GP171_MOUSE
ID GP171_MOUSE Reviewed; 319 AA.
AC Q8BG55; Q8BTN1; Q8BY85; Q8CIF3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=G-protein coupled receptor 171;
GN Name=Gpr171;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 FUNCTION, LIGAND-BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=24043826; DOI=10.1073/pnas.1312938110;
RA Gomes I., Aryal D.K., Wardman J.H., Gupta A., Gagnidze K., Rodriguiz R.M.,
RA Kumar S., Wetsel W.C., Pintar J.E., Fricker L.D., Devi L.A.;
RT "GPR171 is a hypothalamic G protein-coupled receptor for BigLEN, a
RT neuropeptide involved in feeding.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16211-16216(2013).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=27117253; DOI=10.1126/scisignal.aad0694;
RA Gomes I., Bobeck E.N., Margolis E.B., Gupta A., Sierra S., Fakira A.K.,
RA Fujita W., Mueller T.D., Mueller A., Tschoep M.H., Kleinau G.,
RA Fricker L.D., Devi L.A.;
RT "Identification of GPR83 as the receptor for the neuroendocrine peptide
RT PEN.";
RL Sci. Signal. 9:ra43-ra43(2016).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND LIGAND-BINDING.
RX PubMed=28425495; DOI=10.1038/npp.2017.79;
RA Bobeck E.N., Gomes I., Pena D., Cummings K.A., Clem R.L., Mezei M.,
RA Devi L.A.;
RT "The BigLEN-GPR171 peptide receptor system within the basolateral amygdala
RT regulates anxiety-like behavior and contextual fear conditioning.";
RL Neuropsychopharmacology 42:2527-2536(2017).
RN [6]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=31308196; DOI=10.1124/jpet.119.259242;
RA McDermott M.V., Afrose L., Gomes I., Devi L.A., Bobeck E.N.;
RT "Opioid-induced signaling and antinociception are modulated by the recently
RT deorphanized receptor, GPR171.";
RL J. Pharmacol. Exp. Ther. 371:56-62(2019).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=34615877; DOI=10.1038/s41467-021-26135-9;
RA Fujiwara Y., Torphy R.J., Sun Y., Miller E.N., Ho F., Borcherding N.,
RA Wu T., Torres R.M., Zhang W., Schulick R.D., Zhu Y.;
RT "The GPR171 pathway suppresses T cell activation and limits antitumor
RT immunity.";
RL Nat. Commun. 12:5857-5857(2021).
CC -!- FUNCTION: G-protein coupled receptor for Big LEN, a 16-amino acid
CC neuropeptide produced from the precursor protein, proSAAS (encoded by
CC PCSK1N) (PubMed:24043826, PubMed:28425495). Acts through a G(i)-alpha-
CC mediated pathway in response to Big LEN (PubMed:24043826). Big LEN-
CC GPR171 system plays an important role in regulating feeding and
CC metabolism (PubMed:24043826). Also plays a role in modulating fear and
CC anxiety-like behaviors in the basolateral amygdala (PubMed:28425495).
CC Big LEN-GPR171 modulates the mu-type opioid receptor signaling and
CC antinociception (PubMed:31308196). Acts as a negative regulator T cell
CC function (PubMed:34615877). {ECO:0000269|PubMed:24043826,
CC ECO:0000269|PubMed:28425495, ECO:0000269|PubMed:31308196,
CC ECO:0000269|PubMed:34615877}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24043826,
CC ECO:0000269|PubMed:28425495}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Colocalized with GPR83 in the paraventricular
CC nucleus. {ECO:0000269|PubMed:27117253}.
CC -!- TISSUE SPECIFICITY: Highly expressed in hypothalamus, including the
CC arcuate nucleus, paraventricular nucleus and dorsomedial hypothalamus
CC (PubMed:24043826). Expressed in periaqueductal gray (at protein level),
CC found primarily in GABAergic neurons and to a lesser extent in
CC glutamatergic neurons (PubMed:31308196). Expressed in T cells and
CC natural killer cells (PubMed:34615877). {ECO:0000269|PubMed:24043826,
CC ECO:0000269|PubMed:31308196, ECO:0000269|PubMed:34615877}.
CC -!- INDUCTION: Induced upon antigen stimulation.
CC {ECO:0000269|PubMed:34615877}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit stronger antitumor
CC immunity. {ECO:0000269|PubMed:34615877}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AK041381; BAC30925.1; -; mRNA.
DR EMBL; AK041582; BAC30993.1; -; mRNA.
DR EMBL; AK089252; BAC40815.1; -; mRNA.
DR EMBL; AK089287; BAC40829.1; -; mRNA.
DR EMBL; AK154725; BAE32789.1; -; mRNA.
DR EMBL; BC024054; AAH24054.1; -; mRNA.
DR CCDS; CCDS17370.1; -.
DR RefSeq; NP_775574.1; NM_173398.3.
DR AlphaFoldDB; Q8BG55; -.
DR SMR; Q8BG55; -.
DR STRING; 10090.ENSMUSP00000082115; -.
DR GlyGen; Q8BG55; 1 site.
DR iPTMnet; Q8BG55; -.
DR PhosphoSitePlus; Q8BG55; -.
DR EPD; Q8BG55; -.
DR PaxDb; Q8BG55; -.
DR PRIDE; Q8BG55; -.
DR ProteomicsDB; 267749; -.
DR Antibodypedia; 18294; 323 antibodies from 31 providers.
DR DNASU; 229323; -.
DR Ensembl; ENSMUST00000085040; ENSMUSP00000082115; ENSMUSG00000050075.
DR GeneID; 229323; -.
DR KEGG; mmu:229323; -.
DR UCSC; uc008pij.2; mouse.
DR CTD; 29909; -.
DR MGI; MGI:2442043; Gpr171.
DR VEuPathDB; HostDB:ENSMUSG00000050075; -.
DR eggNOG; ENOG502QTCA; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q8BG55; -.
DR OMA; WHVFTNF; -.
DR OrthoDB; 1087125at2759; -.
DR PhylomeDB; Q8BG55; -.
DR TreeFam; TF330969; -.
DR BioGRID-ORCS; 229323; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8BG55; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BG55; protein.
DR Bgee; ENSMUSG00000050075; Expressed in peripheral lymph node and 55 other tissues.
DR Genevisible; Q8BG55; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:UniProtKB.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR GO; GO:0042923; F:neuropeptide binding; IDA:UniProtKB.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI.
DR GO; GO:0060259; P:regulation of feeding behavior; IMP:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..319
FT /note="G-protein coupled receptor 171"
FT /id="PRO_0000303237"
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..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 40..41
FT /note="Missing (in Ref. 1; BAC40815)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="I -> V (in Ref. 2; AAH24054)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="V -> A (in Ref. 1; BAC40815)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="S -> T (in Ref. 1; BAC30993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36720 MW; C2E0D658FB694364 CRC64;
MTNSSTFCPV YRDLEPFTYF FYLVFLIGII GSCFATWAFI QKTTNHRCVS IYLINLLTAD
FLLTLALPVK IIVDLGVAPW KLRIFHCQVT ACLIYINMYL SIIFLAFVSI DRCLQLIHSC
KIYRIQEPGF AKMISAVVWL MVLLIMVPNM VIPIKDIKEK SNVGCMEFKK EFGRNWHLLT
NFICVAIFLN FSVIILISNF LAIRQLYRNR DNTNYPSVKS ALLHILLVTA SYIICFVPYH
AVRIPYTLSQ TEVISDCSTR IALFKAKEAT LLLAVSNLCF DPILYYHLSK AFRLKVTETF
ASPKKSKPLE ERLRSENDV
