KISSR_RAT
ID KISSR_RAT Reviewed; 396 AA.
AC Q924U1; Q9Z0T7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=KiSS-1 receptor;
DE Short=KiSS-1R;
DE AltName: Full=G-protein coupled receptor 54;
DE AltName: Full=G-protein coupled receptor OT7T175;
DE Short=rOT7T175;
DE AltName: Full=Kisspeptins receptor;
DE AltName: Full=Metastin receptor;
GN Name=Kiss1r; Synonyms=Gpr54;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10100623; DOI=10.1016/s0014-5793(99)00009-5;
RA Lee D.K., Nguyen T., O'Neill G.P., Cheng R., Liu Y., Howard A.D.,
RA Coulombe N., Tan C.P., Tang-Nguyen A.-T., George S.R., O'Dowd B.F.;
RT "Discovery of a receptor related to the galanin receptors.";
RL FEBS Lett. 446:103-107(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11385580; DOI=10.1038/35079135;
RA Ohtaki T., Shintani Y., Honda S., Matsumoto H., Hori A., Kanehashi K.,
RA Terao Y., Kumano S., Takatsu Y., Masuda Y., Ishibashi Y., Watanabe T.,
RA Asada M., Yamada T., Suenaga M., Kitada C., Usuki S., Kurokawa T., Onda H.,
RA Nishimura O., Fujino M.;
RT "Metastasis suppressor gene KiSS-1 encodes peptide ligand of a G-protein-
RT coupled receptor.";
RL Nature 411:613-617(2001).
RN [3]
RP ROLE IN STIMULATION OF OXYTOCIN SECRETION.
RC TISSUE=Hypothalamus;
RX PubMed=11457843; DOI=10.1074/jbc.m104847200;
RA Kotani M., Detheux M., Vandenbogaerde A., Communi D., Vanderwinden J.-M.,
RA Le Poul E., Brezillon S., Tyldesley R., Suarez-Huerta N., Vandeput F.,
RA Blanpain C., Schiffmann S.N., Vassart G., Parmentier M.;
RT "The metastasis suppressor gene KiSS-1 encodes kisspeptins, the natural
RT ligands of the orphan G protein-coupled receptor GPR54.";
RL J. Biol. Chem. 276:34631-34636(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15157736; DOI=10.1016/j.bbaexp.2004.02.005;
RA Terao Y., Kumano S., Takatsu Y., Hattori M., Nishimura A., Ohtaki T.,
RA Shintani Y.;
RT "Expression of KiSS-1, a metastasis suppressor gene, in trophoblast giant
RT cells of the rat placenta.";
RL Biochim. Biophys. Acta 1678:102-110(2004).
RN [5]
RP POSSIBLE ROLE IN GONADOPTROPIN RELEASE.
RX PubMed=15219839; DOI=10.1016/j.bbrc.2004.05.185;
RA Matsui H., Takatsu Y., Kumano S., Matsumoto H., Ohtaki T.;
RT "Peripheral administration of metastin induces marked gonadotropin release
RT and ovulation in the rat.";
RL Biochem. Biophys. Res. Commun. 320:383-388(2004).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15242985; DOI=10.1210/en.2004-0413;
RA Navarro V.M., Castellano J.M., Fernandez-Fernandez R., Barreiro M.L.,
RA Roa J., Sanchez-Criado J.E., Aguilar E., Dieguez C., Pinilla L.,
RA Tena-Sempere M.;
RT "Developmental and hormonally regulated messenger ribonucleic acid
RT expression of KiSS-1 and its putative receptor, GPR54, in rat hypothalamus
RT and potent luteinizing hormone-releasing activity of KiSS-1 peptide.";
RL Endocrinology 145:4565-4574(2004).
RN [7]
RP STIMULATION OF THE HYPOTHALAMIC-PITUITARY-GONADAL AXIS.
RX PubMed=15500545; DOI=10.1111/j.1365-2826.2004.01240.x;
RA Thompson E.L., Patterson M., Murphy K.G., Smith K.L., Dhillo W.S.,
RA Todd J.F., Ghatei M.A., Bloom S.R.;
RT "Central and peripheral administration of kisspeptin-10 stimulates the
RT hypothalamic-pituitary-gonadal axis.";
RL J. Neuroendocrinol. 16:850-858(2004).
RN [8]
RP INVOLVEMENT IN REGULATION OF GONADOTROPIN SECRETION.
RX PubMed=15665556; DOI=10.1159/000083140;
RA Irwig M.S., Fraley G.S., Smith J.T., Acohido B.V., Popa S.M.,
RA Cunningham M.J., Gottsch M.L., Clifton D.K., Steiner R.A.;
RT "Kisspeptin activation of gonadotropin releasing hormone neurons and
RT regulation of KiSS-1 mRNA in the male rat.";
RL Neuroendocrinology 80:264-272(2004).
RN [9]
RP FUNCTION.
RX PubMed=15486019; DOI=10.1113/jphysiol.2004.072298;
RA Navarro V.M., Fernandez-Fernandez R., Castellano J.M., Roa J., Mayen A.,
RA Barreiro M.L., Gaytan F., Aguilar E., Pinilla L., Dieguez C.,
RA Tena-Sempere M.;
RT "Advanced vaginal opening and precocious activation of the reproductive
RT axis by KiSS-1 peptide, the endogenous ligand of GPR54.";
RL J. Physiol. (Lond.) 561:379-386(2004).
RN [10]
RP ROLE IN LUTEINIZING HORMONE SECRETION.
RX PubMed=15375028; DOI=10.1210/en.2004-0836;
RA Navarro V.M., Castellano J.M., Fernandez-Fernandez R., Tovar S., Roa J.,
RA Mayen A., Nogueiras R., Vazquez M.J., Barreiro M.L., Magni P., Aguilar E.,
RA Dieguez C., Pinilla L., Tena-Sempere M.;
RT "Characterization of the potent luteinizing hormone-releasing activity of
RT KiSS-1 peptide, the natural ligand of GPR54.";
RL Endocrinology 146:156-163(2005).
RN [11]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=15593369; DOI=10.1002/cne.20350;
RA Brailoiu G.C., Dun S.L., Ohsawa M., Yin D., Yang J., Chang J.K.,
RA Brailoiu E., Dun N.J.;
RT "KiSS-1 expression and metastin-like immunoreactivity in the rat brain.";
RL J. Comp. Neurol. 481:314-329(2005).
RN [12]
RP ROLE IN FOLLICLE-STIMULATING HORMONE SECRETION.
RX PubMed=15637288; DOI=10.1210/en.2004-1353;
RA Navarro V.M., Castellano J.M., Fernandez-Fernandez R., Tovar S., Roa J.,
RA Mayen A., Barreiro M.L., Casanueva F.F., Aguilar E., Dieguez C.,
RA Pinilla L., Tena-Sempere M.;
RT "Effects of KiSS-1 peptide, the natural ligand of GPR54, on follicle-
RT stimulating hormone secretion in the rat.";
RL Endocrinology 146:1689-1697(2005).
CC -!- FUNCTION: Receptor for metastin, a C-terminally amidated peptide of
CC KiSS1. KiSS1 is a metastasis suppressor protein. Activation of the
CC receptor inhibits cell proliferation and cell migration, key
CC characteristics of tumor metastasis. The receptor is essential for
CC normal gonadotropin-released hormone physiology and for puberty. The
CC hypothalamic KiSS1/KISS1R system is a pivotal factor in central
CC regulation of the gonadotropic axis at puberty and in adulthood.
CC Analysis of the transduction pathways activated by the receptor
CC identifies coupling to phospholipase C and intracellular calcium
CC release through pertussis toxin-insensitive G(q) proteins.
CC {ECO:0000269|PubMed:11457843, ECO:0000269|PubMed:15242985,
CC ECO:0000269|PubMed:15375028, ECO:0000269|PubMed:15486019,
CC ECO:0000269|PubMed:15593369, ECO:0000269|PubMed:15637288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highest expression levels in the cerebrum and
CC cecum. Moderate expression in the ovary, colon and placenta. Low levels
CC in the uterus, small intestine, and thymus. Expressed only moderately
CC in the placenta. No expression in kidney tissues. Has a complex and
CC abundant central nervous system expression pattern. Expressed in brain
CC regions such as pons, midbrain, thalamus, hypothalamus, hippocampus,
CC amygdala, cortex, frontal cortex, and striatum. No expression in the
CC cerebellum. Persistent expression is detected in hypothalamus
CC throughout postnatal development, with maximum expression levels at
CC puberty in both male and female. Hypothalamic expression changed
CC throughout the estrus cycle and is significantly increased after
CC gonadectomy, a rise that is prevented by sex steroid replacement both
CC in males and females. {ECO:0000269|PubMed:10100623,
CC ECO:0000269|PubMed:15157736, ECO:0000269|PubMed:15242985,
CC ECO:0000269|PubMed:15593369}.
CC -!- DEVELOPMENTAL STAGE: Expression detected in trophoblast giant cells
CC (TGCs), the placenta-derived cell lineage aligned at the boundary
CC between the uterus and placenta, at embryonic days 12.5 (E12.5).
CC However, expression is faint and only observed in some of these cells,
CC and disappears by E15.5. {ECO:0000269|PubMed:10100623}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF115516; AAD19664.1; -; mRNA.
DR EMBL; AB051066; BAB55447.1; -; mRNA.
DR RefSeq; NP_076482.2; NM_023992.2.
DR AlphaFoldDB; Q924U1; -.
DR SMR; Q924U1; -.
DR BioGRID; 249383; 1.
DR STRING; 10116.ENSRNOP00000016395; -.
DR BindingDB; Q924U1; -.
DR ChEMBL; CHEMBL1169599; -.
DR GuidetoPHARMACOLOGY; 266; -.
DR GlyGen; Q924U1; 3 sites.
DR PhosphoSitePlus; Q924U1; -.
DR PaxDb; Q924U1; -.
DR PRIDE; Q924U1; -.
DR GeneID; 78976; -.
DR KEGG; rno:78976; -.
DR UCSC; RGD:70930; rat.
DR CTD; 84634; -.
DR RGD; 70930; Kiss1r.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q924U1; -.
DR OrthoDB; 1294084at2759; -.
DR PhylomeDB; Q924U1; -.
DR TreeFam; TF315737; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:Q924U1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:RGD.
DR GO; GO:0042923; F:neuropeptide binding; IDA:RGD.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISO:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; IDA:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IDA:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008103; KiSS_1_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01728; KISS1RECEPTR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..396
FT /note="KiSS-1 receptor"
FT /id="PRO_0000069697"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 346..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 289..300
FT /note="GPSGAWHPRSYA -> PLGGLAPSKLC (in Ref. 1; AAD19664)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="R -> H (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42889 MW; E68C680BC003B0F2 CRC64;
MAAEATLGPN VSWWAPSNAS GCPGCGVNAS DGPGSAPRPL DAWLVPLFFA ALMLLGLVGN
SLVIFVICRH KHMQTVTNFY IANLAATDVT FLLCCVPFTA LLYPLPTWVL GDFMCKFVNY
IQQVSVQATC ATLTAMSVDR WYVTVFPLRA LHRRTPRLAL TVSLSIWVGS AAVSAPVLAL
HRLSPGPHTY CSEAFPSRAL ERAFALYNLL ALYLLPLLAT CACYGAMLRH LGRAAVRPAP
TDGALQGQLL AQRAGAVRTK VSRLVAAVVL LFAACWGPIQ LFLVLQALGP SGAWHPRSYA
AYALKIWAHC MSYSNSALNP LLYAFLGSHF RQAFCRVCPC GPQRQRRPHA SAHSDRAAPH
SVPHSRAAHP VRVRTPEPGN PVRRSPSVQD EHTAPL
