AGRE2_MACMU
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 25-MAY-2022, entry version 92.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC 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., Heidt P.J.,
RA 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 sulfate
CC moiety of glycosaminoglycan chains and promotes cell attachment.
CC Promotes granulocyte chemotaxis, degranulation and adhesion. In
CC macrophages, promotes the release of inflammatory cytokines, including
CC IL8 and TNF. Signals probably through G-proteins.
CC {ECO:0000250|UniProtKB:Q9UHX3}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region non-covalently linked to a seven-transmembrane moiety. Interacts
CC with chondroitin sulfate; the interaction with chondroitin sulfate is
CC calcium-dependent. Interacts with CD55 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHX3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UHX3};
CC Multi-pass membrane protein. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9UHX3}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Localized at the leading edge of migrating cells.
CC {ECO:0000250|UniProtKB:Q9UHX3}.
CC -!- DOMAIN: The GPS domain is necessary, but not sufficient for receptor
CC cleavage, which require the entire extracellular stalk.
CC {ECO:0000250|UniProtKB:Q9UHX3}.
CC -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF
CC 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. {ECO:0000305}.
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DR EMBL; DQ227271; ABB53642.1; -; mRNA.
DR RefSeq; NP_001033751.1; NM_001038662.1.
DR AlphaFoldDB; Q2Q426; -.
DR STRING; 9544.ENSMMUP00000024916; -.
DR MEROPS; P02.001; -.
DR GeneID; 654420; -.
DR KEGG; mcc:654420; -.
DR CTD; 30817; -.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; Q2Q426; -.
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 Gene3D; 2.60.220.50; -; 1.
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; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003056; GPCR_2_ADGRE2_ADGRE5.
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; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Inflammatory response; Membrane;
KW Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..822
FT /note="Adhesion G protein-coupled receptor E2"
FT /id="PRO_0000250961"
FT TOPO_DOM 19..530
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 531..551
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 563..583
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..589
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 590..610
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 638..658
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..676
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 677..697
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 729..749
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 750..753
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 754..774
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 775..822
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 22..63
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 64..103
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 116..159
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 160..198
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 209..247
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 472..522
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 797..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 510..511
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX3"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 30..42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 44..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 68..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 76..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 120..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 127..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 144..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 164..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 171..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 213..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 220..235
FT /evidence="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
