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   24-JAN-2024, entry version 135.
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   GlyCosmos; Q7TSN6; 2 sites, No reported glycans.
DR   GlyGen; Q7TSN6; 2 sites.
DR   PhosphoSitePlus; Q7TSN6; -.
DR   PaxDb; 10090-ENSMUSP00000058887; -.
DR   ProteomicsDB; 267652; -.
DR   Antibodypedia; 15831; 362 antibodies from 29 providers.
DR   DNASU; 240239; -.
DR   Ensembl; ENSMUST00000054738.5; ENSMUSP00000058887.4; ENSMUSG00000042816.5.
DR   GeneID; 240239; -.
DR   KEGG; mmu:240239; -.
DR   UCSC; uc008eua.1; mouse.
DR   AGR; MGI:2441887; -.
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; CTIWSVL; -.
DR   OrthoDB; 4729702at2759; -.
DR   PhylomeDB; Q7TSN6; -.
DR   TreeFam; TF332591; -.
DR   BioGRID-ORCS; 240239; 0 hits in 76 CRISPR screens.
DR   PRO; PR:Q7TSN6; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q7TSN6; Protein.
DR   Bgee; ENSMUSG00000042816; Expressed in habenula and 49 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
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   CDD; cd15002; 7tmA_GPR151; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR45695:SF1; G-PROTEIN COUPLED RECEPTOR 151; 1.
DR   PANTHER; PTHR45695; LEUCOKININ RECEPTOR-RELATED; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q7TSN6; MM.
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
//