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Database: UniProt
Entry: AGRG7_MOUSE
LinkDB: AGRG7_MOUSE
Original site: 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   27-MAR-2024, entry version 141.
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   GlyCosmos; Q8BM96; 12 sites, No reported glycans.
DR   GlyGen; Q8BM96; 12 sites.
DR   iPTMnet; Q8BM96; -.
DR   PhosphoSitePlus; Q8BM96; -.
DR   PaxDb; 10090-ENSMUSP00000023437; -.
DR   PeptideAtlas; Q8BM96; -.
DR   ProteomicsDB; 282040; -.
DR   Antibodypedia; 15851; 131 antibodies from 24 providers.
DR   DNASU; 239853; -.
DR   Ensembl; ENSMUST00000023437.5; ENSMUSP00000023437.5; ENSMUSG00000022755.5.
DR   GeneID; 239853; -.
DR   KEGG; mmu:239853; -.
DR   UCSC; uc007zmw.1; mouse.
DR   AGR; MGI:2441732; -.
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; RCTIVNF; -.
DR   OrthoDB; 5400300at2759; -.
DR   PhylomeDB; Q8BM96; -.
DR   TreeFam; TF351485; -.
DR   BioGRID-ORCS; 239853; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q8BM96; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8BM96; Protein.
DR   Bgee; ENSMUSG00000022755; Expressed in jejunum and 20 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   CDD; cd15257; 7tmB2_GPR128; 1.
DR   Gene3D; 2.60.220.50; -; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR046338; GAIN_dom_sf.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR047938; GPR128_7tmB2.
DR   InterPro; IPR000203; GPS.
DR   PANTHER; PTHR47767; ADHESION G PROTEIN-COUPLED RECEPTOR G7; 1.
DR   PANTHER; PTHR47767:SF1; ADHESION G-PROTEIN COUPLED RECEPTOR G7; 1.
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
//
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