AGRE2_CANLF
ID AGRE2_CANLF Reviewed; 830 AA.
AC Q2Q421;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 100.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
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. {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:0000255}. Note=Localized at the leading edge of migrating cells.
CC {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB53647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ227276; ABB53647.1; ALT_INIT; mRNA.
DR RefSeq; NP_001033756.1; NM_001038667.1.
DR AlphaFoldDB; Q2Q421; -.
DR STRING; 9615.ENSCAFP00000024120; -.
DR MEROPS; P02.001; -.
DR PaxDb; Q2Q421; -.
DR GeneID; 610750; -.
DR KEGG; cfa:610750; -.
DR CTD; 30817; -.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; Q2Q421; -.
DR OrthoDB; 210309at2759; -.
DR Proteomes; UP000002254; 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; Glycoprotein;
KW Inflammatory response; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..830
FT /note="Adhesion G protein-coupled receptor E2"
FT /id="PRO_0000250960"
FT TOPO_DOM 23..540
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 541..561
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..576
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 577..597
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..603
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 604..624
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 652..672
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..690
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 691..711
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 745..765
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 766..767
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 768..788
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 26..68
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 69..108
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 121..159
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 165..203
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..253
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 486..536
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT SITE 524..525
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:Q9UHX3"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 34..46
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 48..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 73..87
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 81..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 125..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 132..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 169..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 830 AA; 91452 MW; 5CAC2906FB4C8804 CRC64;
MRHGHPRLLP GLLMLLLLPL GAAAQKTSGC ARWCPPKSTC VNATTCRCSP GFSSLSGEIF
SSPLESCDDI DECGPPPLVS CGRLADCQNT EGSYHCMCSP GYALASGATT FMNESENTCR
DVDECQLKPR VCKSRGICTN TKGSYTCKCP PGFELNLGDL NLCTDVNECT SGQNPCHNST
HCLNNIGGYE CRCRPGWKPV PGSPNGPKST VCEDVDECSS GKHTCHYSTV CINTVGSYKC
RCRRGWKPKP RFQDRQLNTT CEVPAEMSFP TWTPPPGIKS QRLSNFFERV QELHRDFKPA
LAQETIQDLI QEVDELLEIP GDLEALPHSE QHCVATNLLV GLEGVLRNVS QAMPNGPWTF
NASAGTDLSL EVQEEGYRNV TLSQNLAKMM LKWDVVHKSG DSGPSVVGLL STPGMGKLLA
EAPLVLEPEK QAVLHGAPKG LLQGVSSVLL SDVISVFMSN KVTQKLSSPV TFIFSHHSAT
HEPKLKVFCV FWEHSQDECG HWSTRGCTVV DSGDTSTTCQ CTHLSSFAVL MAHYDVQEED
LVLPVITYVG LGLSLLCLLL AALTFLLCKA IQNTSTSLHL QLLICLFLAH LLFLMAIDRT
EIKVLCSIIA GALHYLYLAS FTWMLLEGLH LFLTARNLMV VNYSSVSMLM KKLMYPVGYG
VPTLIVAISA ASRSHLYGTR TRCWLNPEER FIWSFLGPVC TIFSVNLGFF LMTLWILKSK
LSSLNSDVST LQNTRMLTFK AIAQLFILGC TWCLGILQVG PAAHVMAYLF TIINSLQGVF
IFLVYCLLSQ QVREEYGKWF KGIRKTRAES EKYTLSSRAM SDVNKPMMVN
