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Database: UniProt
Entry: Q2Q421
LinkDB: Q2Q421
Original site: Q2Q421 
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   10-APR-2019, 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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
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.
CC       {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:0000255}. Note=Localized at the leading
CC       edge of migrating cells. {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB53647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DQ227276; ABB53647.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001033756.1; NM_001038667.1.
DR   UniGene; Cfa.24646; -.
DR   ProteinModelPortal; Q2Q421; -.
DR   STRING; 9612.ENSCAFP00000024120; -.
DR   MEROPS; P02.001; -.
DR   PaxDb; Q2Q421; -.
DR   PRIDE; Q2Q421; -.
DR   GeneID; 610750; -.
DR   KEGG; cfa:610750; -.
DR   CTD; 30817; -.
DR   eggNOG; KOG4193; Eukaryota.
DR   eggNOG; ENOG410XSD2; LUCA.
DR   HOGENOM; HOG000294115; -.
DR   HOVERGEN; HBG048917; -.
DR   InParanoid; Q2Q421; -.
DR   KO; K08443; -.
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   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   Glycoprotein; Inflammatory response; Membrane; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    830       Adhesion G protein-coupled receptor E2.
FT                                /FTId=PRO_0000250960.
FT   TOPO_DOM     23    540       Extracellular. {ECO:0000305}.
FT   TRANSMEM    541    561       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    562    576       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    577    597       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    598    603       Extracellular. {ECO:0000305}.
FT   TRANSMEM    604    624       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    625    651       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    652    672       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    673    690       Extracellular. {ECO:0000305}.
FT   TRANSMEM    691    711       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    712    744       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    745    765       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    766    767       Extracellular. {ECO:0000305}.
FT   TRANSMEM    768    788       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    789    830       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       26     68       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN       69    108       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      121    159       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      165    203       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      214    253       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      486    536       GPS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00098}.
FT   COMPBIAS    551    633       Leu-rich.
FT   SITE        524    525       Cleavage; by autolysis.
FT                                {ECO:0000250|UniProtKB:Q9UHX3}.
FT   CARBOHYD     42     42       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    113    113       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    178    178       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    258    258       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    348    348       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    379    379       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     30     40       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     34     46       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     48     67       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     73     87       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID     81     96       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    125    138       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    132    147       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    169    182       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    176    191       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    218    231       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    225    240       {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
//
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