HCAR1_MOUSE
ID HCAR1_MOUSE Reviewed; 343 AA.
AC Q8C131; B9EJ36;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Hydroxycarboxylic acid receptor 1;
DE AltName: Full=G-protein coupled receptor 81;
GN Name=Hcar1; Synonyms=Gpr81;
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], TISSUE SPECIFICITY, AND FUNCTION.
RC STRAIN=C57BL/6J;
RX PubMed=19047060; DOI=10.1074/jbc.m806409200;
RA Liu C., Wu J., Zhu J., Kuei C., Yu J., Shelton J., Sutton S.W., Li X.,
RA Yun S.J., Mirzadegan T., Mazur C., Kamme F., Lovenberg T.W.;
RT "Lactate inhibits lipolysis in fat cells through activation of an orphan G-
RT protein-coupled receptor, GPR81.";
RL J. Biol. Chem. 284:2811-2822(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [3]
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 [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=18174606; DOI=10.1194/jlr.m700513-jlr200;
RA Ge H., Weiszmann J., Reagan J.D., Gupte J., Baribault H., Gyuris T.,
RA Chen J.-L., Tian H., Li Y.;
RT "Elucidation of signaling and functional activities of an orphan GPCR,
RT GPR81.";
RL J. Lipid Res. 49:797-803(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a receptor for L-lactate and mediates its anti-
CC lipolytic effect through a G(i)-protein-mediated pathway.
CC {ECO:0000269|PubMed:18174606, ECO:0000269|PubMed:19047060}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in subcutaneous fat and omental
CC fat and detectable in lower levels in brain and many other tissues.
CC High levels detected in epididymal and subcutaneous fat with slightly
CC lower in omental fat, low levels are detected in the brain, skeletal
CC muscle, kidney, liver and the pancreas (at protein level).
CC {ECO:0000269|PubMed:18174606, ECO:0000269|PubMed:19047060}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU809460; ACJ03846.1; -; mRNA.
DR EMBL; AK029064; BAC26273.1; -; mRNA.
DR EMBL; BC141305; AAI41306.1; -; mRNA.
DR CCDS; CCDS19669.2; -.
DR RefSeq; NP_780729.2; NM_175520.4.
DR AlphaFoldDB; Q8C131; -.
DR SMR; Q8C131; -.
DR STRING; 10090.ENSMUSP00000129280; -.
DR BindingDB; Q8C131; -.
DR ChEMBL; CHEMBL2146354; -.
DR GuidetoPHARMACOLOGY; 311; -.
DR GlyGen; Q8C131; 1 site.
DR iPTMnet; Q8C131; -.
DR PhosphoSitePlus; Q8C131; -.
DR PaxDb; Q8C131; -.
DR PRIDE; Q8C131; -.
DR ProteomicsDB; 271494; -.
DR DNASU; 243270; -.
DR Ensembl; ENSMUST00000164267; ENSMUSP00000129280; ENSMUSG00000049241.
DR GeneID; 243270; -.
DR KEGG; mmu:243270; -.
DR CTD; 27198; -.
DR MGI; MGI:2441671; Hcar1.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00990000203619; -.
DR InParanoid; Q8C131; -.
DR PhylomeDB; Q8C131; -.
DR Reactome; R-MMU-3296197; Hydroxycarboxylic acid-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR PRO; PR:Q8C131; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C131; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR028016; HCAR1_rcpt.
DR PANTHER; PTHR46048:SF3; PTHR46048:SF3; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
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..343
FT /note="Hydroxycarboxylic acid receptor 1"
FT /id="PRO_0000069587"
FT TOPO_DOM 1..21
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 319..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 290
FT /note="T -> A (in Ref. 1; ACJ03846 and 3; AAI41306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 343 AA; 38927 MW; 917FA9499B2E03FD CRC64;
MDNGSCCLIE GEPISQVMPP LLILVFVLGA LGNGIALCGF CFHMKTWKSS TIYLFNLAVA
DFLLMICLPL RTDYYLRRRH WIFGDIACRL VLFKLAMNRA GSIVFLTVVA VDRYFKVVHP
HHMVNAISNR TAAATACVLW TLVILGTVYL LMESHLCVQG TLSSCESFIM ESANGWHDVM
FQLEFFLPLT IILFCSVNVV WSLRRRQQLT RQARMRRATR FIMVVASVFI TCYLPSVLAR
LYFLWTVPTS ACDPSVHTAL HVTLSFTYLN SMLDPLVYYF SSPSLPKFYT KLTICSLKPK
RPGRTKTRRS EEMPISNLCS KSSIDGANRS QRPSDGQWDL QVC
