AGRG7_MOUSE
ID AGRG7_MOUSE Reviewed; 785 AA.
AC Q8BM96; A2RSY9; Q80T42;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Adhesion G-protein coupled receptor G7;
DE AltName: Full=G-protein coupled receptor 128;
DE Flags: Precursor;
GN Name=Adgrg7; Synonyms=Gpr128;
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=Cecum;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-116.
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 PROTEIN SEQUENCE OF 39-53, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=24574718; DOI=10.3748/wjg.v20.i2.498;
RA Ni Y.Y., Chen Y., Lu S.Y., Sun B.Y., Wang F., Wu X.L., Dang S.Y.,
RA Zhang G.H., Zhang H.X., Kuang Y., Fei J., Gu M.M., Rong W.F., Wang Z.G.;
RT "Deletion of Gpr128 results in weight loss and increased intestinal
RT contraction frequency.";
RL World J. Gastroenterol. 20:498-508(2014).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in the intestinal tissues.
CC {ECO:0000269|PubMed:24574718}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit less body weight gain and
CC an increase in intestinal contraction frequency.
CC {ECO:0000269|PubMed:24574718}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
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DR EMBL; AK033593; BAC28377.1; -; mRNA.
DR EMBL; CT025158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466521; EDK98164.1; -; Genomic_DNA.
DR EMBL; BC132302; AAI32303.1; -; mRNA.
DR EMBL; BC137963; AAI37964.1; -; mRNA.
DR EMBL; AY255604; AAO85116.1; -; mRNA.
DR CCDS; CCDS28225.1; -.
DR RefSeq; NP_766413.2; NM_172825.3.
DR AlphaFoldDB; Q8BM96; -.
DR SMR; Q8BM96; -.
DR STRING; 10090.ENSMUSP00000023437; -.
DR MEROPS; P02.031; -.
DR GlyGen; Q8BM96; 12 sites.
DR iPTMnet; Q8BM96; -.
DR PhosphoSitePlus; Q8BM96; -.
DR PaxDb; Q8BM96; -.
DR PeptideAtlas; Q8BM96; -.
DR PRIDE; Q8BM96; -.
DR ProteomicsDB; 282040; -.
DR Antibodypedia; 15851; 109 antibodies from 24 providers.
DR DNASU; 239853; -.
DR Ensembl; ENSMUST00000023437; ENSMUSP00000023437; ENSMUSG00000022755.
DR GeneID; 239853; -.
DR KEGG; mmu:239853; -.
DR UCSC; uc007zmw.1; mouse.
DR CTD; 84873; -.
DR MGI; MGI:2441732; Adgrg7.
DR VEuPathDB; HostDB:ENSMUSG00000022755; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000159169; -.
DR HOGENOM; CLU_370321_0_0_1; -.
DR InParanoid; Q8BM96; -.
DR OMA; DLMKICQ; -.
DR OrthoDB; 349194at2759; -.
DR PhylomeDB; Q8BM96; -.
DR TreeFam; TF351485; -.
DR BioGRID-ORCS; 239853; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8BM96; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BM96; protein.
DR Bgee; ENSMUSG00000022755; Expressed in jejunum and 19 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..785
FT /note="Adhesion G-protein coupled receptor G7"
FT /id="PRO_0000012904"
FT TOPO_DOM 27..435
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 436..456
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 466..486
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..523
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 524..544
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..561
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 562..582
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..623
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 624..644
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 669..689
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..694
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 695..715
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 377..424
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 295
FT /note="L -> F (in Ref. 1; BAC28377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 87684 MW; 9CC84D14747704A7 CRC64;
MRSCRSCNVR VLVAIVCGLL TGIVLGLGIW RMVIRINRGI FVPVPSIPVQ FCRNGGTWQN
GRCICTEEWK GLRCTIANFC ENSTDGEFTF GSIPVGRYGP SLQTCEPGTL NAGSPKATRL
CNVSEFGNIE LQNVTKGSCN INLQTLEIQI NNQTASAENI SREAQVLTAD ASKLTAQNIT
SATTVVGQIF GKANNESQAK KTAIATVSQI LDASEDVFQK AAEMDNSKSF SNLIKQMENY
SYSQGDQTVV EPNIAIQSVT RDDNSGPSVL FSVQKGSSNS LVSGRILINK TANGLNPDGQ
TELQILLNTG ENRKSCGFMV YQNHKLFQSK TFTATSDFSQ KIISSKINES EQQRQNKVSV
EMVFNPTYDK RELRLHSYAC VYWNFLINDW DTQGCQKTGN TTEFLRCNCS HTTNFAVLMS
FKKDYKYPKS LDILSNIGCA LSIAGLALTI LFQILTRKIR KTSVTWVLVS LCSSMLIFNL
LFVFGIENSN KNLKTSDSDI NVKPENNKIP ESDTIETPNP SCTAIAALLH YFLLVTFTWN
GLSATQLYFL LIRTMKPLPR HFIIFISLVG WGVPAIIVGV TIGSIYALSG NKRYWELDYR
QEEICWLAVP KDNDYARSPL LWSFIIPVTI ILITNITIFV IITVKVLWKN NQNLTSTKKV
SSLKKVFSTL SIAVVFGVTW ILAYAMLISN DDIRIVFSYI FCLFNTTQGL QIFILYTVRT
KVFQSEASKI LKSLSSSFDR TKPMPSITPL KLRVRMYNML RSLPSLNERF RLLEPSGMTE
ETSLS