GP176_MOUSE
ID GP176_MOUSE Reviewed; 515 AA.
AC Q80WT4; Q80UC4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=G-protein coupled receptor 176;
DE AltName: Full=G-protein coupled receptor AGR9;
GN Name=Gpr176; Synonyms=Agr9, Gm1012;
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; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-261.
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 140-ASP-ARG-141 AND VAL-145.
RX PubMed=26882873; DOI=10.1038/ncomms10583;
RA Doi M., Murai I., Kunisue S., Setsu G., Uchio N., Tanaka R., Kobayashi S.,
RA Shimatani H., Hayashi H., Chao H.W., Nakagawa Y., Takahashi Y., Hotta Y.,
RA Yasunaga J., Matsuoka M., Hastings M.H., Kiyonari H., Okamura H.;
RT "Gpr176 is a Gz-linked orphan G-protein-coupled receptor that sets the pace
RT of circadian behaviour.";
RL Nat. Commun. 7:10583-10583(2016).
CC -!- FUNCTION: Orphan receptor involved in normal circadian rhythm behavior
CC (PubMed:26882873). Acts through the G-protein subclass G(z)-alpha and
CC has an agonist-independent basal activity to repress cAMP production
CC (PubMed:26882873). {ECO:0000269|PubMed:26882873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26882873};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain, with prominent
CC expression in the SCN (at protein level) (PubMed:26882873).
CC {ECO:0000269|PubMed:26882873}.
CC -!- DEVELOPMENTAL STAGE: Fluctuates in a circadian fashion, with highest
CC level in night and lowest in the morning (at protein level).
CC {ECO:0000269|PubMed:26882873}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit a significantly shorter
CC circadian period. {ECO:0000269|PubMed:26882873}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC052037; AAH52037.1; -; mRNA.
DR EMBL; AY255554; AAO85066.1; -; mRNA.
DR CCDS; CCDS16575.1; -.
DR RefSeq; NP_958755.1; NM_201367.3.
DR AlphaFoldDB; Q80WT4; -.
DR SMR; Q80WT4; -.
DR STRING; 10090.ENSMUSP00000037586; -.
DR GlyGen; Q80WT4; 4 sites.
DR iPTMnet; Q80WT4; -.
DR PhosphoSitePlus; Q80WT4; -.
DR MaxQB; Q80WT4; -.
DR PaxDb; Q80WT4; -.
DR PRIDE; Q80WT4; -.
DR ProteomicsDB; 271426; -.
DR Antibodypedia; 9997; 187 antibodies from 28 providers.
DR DNASU; 381413; -.
DR Ensembl; ENSMUST00000039160; ENSMUSP00000037586; ENSMUSG00000040133.
DR GeneID; 381413; -.
DR KEGG; mmu:381413; -.
DR UCSC; uc008lru.2; mouse.
DR CTD; 11245; -.
DR MGI; MGI:2685858; Gpr176.
DR VEuPathDB; HostDB:ENSMUSG00000040133; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000182998; -.
DR HOGENOM; CLU_045778_0_0_1; -.
DR InParanoid; Q80WT4; -.
DR OMA; MVMIFIF; -.
DR OrthoDB; 602137at2759; -.
DR PhylomeDB; Q80WT4; -.
DR TreeFam; TF331506; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR BioGRID-ORCS; 381413; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Gpr176; mouse.
DR PRO; PR:Q80WT4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80WT4; protein.
DR Bgee; ENSMUSG00000040133; Expressed in vault of skull and 122 other tissues.
DR Genevisible; Q80WT4; 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:0004930; F:G protein-coupled receptor activity; IDA:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:MGI.
DR GO; GO:0048512; P:circadian behavior; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR CDD; cd15006; 7tmA_GPR176; 1.
DR InterPro; IPR043523; GPCR_176_Rhodpsn_7TM.
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 Biological rhythms; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..515
FT /note="G-protein coupled receptor 176"
FT /id="PRO_0000069657"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..108
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..204
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 205..225
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 226..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..301
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..515
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 407..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 140..141
FT /note="DR->RD: Decreases expression; No reduction of cAMP
FT upon induction."
FT /evidence="ECO:0000269|PubMed:26882873"
FT MUTAGEN 145
FT /note="V->R: No reduction of cAMP upon induction."
FT /evidence="ECO:0000269|PubMed:26882873"
SQ SEQUENCE 515 AA; 57143 MW; 81D9B48CE5C4BB70 CRC64;
MGHNSSWVSP NTSHPRNTSG AEAGANLSAF GELSEAQLYR QFTTTVQVVI FIGSLLGNFM
VLWSTCRTTV FKSVTNRFIK NLACSGICAS VVCVPFDIIL SSSPHCCWWI YTMLFCKVLK
FLHKVFCSVT VLSFPAIALD RYYSVLYPLE RKISDAKSRE LVMYIWAHAV VASVPVFAVT
NVADIYAMST CTEVWSNSLG HLVYVLIYNV TTVIVPVAVV FLFLILIRRA LSASQKKKVI
IAALRTPQNT ISIPYASQRE AELHATLLSM VTVFILCSVP YATLVVYQTV LNVPNTSVFL
LLTAIWLPKV SLLANPVLFL TVNKSVRKCL VGTLVQLHHR YSRRNVVSTG SGVAEPSLEP
SMRSGSQLLE MFHIGQQQIF KPSEDEEESE AKYLGSADFQ AKEVLTSCPE GEQEPPQLAP
SVPPPGTVDS EPRVSPVAPM ESGIFPDKYS LQFGFGPFEL PPQWLSETRN SKKRLLPPLG
NTPEELIQTK VPRVNRVERK MSRNNKVSIF PKVDS
