GP151_MOUSE
ID GP151_MOUSE Reviewed; 422 AA.
AC Q7TSN6; Q0VBS2; Q80UD8; Q8BX88;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=G-protein coupled receptor 151 protein;
DE AltName: Full=G-protein coupled receptor PGR7;
DE AltName: Full=GPCR-2037;
GN Name=Gpr151; Synonyms=Pgr7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=14667573; DOI=10.1016/j.molbrainres.2003.09.013;
RA Berthold M., Collin M., Sejlitz T., Meister B., Lind P.;
RT "Cloning of a novel orphan G protein-coupled receptor (GPCR-2037): in situ
RT hybridization reveals high mRNA expression in rat brain restricted to
RT neurons of the habenular complex.";
RL Brain Res. Mol. Brain Res. 120:22-29(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-422, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15111018; DOI=10.1016/j.neuropharm.2004.02.004;
RA Ignatov A., Hermans-Borgmeyer I., Schaller H.C.;
RT "Cloning and characterization of a novel G-protein-coupled receptor with
RT homology to galanin receptors.";
RL Neuropharmacology 46:1114-1120(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-422.
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-158.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=25116430; DOI=10.1002/cne.23664;
RA Broms J., Antolin-Fontes B., Tingstroem A., Ibanez-Tallon I.;
RT "Conserved expression of the GPR151 receptor in habenular axonal
RT projections of vertebrates.";
RL J. Comp. Neurol. 523:359-380(2015).
CC -!- FUNCTION: Proton-sensing G-protein coupled receptor.
CC {ECO:0000250|UniProtKB:Q8TDV0}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TDV0};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: High expression in the brain and lower levels in
CC kidney and liver (PubMed:14667573). In the nervous system expressed
CC specifically in the habenular area (at protein level)
CC (PubMed:25116430). {ECO:0000269|PubMed:14667573,
CC ECO:0000269|PubMed:25116430}.
CC -!- DEVELOPMENTAL STAGE: High levels detected at 7 dpc.
CC {ECO:0000269|PubMed:15111018}.
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DR EMBL; AJ564167; CAD91896.1; -; mRNA.
DR EMBL; BC120520; AAI20521.1; -; mRNA.
DR EMBL; BC120526; AAI20527.1; -; mRNA.
DR EMBL; AY351677; AAQ62568.1; -; mRNA.
DR EMBL; AK048591; BAC33383.1; -; mRNA.
DR EMBL; AY255533; AAO85045.1; -; mRNA.
DR CCDS; CCDS29215.1; -.
DR RefSeq; NP_853521.1; NM_181543.1.
DR AlphaFoldDB; Q7TSN6; -.
DR SMR; Q7TSN6; -.
DR BioGRID; 232184; 1.
DR IntAct; Q7TSN6; 1.
DR STRING; 10090.ENSMUSP00000058887; -.
DR GlyGen; Q7TSN6; 2 sites.
DR PhosphoSitePlus; Q7TSN6; -.
DR PaxDb; Q7TSN6; -.
DR PRIDE; Q7TSN6; -.
DR ProteomicsDB; 267652; -.
DR Antibodypedia; 15831; 322 antibodies from 29 providers.
DR DNASU; 240239; -.
DR Ensembl; ENSMUST00000054738; ENSMUSP00000058887; ENSMUSG00000042816.
DR GeneID; 240239; -.
DR KEGG; mmu:240239; -.
DR UCSC; uc008eua.1; mouse.
DR CTD; 134391; -.
DR MGI; MGI:2441887; Gpr151.
DR VEuPathDB; HostDB:ENSMUSG00000042816; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_053982_0_0_1; -.
DR InParanoid; Q7TSN6; -.
DR OMA; YFWRAYG; -.
DR OrthoDB; 658542at2759; -.
DR PhylomeDB; Q7TSN6; -.
DR TreeFam; TF332591; -.
DR BioGRID-ORCS; 240239; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q7TSN6; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q7TSN6; protein.
DR Bgee; ENSMUSG00000042816; Expressed in habenula and 47 other tissues.
DR Genevisible; Q7TSN6; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; ISS:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..422
FT /note="G-protein coupled receptor 151 protein"
FT /id="PRO_0000069633"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 339..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 422 AA; 46826 MW; 06F6F2FB2127793F CRC64;
MGKAMLRAGF ADTNSSNMNE SFARLHFAGG YLPSDSKDWR TIIPSLLMAV CLVGLVGNLC
VIGILLHGVW KRKPSTIHSL ILNLSLADFS LLLFSAPVRA AAYSKGVWDL GWFICKSSDW
FTHVCMAAKS LTFVVVAKAC FAYASDPAKQ ESIHSRTIWS VLAGIWVVAS LLPLPEWLFS
TTRRHAGVEM CLVDVPAVAE EFMSMFGKLY PLLVFCLPLL LAGVYFWRAY DQCKTRCTKT
RNLRDQMRSK QLTVMLLSTA IISALLWLPE WIAWLWVWHV KAGGPMPPQG FIALSQVLMF
FTSTANPLIF LVMSEEFKAG LKGLWKWMIT RKPAVTSEVQ EAPAGNTEAL PGKAPSPETQ
TCILDTDGRG SPDDSKEKSG KVVAPILPDV EQFWHERDAV PSAQDNDPIP WEHEGQETEG
CN
