ID   SOMA_ANGJA              Reviewed;         209 AA.
AC   P08899;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Somatotropin-1;
DE   AltName: Full=Growth hormone I;
DE   AltName: Full=Somatotropin I;
DE   Flags: Precursor;
GN   Name=gh1;
OS   Anguilla japonica (Japanese eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2468582; DOI=10.1016/0378-1119(88)90519-7;
RA   Saito A., Sekine S., Komatsu Y., Sato M., Hirano T., Itoh S.;
RT   "Molecular cloning of eel growth hormone cDNA and its expression in
RT   Escherichia coli.";
RL   Gene 73:545-551(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-209.
RC   TISSUE=Pituitary;
RX   PubMed=3609715; DOI=10.1016/0016-6480(87)90256-5;
RA   Yamaguchi K., Yasuda A., Kishida M., Hirano T., Sano H., Kawauchi H.;
RT   "Primary structure of eel (Anguilla japonica) growth hormone.";
RL   Gen. Comp. Endocrinol. 66:447-453(1987).
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; M24066; AAA48535.1; -; mRNA.
DR   PIR; JT0483; JT0483.
DR   AlphaFoldDB; P08899; -.
DR   SMR; P08899; -.
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   Secreted; Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:3609715"
FT   CHAIN           20..209
FT                   /note="Somatotropin-1"
FT                   /id="PRO_0000033013"
FT   REGION          59..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..182
FT   DISULFID        199..207
FT   CONFLICT        48
FT                   /note="K -> L (in Ref. 1; AAA48535)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  23556 MW;  128B461A4B340F78 CRC64;
     MASGFLLWPV LLVSFSVNAV EPISLYNLFT SAVNRAQHLH TLAAEIYKEF ERSIPPEAHR
     QLSKTSPLAG CYSDSIPTPT GKDETQEKSD GYLLRISSAL IQSWVYPLKT LSDAFSNSLM
     FGTSDGIFDK LEDLNKGINE LMKVVGDGGI YIEDVRNLRY ENFDVHLRND AGLMKNYGLL
     ACFKKDMHKV ETYLKVTKCR RFVESNCTL