D098 CRC64;
     MARALVLLSV VLVSLLVNQG TASENQRLFN NAVIRVQHLH QLAAKMINDF EDNLLPEERR
     QLSKIFPLSF CNSDSIEAPT GKDETQKSSM LKLLRISFRL IESWEFPSQT LSGAVSNSLT
     VGNPNQITEK LADLKVGISV LIKGCLDGQP NMDDNDSLPL PFEDFYLTMG ESSLRESFRL
     LACFKKDMHK VETYLRVANC RRSLDSNCTL