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Adhesion G-protein coupled receptor G5 (G-protein coupled receptor 114) (G-protein coupled receptor PGR27)

 AGRG5_MOUSE             Reviewed;         524 AA.
Q3V3Z3; A6H6A1; G5E8G8;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
05-OCT-2016, sequence version 3.
25-OCT-2017, entry version 90.
RecName: Full=Adhesion G-protein coupled receptor G5;
AltName: Full=G-protein coupled receptor 114;
AltName: Full=G-protein coupled receptor PGR27;
Flags: Precursor;
Name=Adgrg5; Synonyms=Gm1109, Gpr114, Pgr27;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=22575658; DOI=10.1016/j.febslet.2012.03.014;
Gupte J., Swaminath G., Danao J., Tian H., Li Y., Wu X.;
"Signaling property study of adhesion G-protein-coupled receptors.";
FEBS Lett. 586:1214-1219(2012).
[6]
REVIEW.
PubMed=25713288; DOI=10.1124/pr.114.009647;
Hamann J., Aust G., Arac D., Engel F.B., Formstone C., Fredriksson R.,
Hall R.A., Harty B.L., Kirchhoff C., Knapp B., Krishnan A.,
Liebscher I., Lin H.H., Martinelli D.C., Monk K.R., Peeters M.C.,
Piao X., Promel S., Schoneberg T., Schwartz T.W., Singer K.,
Stacey M., Ushkaryov Y.A., Vallon M., Wolfrum U., Wright M.W., Xu L.,
Langenhan T., Schioth H.B.;
"International union of basic and clinical pharmacology. XCIV.
Adhesion G protein-coupled receptors.";
Pharmacol. Rev. 67:338-367(2015).
[7]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
LEU-222 AND GLN-230.
PubMed=26499266; DOI=10.1096/fj.15-276220;
Wilde C., Fischer L., Lede V., Kirchberger J., Rothemund S.,
Schoeneberg T., Liebscher I.;
"The constitutive activity of the adhesion GPCR GPR114/ADGRG5 is
mediated by its tethered agonist.";
FASEB J. 30:666-673(2016).
-!- FUNCTION: Adhesion G protein-coupled receptor (GPCR). Transduces
intracellular signals through coupling to guanine nucleotide-
binding protein G(s) subunit alpha and activation of adenylate
cyclase pathway (PubMed:22575658). Isoform 1, but not isoform 2,
is constitutively active, as evidenced by elevated basal cAMP
levels, and responds to mechanical activation (shaking)
(PubMed:26499266). {ECO:0000269|PubMed:22575658,
ECO:0000269|PubMed:26499266, ECO:0000305|PubMed:25713288}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26499266};
Multi-pass membrane protein {ECO:0000305|PubMed:25713288}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3V3Z3-1; Sequence=Displayed;
Name=2;
IsoId=Q3V3Z3-2; Sequence=VSP_058541;
Note=May be due to competing acceptor splice site.;
-!- TISSUE SPECIFICITY: Expressed at least in kidney, heart, brain and
spleen. In the kidney, both isoform 1 and isoform 2 are expressed
at similar levels. Isoform 1 is predominant in spleen, while
isoform 2 is the major form in heart and brain.
{ECO:0000269|PubMed:26499266}.
-!- PTM: Autoproteolysis between residues Leu-222 and Thr-223 occurs
in the lumen of the endoplasmic reticulum during receptor
biosynthesis. The N-terminal fragment (NTF) subsequently
reassociates with the C-terminal fragment (CTF) either in a
homogeneric heterodimerization, or with another family member
through heterogeneric heterodimerization. Autocatalytic cleavage
is thought to be critical for the maturation, stability,
trafficking, and function. {ECO:0000305|PubMed:25713288}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
Adhesion G-protein coupled receptor (ADGR) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK028878; BAE20445.1; -; mRNA.
EMBL; AC129606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466525; EDL11153.1; -; Genomic_DNA.
EMBL; BC144851; AAI44852.1; -; mRNA.
EMBL; BC145803; AAI45804.1; -; mRNA.
CCDS; CCDS22552.1; -. [Q3V3Z3-2]
CCDS; CCDS52637.1; -. [Q3V3Z3-1]
RefSeq; NP_001028640.2; NM_001033468.3. [Q3V3Z3-2]
RefSeq; NP_001139444.1; NM_001145972.1. [Q3V3Z3-1]
RefSeq; XP_011246724.1; XM_011248422.1. [Q3V3Z3-2]
RefSeq; XP_017168373.1; XM_017312884.1. [Q3V3Z3-1]
RefSeq; XP_017168374.1; XM_017312885.1. [Q3V3Z3-1]
RefSeq; XP_017168375.1; XM_017312886.1. [Q3V3Z3-1]
UniGene; Mm.334726; -.
ProteinModelPortal; Q3V3Z3; -.
STRING; 10090.ENSMUSP00000132628; -.
MEROPS; P02.016; -.
PhosphoSitePlus; Q3V3Z3; -.
PaxDb; Q3V3Z3; -.
PRIDE; Q3V3Z3; -.
Ensembl; ENSMUST00000074570; ENSMUSP00000074155; ENSMUSG00000061577. [Q3V3Z3-2]
Ensembl; ENSMUST00000166802; ENSMUSP00000132628; ENSMUSG00000061577. [Q3V3Z3-1]
GeneID; 382045; -.
KEGG; mmu:382045; -.
UCSC; uc009mxi.2; mouse. [Q3V3Z3-1]
UCSC; uc009mxj.2; mouse.
CTD; 221188; -.
MGI; MGI:2685955; Adgrg5.
eggNOG; KOG4193; Eukaryota.
eggNOG; ENOG410XSD2; LUCA.
GeneTree; ENSGT00900000140853; -.
HOVERGEN; HBG107961; -.
InParanoid; Q3V3Z3; -.
KO; K08459; -.
OMA; FLFLWFC; -.
OrthoDB; EOG091G090X; -.
PhylomeDB; Q3V3Z3; -.
TreeFam; TF321769; -.
PRO; PR:Q3V3Z3; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000061577; -.
CleanEx; MM_GPR114; -.
ExpressionAtlas; Q3V3Z3; baseline and differential.
Genevisible; Q3V3Z3; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR003910; GPR1/GPR3/GPR5.
InterPro; IPR000203; GPS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF01825; GPS; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR01422; GPR56ORPHANR.
SMART; SM00303; GPS; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 524 Adhesion G-protein coupled receptor G5.
/FTId=PRO_0000288638.
TOPO_DOM 24 246 Extracellular. {ECO:0000305}.
TRANSMEM 247 267 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 268 284 Cytoplasmic. {ECO:0000305}.
TRANSMEM 285 305 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 306 319 Extracellular. {ECO:0000305}.
TRANSMEM 320 340 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 341 351 Cytoplasmic. {ECO:0000305}.
TRANSMEM 352 372 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 373 413 Extracellular. {ECO:0000305}.
TRANSMEM 414 434 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 435 453 Cytoplasmic. {ECO:0000305}.
TRANSMEM 454 476 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 477 480 Extracellular. {ECO:0000305}.
TRANSMEM 481 500 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 501 524 Cytoplasmic. {ECO:0000305}.
DOMAIN 182 235 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
SITE 222 223 Cleavage; by autolysis.
{ECO:0000305|PubMed:26499266}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 143 143 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 390 390 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 230 230 Missing (in isoform 2).
/FTId=VSP_058541.
MUTAGEN 222 222 Missing: Drastic decrease in basal cAMP
production.
{ECO:0000269|PubMed:26499266}.
MUTAGEN 230 230 Q->A,C,D,E,G,F,H,I,L,M,P,W,Y: Drastic
reduction in basal cAMP production.
{ECO:0000269|PubMed:26499266}.
MUTAGEN 230 230 Q->K,N,R,S: No effect on basal cAMP
production.
{ECO:0000269|PubMed:26499266}.
MUTAGEN 230 230 Q->T,V: Small reduction in basal cAMP
production.
{ECO:0000269|PubMed:26499266}.
CONFLICT 79 79 K -> N (in Ref. 1; BAE20445).
{ECO:0000305}.
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


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