AGRG5_MOUSE
ID AGRG5_MOUSE Reviewed; 524 AA.
AC Q3V3Z3; A6H6A1; G5E8G8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2016, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Adhesion G-protein coupled receptor G5;
DE AltName: Full=G-protein coupled receptor 114;
DE AltName: Full=G-protein coupled receptor PGR27;
DE Flags: Precursor;
GN Name=Adgrg5; Synonyms=Gm1109, Gpr114, Pgr27;
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] (ISOFORM 2).
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 [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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 FUNCTION.
RX PubMed=22575658; DOI=10.1016/j.febslet.2012.03.014;
RA Gupte J., Swaminath G., Danao J., Tian H., Li Y., Wu X.;
RT "Signaling property study of adhesion G-protein-coupled receptors.";
RL FEBS Lett. 586:1214-1219(2012).
RN [6]
RP REVIEW.
RX PubMed=25713288; DOI=10.1124/pr.114.009647;
RA Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
RA Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A., Liebscher I.,
RA Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C., Piao X., Promel S.,
RA Schoneberg T., Schwartz T.W., Singer K., Stacey M., Ushkaryov Y.A.,
RA Vallon M., Wolfrum U., Wright M.W., Xu L., Langenhan T., Schioth H.B.;
RT "International union of basic and clinical pharmacology. XCIV. Adhesion G
RT protein-coupled receptors.";
RL Pharmacol. Rev. 67:338-367(2015).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP LEU-222 AND GLN-230.
RX PubMed=26499266; DOI=10.1096/fj.15-276220;
RA Wilde C., Fischer L., Lede V., Kirchberger J., Rothemund S.,
RA Schoeneberg T., Liebscher I.;
RT "The constitutive activity of the adhesion GPCR GPR114/ADGRG5 is mediated
RT by its tethered agonist.";
RL FASEB J. 30:666-673(2016).
CC -!- FUNCTION: Adhesion G protein-coupled receptor (GPCR). Transduces
CC intracellular signals through coupling to guanine nucleotide-binding
CC protein G(s) subunit alpha and activation of adenylate cyclase pathway
CC (PubMed:22575658). Isoform 1, but not isoform 2, is constitutively
CC active, as evidenced by elevated basal cAMP levels, and responds to
CC mechanical activation (shaking) (PubMed:26499266).
CC {ECO:0000269|PubMed:22575658, ECO:0000269|PubMed:26499266,
CC ECO:0000305|PubMed:25713288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26499266};
CC Multi-pass membrane protein {ECO:0000305|PubMed:25713288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3V3Z3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3V3Z3-2; Sequence=VSP_058541;
CC -!- TISSUE SPECIFICITY: Expressed at least in kidney, heart, brain and
CC spleen. In the kidney, both isoform 1 and isoform 2 are expressed at
CC similar levels. Isoform 1 is predominant in spleen, while isoform 2 is
CC the major form in heart and brain. {ECO:0000269|PubMed:26499266}.
CC -!- PTM: Autoproteolysis between residues Leu-222 and Thr-223 occurs in the
CC lumen of the endoplasmic reticulum during receptor biosynthesis. The N-
CC terminal fragment (NTF) subsequently reassociates with the C-terminal
CC fragment (CTF) either in a homogeneric heterodimerization, or with
CC another family member through heterogeneric heterodimerization.
CC Autocatalytic cleavage is thought to be critical for the maturation,
CC stability, trafficking, and function. {ECO:0000305|PubMed:25713288}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
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; AK028878; BAE20445.1; -; mRNA.
DR EMBL; AC129606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11153.1; -; Genomic_DNA.
DR EMBL; BC144851; AAI44852.1; -; mRNA.
DR EMBL; BC145803; AAI45804.1; -; mRNA.
DR CCDS; CCDS22552.1; -. [Q3V3Z3-2]
DR CCDS; CCDS52637.1; -. [Q3V3Z3-1]
DR RefSeq; NP_001028640.2; NM_001033468.3. [Q3V3Z3-2]
DR RefSeq; NP_001139444.1; NM_001145972.1. [Q3V3Z3-1]
DR RefSeq; XP_011246724.1; XM_011248422.1. [Q3V3Z3-2]
DR RefSeq; XP_017168373.1; XM_017312884.1. [Q3V3Z3-1]
DR RefSeq; XP_017168374.1; XM_017312885.1. [Q3V3Z3-1]
DR RefSeq; XP_017168375.1; XM_017312886.1. [Q3V3Z3-1]
DR AlphaFoldDB; Q3V3Z3; -.
DR SMR; Q3V3Z3; -.
DR STRING; 10090.ENSMUSP00000074155; -.
DR MEROPS; P02.016; -.
DR GlyGen; Q3V3Z3; 8 sites.
DR PhosphoSitePlus; Q3V3Z3; -.
DR EPD; Q3V3Z3; -.
DR PaxDb; Q3V3Z3; -.
DR PRIDE; Q3V3Z3; -.
DR ProteomicsDB; 282037; -. [Q3V3Z3-1]
DR ProteomicsDB; 282038; -. [Q3V3Z3-2]
DR Antibodypedia; 1937; 71 antibodies from 21 providers.
DR Ensembl; ENSMUST00000074570; ENSMUSP00000074155; ENSMUSG00000061577. [Q3V3Z3-2]
DR Ensembl; ENSMUST00000166802; ENSMUSP00000132628; ENSMUSG00000061577. [Q3V3Z3-1]
DR GeneID; 382045; -.
DR KEGG; mmu:382045; -.
DR UCSC; uc009mxi.2; mouse. [Q3V3Z3-1]
DR UCSC; uc009mxj.2; mouse.
DR CTD; 221188; -.
DR MGI; MGI:2685955; Adgrg5.
DR VEuPathDB; HostDB:ENSMUSG00000061577; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161359; -.
DR HOGENOM; CLU_002753_3_9_1; -.
DR InParanoid; Q3V3Z3; -.
DR OMA; HFALLSC; -.
DR OrthoDB; 501343at2759; -.
DR PhylomeDB; Q3V3Z3; -.
DR TreeFam; TF321769; -.
DR BioGRID-ORCS; 382045; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q3V3Z3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3V3Z3; protein.
DR Bgee; ENSMUSG00000061577; Expressed in mesenteric lymph node and 48 other tissues.
DR ExpressionAtlas; Q3V3Z3; baseline and differential.
DR Genevisible; Q3V3Z3; MM.
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; IPR003910; GPR1/GPR3/GPR5.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR01422; GPR56ORPHANR.
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 Alternative splicing; Cell membrane; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..524
FT /note="Adhesion G-protein coupled receptor G5"
FT /id="PRO_0000288638"
FT TOPO_DOM 24..246
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 247..267
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..305
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..319
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..340
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 352..372
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..413
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 414..434
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..476
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 477..480
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 481..500
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 182..235
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 222..223
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000305|PubMed:26499266"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 230
FT /note="Missing (in isoform 2)"
FT /id="VSP_058541"
FT MUTAGEN 222
FT /note="Missing: Drastic decrease in basal cAMP production."
FT /evidence="ECO:0000269|PubMed:26499266"
FT MUTAGEN 230
FT /note="Q->A,C,D,E,G,F,H,I,L,M,P,W,Y: Drastic reduction in
FT basal cAMP production."
FT /evidence="ECO:0000269|PubMed:26499266"
FT MUTAGEN 230
FT /note="Q->K,N,R,S: No effect on basal cAMP production."
FT /evidence="ECO:0000269|PubMed:26499266"
FT MUTAGEN 230
FT /note="Q->T,V: Small reduction in basal cAMP production."
FT /evidence="ECO:0000269|PubMed:26499266"
FT CONFLICT 79
FT /note="K -> N (in Ref. 1; BAE20445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 58675 MW; E1AE9C85BA11DDC7 CRC64;
MDPHGALFFY LCLLAAQVVL VETLSDLLVL MKRLEQPVGR GLSSRARHIH SLEQKLLNAS
FGGHNLTLQT NSIQSLVFKL SCDFPGLSLS STTLTNVSQV RAPHAMQFPA ELTKGACVTS
RPAELRLICI YFFTAHLFQD DRNSSLLNNY VLGAQLDHRP VNNLQKPVNI SFWHNRSLEG
YTVSCVFWKE GASKSSWGAW SPEGCYTEQP SATQVLCHCN HLTYFAVLMQ LSGDPVPAEL
QVPLEYISFV GCSISIVASL LTILLYAQSR KQSDSTTRIH MNLNGSVLLL NVTFLLSSQM
TLPTMPRPVC KVLAAVLHYA LLSSLTWMAI EGFNLYLFLG RVYNAYIRRY LLKLCMLGWG
FPALLVLLLL MIKSSVYGPC VTSLSKSQEN GTGFQNVSMC WIRSPMVHSI LVMGYGGFTS
LFNLVVLAWA LWILCRLRAR EKALSPWAYR DTAMVLGLTV LLGTTWTLAF FSFGVFLLPQ
LFLFTIFNSL YGFFLFLWFC SQKRYSDAEA KAEMEAVSSS QMTH
