ID   GNIH_COTJA              Reviewed;         173 AA.
AC   Q9DGD4;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Gonadotropin inhibitory hormone peptides;
DE   Contains:
DE     RecName: Full=Gonadotropin inhibitory hormone;
DE              Short=GnIH;
DE   Contains:
DE     RecName: Full=Gonadotropin inhibitory hormone-related peptide 1;
DE              Short=GnIH-RP1;
DE   Contains:
DE     RecName: Full=Gonadotropin inhibitory hormone-related peptide 2;
DE              Short=GnIH-RP2;
DE   Flags: Precursor;
GN   Name=GNIH;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934 {ECO:0000312|EMBL:BAB15932.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AMIDATION AT PHE-95; PHE-115 AND PHE-154,
RP   TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=11171117; DOI=10.1042/0264-6021:3540379;
RA   Satake H., Hisada M., Kawada T., Minakata H., Ukena K., Tsutsui K.;
RT   "Characterization of a cDNA encoding a novel avian hypothalamic
RT   neuropeptide exerting an inhibitory effect on gonadotropin release.";
RL   Biochem. J. 354:379-385(2001).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 104-115, AMIDATION AT PHE-115, SYNTHESIS, FUNCTION,
RP   TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=10964719; DOI=10.1006/bbrc.2000.3350;
RA   Tsutsui K., Saigoh E., Ukena K., Teranishi H., Fujisawa Y., Kikuchi M.,
RA   Ishii S., Sharp P.J.;
RT   "A novel avian hypothalamic peptide inhibiting gonadotropin release.";
RL   Biochem. Biophys. Res. Commun. 275:661-667(2000).
CC   -!- FUNCTION: Hypothalamic factor, responsible for the negative regulation
CC       of gonadotropin secretion. {ECO:0000269|PubMed:10964719}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the diencephalon.
CC       {ECO:0000269|PubMed:10964719, ECO:0000269|PubMed:11171117}.
CC   -!- MASS SPECTROMETRY: [Gonadotropin inhibitory hormone]: Mass=1390.81;
CC       Method=MALDI; Evidence={ECO:0000269|PubMed:10964719,
CC       ECO:0000269|PubMed:11171117};
CC   -!- MASS SPECTROMETRY: [Gonadotropin inhibitory hormone]: Mass=1389.4;
CC       Method=FAB; Evidence={ECO:0000269|PubMed:10964719,
CC       ECO:0000269|PubMed:11171117};
CC   -!- MASS SPECTROMETRY: [Gonadotropin inhibitory hormone-related peptide 2]:
CC       Mass=1501.81; Method=MALDI; Evidence={ECO:0000269|PubMed:11171117};
CC   -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB039815; BAB15932.1; -; mRNA.
DR   AlphaFoldDB; Q9DGD4; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IDA:AgBase.
DR   GO; GO:0043025; C:neuronal cell body; IDA:AgBase.
DR   GO; GO:0043204; C:perikaryon; IDA:AgBase.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:AgBase.
DR   GO; GO:0033685; P:negative regulation of luteinizing hormone secretion; IDA:AgBase.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0032100; P:positive regulation of appetite; IDA:AgBase.
DR   InterPro; IPR026297; FMRFamide-related/fGRP.
DR   PANTHER; PTHR14403; PTHR14403; 1.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Neuropeptide; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..82
FT                   /id="PRO_0000009944"
FT   PEPTIDE         84..95
FT                   /note="Gonadotropin inhibitory hormone-related peptide 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000009945"
FT   PROPEP          98..103
FT                   /evidence="ECO:0000269|PubMed:10964719"
FT                   /id="PRO_0000009946"
FT   PEPTIDE         104..115
FT                   /note="Gonadotropin inhibitory hormone"
FT                   /id="PRO_0000009947"
FT   PROPEP          118..140
FT                   /id="PRO_0000009948"
FT   PEPTIDE         142..154
FT                   /note="Gonadotropin inhibitory hormone-related peptide 2"
FT                   /id="PRO_0000009949"
FT   PROPEP          157..173
FT                   /id="PRO_0000009950"
FT   MOD_RES         95
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:11171117"
FT   MOD_RES         115
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:10964719,
FT                   ECO:0000269|PubMed:11171117"
FT   MOD_RES         154
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:11171117"
SQ   SEQUENCE   173 AA;  19428 MW;  B8D5CD3239C8E61B CRC64;
     MEIISTQKFI LLTLATVAFL TPHGACLDEL MKSSLESRED DDDKYYETKD SILEEKQRSL
     NFEEMKDWGS KNFMKVNTPT VNKVPNSVAN LPLRFGRSNP EERSIKPSAY LPLRFGRAFG
     ESLSRRAPNL SNRSGRSPLA RSSIQSLLNL SQRFGKSVPI SLSQGVQESE PGM