GON1_CAVPO
ID GON1_CAVPO Reviewed; 92 AA.
AC O54713;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Progonadoliberin-1;
DE AltName: Full=Progonadoliberin I;
DE Contains:
DE RecName: Full=Gonadoliberin-1;
DE AltName: Full=Gonadoliberin I;
DE AltName: Full=Gonadotropin-releasing hormone I;
DE Short=GnRH-I;
DE AltName: Full=Luliberin I;
DE AltName: Full=Luteinizing hormone-releasing hormone I;
DE Short=LH-RH I;
DE Contains:
DE RecName: Full=GnRH-associated peptide 1;
DE AltName: Full=GnRH-associated peptide I;
DE Flags: Precursor;
GN Name=GNRH1; Synonyms=GNRH, LHRH;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Hypothalamus;
RX PubMed=9322920; DOI=10.1210/endo.138.10.5454;
RA Jimenez-Linan M., Rubin B.S., King J.C.;
RT "Examination of guinea pig luteinizing hormone-releasing hormone gene
RT reveals a unique decapeptide and existence of two transcripts in the
RT brain.";
RL Endocrinology 138:4123-4130(1997).
CC -!- FUNCTION: Stimulates the secretion of gonadotropins; it stimulates the
CC secretion of both luteinizing and follicle-stimulating hormones.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: [Gonadoliberin-1]: The precursor is cleaved by ACE, which removes
CC the Gly-Lys-Arg peptide at the C-terminus, leading to mature hormone.
CC The mature form of Gonadoliberin-1 is also cleaved and degraded by ACE.
CC {ECO:0000250|UniProtKB:P01148}.
CC -!- SIMILARITY: Belongs to the GnRH family. {ECO:0000305}.
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DR EMBL; AF033346; AAB87688.1; -; mRNA.
DR RefSeq; NP_001166427.1; NM_001172956.1.
DR AlphaFoldDB; O54713; -.
DR SMR; O54713; -.
DR STRING; 10141.ENSCPOP00000014012; -.
DR Ensembl; ENSCPOT00000015690; ENSCPOP00000014012; ENSCPOG00000015538.
DR GeneID; 100135531; -.
DR KEGG; cpoc:100135531; -.
DR CTD; 2796; -.
DR eggNOG; ENOG502S8C8; Eukaryota.
DR GeneTree; ENSGT00390000008225; -.
DR HOGENOM; CLU_2412553_0_0_1; -.
DR InParanoid; O54713; -.
DR OMA; ISSGQHW; -.
DR OrthoDB; 1556205at2759; -.
DR TreeFam; TF330934; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000015538; Expressed in hypothalamus and 1 other tissue.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005183; F:gonadotropin hormone-releasing hormone activity; IEA:InterPro.
DR GO; GO:2001223; P:negative regulation of neuron migration; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:2000354; P:regulation of ovarian follicle development; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR InterPro; IPR002012; GnRH.
DR InterPro; IPR019792; Gonadoliberin.
DR InterPro; IPR004079; Gonadoliberin_I_precursor.
DR PANTHER; PTHR10522; PTHR10522; 1.
DR PRINTS; PR01541; GONADOLIBRNI.
DR PROSITE; PS00473; GNRH; 1.
PE 3: Inferred from homology;
KW Amidation; Cleavage on pair of basic residues; Hormone;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..92
FT /note="Progonadoliberin-1"
FT /id="PRO_0000012392"
FT PEPTIDE 24..33
FT /note="Gonadoliberin-1"
FT /id="PRO_0000012393"
FT PEPTIDE 37..92
FT /note="GnRH-associated peptide 1"
FT /id="PRO_0000012394"
FT SITE 26..27
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000250|UniProtKB:P01148"
FT SITE 26
FT /note="Appears to be essential for biological activity"
FT /evidence="ECO:0000250"
FT SITE 28..29
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000250|UniProtKB:P01148"
FT SITE 30..31
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000250|UniProtKB:P01148"
FT SITE 33..34
FT /note="Cleavage; by ACE"
FT /evidence="ECO:0000250|UniProtKB:P01148"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P01148"
FT MOD_RES 33
FT /note="Glycine amide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 92 AA; 10279 MW; ACF74613F456D663 CRC64;
MGLIPKLLAG LVLLTLCVEN GSGQYWSYGV RPGGKRNIEP LVDSFQEMAK EIDQLAEPQH
FECTLHQPRS PLRDLKGALE SLMEEETGQK KI
