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Adhesion G protein-coupled receptor A2 (G-protein coupled receptor 124) (Tumor endothelial marker 5)

 AGRA2_HUMAN             Reviewed;        1338 AA.
Q96PE1; A6H8W3; D3DSW4; Q8N3R1; Q8TEM3; Q96KB2; Q9P1Z7; Q9UFY4;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
20-JAN-2009, sequence version 2.
18-JUL-2018, entry version 158.
RecName: Full=Adhesion G protein-coupled receptor A2 {ECO:0000312|HGNC:HGNC:17849};
AltName: Full=G-protein coupled receptor 124 {ECO:0000312|HGNC:HGNC:17849};
AltName: Full=Tumor endothelial marker 5 {ECO:0000303|PubMed:11559528};
Flags: Precursor;
Name=ADGRA2 {ECO:0000312|HGNC:HGNC:17849};
Synonyms=GPR124, KIAA1531 {ECO:0000312|HGNC:HGNC:17849},
TEM5 {ECO:0000303|PubMed:11559528};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11559528;
Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B.,
Kinzler K.W., St Croix B.;
"Cell surface tumor endothelial markers are conserved in mice and
humans.";
Cancer Res. 61:6649-6655(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10819331; DOI=10.1093/dnares/7.2.143;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:143-150(2000).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-1338 (ISOFORM 1).
PubMed=12565841; DOI=10.1016/S0006-291X(03)00026-3;
Fredriksson R., Gloriam D.E.I., Hoeglund P.J., Lagerstroem M.C.,
Schioeth H.B.;
"There exist at least 30 human G-protein-coupled receptors with long
Ser/Thr-rich N-termini.";
Biochem. Biophys. Res. Commun. 301:725-734(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-1338 (ISOFORM 1).
TISSUE=Spleen;
Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
"The nucleotide sequence of a long cDNA clone isolated from human
spleen.";
Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 370-374 AND 399-403, SUBCELLULAR LOCATION,
PROTEOLYTIC CLEAVAGE, PRESENCE OF DISULFIDE BONDS, TOPOLOGY, AND
MUTAGENESIS OF ARG-369 AND ARG-398.
PubMed=22013897; DOI=10.1042/BJ20111682;
Vallon M., Aubele P., Janssen K.P., Essler M.;
"Thrombin-induced shedding of tumour endothelial marker 5 and exposure
of its RGD motif are regulated by cell-surface protein disulfide-
isomerase.";
Biochem. J. 441:937-944(2012).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 850-1338.
TISSUE=Amygdala, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[12]
TISSUE SPECIFICITY, INTERACTION WITH DLG1, MOTIF PDZ-BINDING, AND
MUTAGENESIS OF 1335-GLU--VAL-1338.
PubMed=15021905; DOI=10.1038/sj.onc.1207495;
Yamamoto Y., Irie K., Asada M., Mino A., Mandai K., Takai Y.;
"Direct binding of the human homologue of the Drosophila disc large
tumor suppressor gene to seven-pass transmembrane proteins, tumor
endothelial marker 5 (TEM5), and a novel TEM5-like protein.";
Oncogene 23:3889-3897(2004).
[13]
FUNCTION, INTERACTION WITH ITGAV AND ITGB3, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, PROTEOLYTIC CLEAVAGE, TOPOLOGY, AND MOTIF RGD.
PubMed=16982628; DOI=10.1074/jbc.M605291200;
Vallon M., Essler M.;
"Proteolytically processed soluble tumor endothelial marker (TEM) 5
mediates endothelial cell survival during angiogenesis by linking
integrin alpha(v)beta3 to glycosaminoglycans.";
J. Biol. Chem. 281:34179-34188(2006).
[14]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND TOPOLOGY.
PubMed=21421844; DOI=10.1073/pnas.1017192108;
Cullen M., Elzarrad M.K., Seaman S., Zudaire E., Stevens J.,
Yang M.Y., Li X., Chaudhary A., Xu L., Hilton M.B., Logsdon D.,
Hsiao E., Stein E.V., Cuttitta F., Haines D.C., Nagashima K.,
Tessarollo L., St Croix B.;
"GPR124, an orphan G protein-coupled receptor, is required for CNS-
specific vascularization and establishment of the blood-brain
barrier.";
Proc. Natl. Acad. Sci. U.S.A. 108:5759-5764(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANT LEU-29.
PubMed=24501278; DOI=10.1093/hmg/ddu056;
Lee H., Lin M.C., Kornblum H.I., Papazian D.M., Nelson S.F.;
"Exome sequencing identifies de novo gain of function missense
mutation in KCND2 in identical twins with autism and seizures that
slows potassium channel inactivation.";
Hum. Mol. Genet. 23:3481-3489(2014).
[17]
VARIANT LYS-375.
PubMed=24925318; DOI=10.1093/hmg/ddu296;
Di Costanzo S., Balasubramanian A., Pond H.L., Rozkalne A.,
Pantaleoni C., Saredi S., Gupta V.A., Sunu C.M., Yu T.W., Kang P.B.,
Salih M.A., Mora M., Gussoni E., Walsh C.A., Manzini M.C.;
"POMK mutations disrupt muscle development leading to a spectrum of
neuromuscular presentations.";
Hum. Mol. Genet. 23:5781-5792(2014).
-!- FUNCTION: Endothelial receptor which functions as a WNT7-specific
coactivator of canonical Wnt signaling (By similarity). Required
for normal endothelial cell sprouting and migration in the
forebrain and neural tube (By similarity). Has a major role in
establishing the blood-brain barrier (By similarity). Binds to the
glycosaminoglycans heparin, heparin sulfate, chondroitin sulfate
and dermatan sulfate (PubMed:16982628).
{ECO:0000250|UniProtKB:Q91ZV8, ECO:0000269|PubMed:22013897}.
-!- SUBUNIT: Interacts (via PDZ-binding motif) with DLG1 (via PDZ
domains) (PubMed:15021905). The cleaved extracellular subunit
interacts with the integrin heterodimer ITGAV:ITGB3
(PubMed:16982628). {ECO:0000269|PubMed:15021905,
ECO:0000269|PubMed:16982628}.
-!- INTERACTION:
Q12959:DLG1; NbExp=2; IntAct=EBI-10893263, EBI-357481;
Q12959-2:DLG1; NbExp=2; IntAct=EBI-10893263, EBI-357500;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16982628,
ECO:0000269|PubMed:21421844, ECO:0000269|PubMed:22013897}; Multi-
pass membrane protein {ECO:0000255}. Cell projection, filopodium
{ECO:0000269|PubMed:21421844}. Note=Enriched at lateral cell
borders and also at sites of cell-ECM (extracellular matrix)
contact. {ECO:0000269|PubMed:21421844}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96PE1-1; Sequence=Displayed;
Name=2;
IsoId=Q96PE1-2; Sequence=VSP_010076;
Name=3;
IsoId=Q96PE1-3; Sequence=VSP_036215;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in endothelial cells (at protein
level) (PubMed:15021905, PubMed:16982628). Abundantly expressed in
heart, placenta, ovary, small intestine, and colon
(PubMed:15021905). {ECO:0000269|PubMed:15021905,
ECO:0000269|PubMed:16982628}.
-!- DOMAIN: The leucine-rich repeats (LRRs) are important for
potentiation of WNT7 signaling. {ECO:0000250|UniProtKB:Q91ZV8}.
-!- DOMAIN: The RGD motif is involved in integrin ITGAV:ITGB3 binding.
{ECO:0000269|PubMed:16982628}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:21421844}.
-!- PTM: Proteolytically cleaved into two subunits, an extracellular
subunit and a seven-transmembrane subunit (PubMed:22013897,
PubMed:16982628). Cleaved by thrombin (F2) and MMP1
(PubMed:22013897). Also cleaved by MMP9, with lower efficiency
(PubMed:22013897, PubMed:16982628). Presence of the protein
disulfide-isomerase P4HB at the cell surface is additionally
required for shedding of the extracellular subunit, suggesting
that the subunits are linked by disulfide bonds (PubMed:22013897).
Shedding is enhanced by the growth factor FGF2 and may promote
cell survival during angiogenesis (PubMed:16982628).
{ECO:0000269|PubMed:16982628, ECO:0000269|PubMed:22013897}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
Adhesion G-protein coupled receptor (ADGR) subfamily.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI46775.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL11992.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAO27354.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA96055.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF378755; AAL11992.1; ALT_INIT; mRNA.
EMBL; AB040964; BAA96055.2; ALT_INIT; mRNA.
EMBL; AK027296; BAB55022.1; -; mRNA.
EMBL; AC138356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63355.1; -; Genomic_DNA.
EMBL; CH471080; EAW63356.1; -; Genomic_DNA.
EMBL; BC146774; AAI46775.1; ALT_INIT; mRNA.
EMBL; AY181242; AAO27354.1; ALT_INIT; mRNA.
EMBL; AK074099; BAB84925.2; -; mRNA.
EMBL; AL110244; CAB53694.1; -; mRNA.
EMBL; AL832524; CAD38629.1; -; mRNA.
CCDS; CCDS6097.2; -. [Q96PE1-1]
PIR; T14774; T14774.
RefSeq; NP_116166.9; NM_032777.9. [Q96PE1-1]
UniGene; Hs.274136; -.
ProteinModelPortal; Q96PE1; -.
SMR; Q96PE1; -.
BioGrid; 117450; 2.
IntAct; Q96PE1; 3.
MINT; Q96PE1; -.
STRING; 9606.ENSP00000406367; -.
iPTMnet; Q96PE1; -.
PhosphoSitePlus; Q96PE1; -.
BioMuta; GPR124; -.
DMDM; 221222450; -.
PaxDb; Q96PE1; -.
PeptideAtlas; Q96PE1; -.
PRIDE; Q96PE1; -.
ProteomicsDB; 77674; -.
ProteomicsDB; 77675; -. [Q96PE1-2]
ProteomicsDB; 77676; -. [Q96PE1-3]
Ensembl; ENST00000315215; ENSP00000323508; ENSG00000020181. [Q96PE1-2]
Ensembl; ENST00000412232; ENSP00000406367; ENSG00000020181. [Q96PE1-1]
GeneID; 25960; -.
KEGG; hsa:25960; -.
UCSC; uc003xkj.4; human. [Q96PE1-1]
CTD; 25960; -.
DisGeNET; 25960; -.
EuPathDB; HostDB:ENSG00000020181.17; -.
GeneCards; ADGRA2; -.
HGNC; HGNC:17849; ADGRA2.
HPA; HPA012393; -.
MIM; 606823; gene.
neXtProt; NX_Q96PE1; -.
OpenTargets; ENSG00000020181; -.
PharmGKB; PA134869404; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00920000148954; -.
HOVERGEN; HBG051777; -.
InParanoid; Q96PE1; -.
KO; K08461; -.
OMA; RTLCAYP; -.
OrthoDB; EOG091G03GB; -.
PhylomeDB; Q96PE1; -.
TreeFam; TF331206; -.
ChiTaRS; ADGRA2; human.
GeneWiki; GPR124; -.
GenomeRNAi; 25960; -.
PRO; PR:Q96PE1; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000020181; -.
CleanEx; HS_GPR124; -.
ExpressionAtlas; Q96PE1; baseline and differential.
Genevisible; Q96PE1; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:GDB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:GDB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:GDB.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0050920; P:regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0090210; P:regulation of establishment of blood-brain barrier; IEA:Ensembl.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 1.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR000203; GPS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF01825; GPS; 1.
Pfam; PF13855; LRR_8; 1.
SMART; SM00409; IG; 1.
SMART; SM00369; LRR_TYP; 4.
SMART; SM00082; LRRCT; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51450; LRR; 4.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Cell membrane; Cell projection;
Complete proteome; Direct protein sequencing; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Immunoglobulin domain;
Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 1338 Adhesion G protein-coupled receptor A2.
/FTId=PRO_0000012898.
TOPO_DOM 34 771 Extracellular.
{ECO:0000305|PubMed:16982628,
ECO:0000305|PubMed:21421844,
ECO:0000305|PubMed:22013897}.
TRANSMEM 772 792 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 793 807 Cytoplasmic. {ECO:0000255}.
TRANSMEM 808 828 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 829 832 Extracellular. {ECO:0000255}.
TRANSMEM 833 853 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 854 886 Cytoplasmic. {ECO:0000255}.
TRANSMEM 887 907 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 908 924 Extracellular. {ECO:0000255}.
TRANSMEM 925 945 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 946 1019 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1020 1040 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 1041 1047 Extracellular. {ECO:0000255}.
TRANSMEM 1048 1068 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 1069 1338 Cytoplasmic.
{ECO:0000269|PubMed:21421844}.
REPEAT 82 106 LRR 1. {ECO:0000255}.
REPEAT 107 130 LRR 2. {ECO:0000255}.
REPEAT 131 154 LRR 3. {ECO:0000255}.
REPEAT 156 178 LRR 4. {ECO:0000255}.
DOMAIN 190 240 LRRCT. {ECO:0000255}.
DOMAIN 247 344 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 707 758 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
MOTIF 362 364 RGD. {ECO:0000269|PubMed:16982628}.
MOTIF 1335 1338 PDZ-binding.
{ECO:0000269|PubMed:15021905}.
SITE 369 370 Cleavage; by thrombin.
{ECO:0000269|PubMed:22013897}.
SITE 398 399 Cleavage; by thrombin.
{ECO:0000269|PubMed:22013897}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 602 602 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 268 328 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 186 1338 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_036215.
VAR_SEQ 537 753 Missing (in isoform 2).
{ECO:0000303|PubMed:10819331,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010076.
VARIANT 29 29 P -> L (found in a family with atypical
autism and severe epilepsy; unknown
pathological significance).
{ECO:0000269|PubMed:24501278}.
/FTId=VAR_072079.
VARIANT 375 375 T -> K. {ECO:0000269|PubMed:24925318}.
/FTId=VAR_072561.
MUTAGEN 369 369 R->A: Minimal effect on thrombin
cleavage. Abolishes thrombin cleavage;
when associated with G-398.
{ECO:0000269|PubMed:22013897}.
MUTAGEN 398 398 R->G: Minimal effect on thrombin
cleavage. Abolishes thrombin cleavage;
when associated with A-369.
{ECO:0000269|PubMed:22013897}.
MUTAGEN 1335 1338 Missing: Fails to interact with DLG1.
{ECO:0000269|PubMed:15021905}.
CONFLICT 407 407 G -> S (in Ref. 9; BAB84925).
{ECO:0000305}.
CONFLICT 1221 1221 S -> G (in Ref. 2; BAA96055 and 7;
AAI46775). {ECO:0000305}.
SEQUENCE 1338 AA; 142647 MW; 322838CB31E99A97 CRC64;
MGAGGRRMRG APARLLLPLL PWLLLLLAPE ARGAPGCPLS IRSCKCSGER PKGLSGGVPG
PARRRVVCSG GDLPEPPEPG LLPNGTVTLL LSNNKITGLR NGSFLGLSLL EKLDLRNNII
STVQPGAFLG LGELKRLDLS NNRIGCLTSE TFQGLPRLLR LNISGNIFSS LQPGVFDELP
ALKVVDLGTE FLTCDCHLRW LLPWAQNRSL QLSEHTLCAY PSALHAQALG SLQEAQLCCE
GALELHTHHL IPSLRQVVFQ GDRLPFQCSA SYLGNDTRIR WYHNRAPVEG DEQAGILLAE
SLIHDCTFIT SELTLSHIGV WASGEWECTV SMAQGNASKK VEIVVLETSA SYCPAERVAN
NRGDFRWPRT LAGITAYQSC LQYPFTSVPL GGGAPGTRAS RRCDRAGRWE PGDYSHCLYT
NDITRVLYTF VLMPINASNA LTLAHQLRVY TAEAASFSDM MDVVYVAQMI QKFLGYVDQI
KELVEVMVDM ASNLMLVDEH LLWLAQREDK ACSRIVGALE RIGGAALSPH AQHISVNARN
VALEAYLIKP HSYVGLTCTA FQRREGGVPG TRPGSPGQNP PPEPEPPADQ QLRFRCTTGR
PNVSLSSFHI KNSVALASIQ LPPSLFSSLP AALAPPVPPD CTLQLLVFRN GRLFHSHSNT
SRPGAAGPGK RRGVATPVIF AGTSGCGVGN LTEPVAVSLR HWAEGAEPVA AWWSQEGPGE
AGGWTSEGCQ LRSSQPNVSA LHCQHLGNVA VLMELSAFPR EVGGAGAGLH PVVYPCTALL
LLCLFATIIT YILNHSSIRV SRKGWHMLLN LCFHIAMTSA VFAGGITLTN YQMVCQAVGI
TLHYSSLSTL LWMGVKARVL HKELTWRAPP PQEGDPALPT PSPMLRFYLI AGGIPLIICG
ITAAVNIHNY RDHSPYCWLV WRPSLGAFYI PVALILLITW IYFLCAGLRL RGPLAQNPKA
GNSRASLEAG EELRGSTRLR GSGPLLSDSG SLLATGSARV GTPGPPEDGD SLYSPGVQLG
ALVTTHFLYL AMWACGALAV SQRWLPRVVC SCLYGVAASA LGLFVFTHHC ARRRDVRASW
RACCPPASPA APHAPPRALP AAAEDGSPVF GEGPPSLKSS PSGSSGHPLA LGPCKLTNLQ
LAQSQVCEAG AAAGGEGEPE PAGTRGNLAH RHPNNVHHGR RAHKSRAKGH RAGEACGKNR
LKALRGGAAG ALELLSSESG SLHNSPTDSY LGSSRNSPGA GLQLEGEPML TPSEGSDTSA
APLSEAGRAG QRRSASRDSL KGGGALEKES HRRSYPLNAA SLNGAPKGGK YDDVTLMGAE
VASGGCMKTG LWKSETTV


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