GenomeNet

Database: UniProt
Entry: Q2Q426
LinkDB: Q2Q426
Original site: Q2Q426 
ID   AGRE2_MACMU             Reviewed;         822 AA.
AC   Q2Q426;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 84.
DE   RecName: Full=Adhesion G protein-coupled receptor E2;
DE   AltName: Full=EGF-like module receptor 2;
DE   AltName: Full=EGF-like module-containing mucin-like hormone receptor-like 2;
DE   AltName: CD_antigen=CD312;
DE   Flags: Precursor;
GN   Name=ADGRE2; Synonyms=EMR2;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kwakkenbos M.J., Matmati M., Pouwels W., Wang Y., Bontrop R.E.,
RA   Heidt P.J., Hoek R.M., Hamann J.;
RT   "A unique mode of concerted evolution of the EGF-TM7 receptor chimera
RT   EMR2.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell surface receptor that binds to the chondroitin
CC       sulfate moiety of glycosaminoglycan chains and promotes cell
CC       attachment. Promotes granulocyte chemotaxis, degranulation and
CC       adhesion. In macrophages, promotes the release of inflammatory
CC       cytokines, including IL8 and TNF. Signals probably through G-
CC       proteins. {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region non-covalently linked to a seven-transmembrane moiety.
CC       Interacts with chondroitin sulfate; the interaction with
CC       chondroitin sulfate is calcium-dependent. Interacts with CD55 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q9UHX3}; Multi-pass membrane protein. Cell
CC       projection, ruffle membrane {ECO:0000250|UniProtKB:Q9UHX3}; Multi-
CC       pass membrane protein {ECO:0000250}. Note=Localized at the leading
CC       edge of migrating cells. {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- DOMAIN: The GPS domain is necessary, but not sufficient for
CC       receptor cleavage, which require the entire extracellular stalk.
CC       {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth
CC       EGF domain. {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- PTM: Autoproteolytically cleaved into 2 subunits, an extracellular
CC       alpha subunit and a seven-transmembrane beta subunit.
CC       {ECO:0000250|UniProtKB:Q9UHX3}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       Adhesion G-protein coupled receptor (ADGR) subfamily.
CC       {ECO:0000305}.
DR   EMBL; DQ227271; ABB53642.1; -; mRNA.
DR   RefSeq; NP_001033751.1; NM_001038662.1.
DR   UniGene; Mmu.9556; -.
DR   ProteinModelPortal; Q2Q426; -.
DR   STRING; 9544.ENSMMUP00000024916; -.
DR   MEROPS; P02.001; -.
DR   PRIDE; Q2Q426; -.
DR   GeneID; 654420; -.
DR   KEGG; mcc:654420; -.
DR   CTD; 30817; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; ENOG410XSD2; LUCA.
DR   HOVERGEN; HBG048917; -.
DR   InParanoid; Q2Q426; -.
DR   KO; K08443; -.
DR   OrthoDB; 210309at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0031256; C:leading edge membrane; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
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:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0071621; P:granulocyte chemotaxis; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR003056; GPCR_2_CD97.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF07645; EGF_CA; 4.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR01278; CD97PROTEIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 4.
DR   SMART; SM00303; GPS; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 4.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   2: Evidence at transcript level;
KW   Autocatalytic cleavage; Calcium; Cell adhesion; Cell membrane;
KW   Cell projection; Complete proteome; Disulfide bond; EGF-like domain;
KW   G-protein coupled receptor; Glycoprotein; Inflammatory response;
KW   Membrane; Receptor; Reference proteome; Repeat; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    822       Adhesion G protein-coupled receptor E2.
FT                                /FTId=PRO_0000250961.
FT   TOPO_DOM     19    530       Extracellular. {ECO:0000305}.
FT   TRANSMEM    531    551       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    552    562       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    563    583       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    584    589       Extracellular. {ECO:0000305}.
FT   TRANSMEM    590    610       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    611    637       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    638    658       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    659    676       Extracellular. {ECO:0000305}.
FT   TRANSMEM    677    697       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    698    728       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    729    749       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    750    753       Extracellular. {ECO:0000305}.
FT   TRANSMEM    754    774       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    775    822       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       22     63       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       64    103       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      116    159       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      160    198       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      209    247       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      472    522       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS     49     52       Poly-Ser.
FT   COMPBIAS    537    619       Leu-rich.
FT   SITE        510    511       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:Q9UHX3}.
FT   CARBOHYD     33     33       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    108    108       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    203    203       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    222    222       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    351    351       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    427    427       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    449    449       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    453    453       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     26     36       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     30     42       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     44     62       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     68     82       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     76     91       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    120    133       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    127    142       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    144    158       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    164    177       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    171    186       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    213    226       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    220    235       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   822 AA;  90787 MW;  17129FD44C2170CB CRC64;
     MGGRVFLAFC VWLTLLGAET QDSRDCARWC PENSSCVNAT ACRCNPGFSS SSEIFTSPTE
     ICDDINECVP PSKVSCGKSS DCRNTEGSYD CVCNPGYELV SGAKTFKNES ENTCQDVDEC
     QQNPRLCKSY GTCVNTLGSF TCQCLPGFKF KPEDPKLCTD VNECTSGQNP CHSSTHCLNN
     VGSYQCRCRP GWQPIPGSPN GPNNTICEDV DECSSGLHQC DNSTVCFNTV GSYTCRCRPG
     WEPKHGIPNN QKDTVCKDMN FPTWTLPPGV HSQTLSQFFN KVQDLDRDFK TSSAKVTIQS
     ILKELDELLE APGDLETLPR FQQHCVATHL LDGLEDVLRG LSKNPSIGLL NFSYPAGTEF
     SLEVQKQVDR NVTLRQNQAT MQLHWNLAQK SGDPGPSVVG LVSVPGMGKL LAEAPLVSEP
     ENQVVRNETH QGLLPILLSD VISAFLSNND TQNLSSPVTF IFSHRSVIPR RKVLCVFWEH
     GQNGCGHWAT TGCSTMDTRD TSTICRCTHL SSFAVLMAPY DVQEEDPVLT VITYMGLSLS
     LLCLLLAALT FLLCKAIQNI STSLHLQLSL CLLLAHLLFL VAIDRTEHEV LCAIIASALH
     YLYLAAFTWM LLEALYLFLT ARNLMVVNYS SINRFTKKLM FPVAYGVPAV TVAISAASRP
     HLYGTPSRCW LQPEKGFIWG FLGPVCAIFS VNLALLLVTL WILKNRLSSL NNEVSTLQNT
     RMLAFKATAQ LFILGCTWCL GILQVGPAAR VMAYLFTIIN SLQGVFIFLV YCLLSQQVRE
     QYRKWSKGFR KLRTESEMHT LSSSAKRDTP KPSTPGLLGL QS
//
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