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Protein

Adhesion G protein-coupled receptor E2

Gene

ADGRE2

Organism
Macaca mulatta (Rhesus macaque)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Cell adhesion, Inflammatory response

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiP02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor E2
Alternative name(s):
EGF-like module receptor 2
EGF-like module-containing mucin-like hormone receptor-like 2
CD_antigen: CD312
Gene namesi
Name:ADGRE2
Synonyms:EMR2
OrganismiMacaca mulatta (Rhesus macaque)
Taxonomic identifieri9544 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000006718 Componenti: Unplaced

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein
  • Cell projectionruffle membrane By similarity; Multi-pass membrane protein By similarity

  • Note: Localized at the leading edge of migrating cells.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 530512ExtracellularCuratedAdd
BLAST
Transmembranei531 – 55121Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini552 – 56211CytoplasmicCuratedAdd
BLAST
Transmembranei563 – 58321Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini584 – 5896ExtracellularCurated
Transmembranei590 – 61021Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini611 – 63727CytoplasmicCuratedAdd
BLAST
Transmembranei638 – 65821Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini659 – 67618ExtracellularCuratedAdd
BLAST
Transmembranei677 – 69721Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini698 – 72831CytoplasmicCuratedAdd
BLAST
Transmembranei729 – 74921Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini750 – 7534ExtracellularCurated
Transmembranei754 – 77421Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini775 – 82248CytoplasmicCuratedAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 822804Adhesion G protein-coupled receptor E2PRO_0000250961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 36PROSITE-ProRule annotation
Disulfide bondi30 ↔ 42PROSITE-ProRule annotation
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence analysis
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi44 ↔ 62PROSITE-ProRule annotation
Disulfide bondi68 ↔ 82PROSITE-ProRule annotation
Disulfide bondi76 ↔ 91PROSITE-ProRule annotation
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Disulfide bondi120 ↔ 133PROSITE-ProRule annotation
Disulfide bondi127 ↔ 142PROSITE-ProRule annotation
Disulfide bondi144 ↔ 158PROSITE-ProRule annotation
Disulfide bondi164 ↔ 177PROSITE-ProRule annotation
Disulfide bondi171 ↔ 186PROSITE-ProRule annotation
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi213 ↔ 226PROSITE-ProRule annotation
Disulfide bondi220 ↔ 235PROSITE-ProRule annotation
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence analysis
Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence analysis
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence analysis
Glycosylationi453 – 4531N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei510 – 5112Cleavage; by autolysisBy similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts with chondroitin sulfate; the interaction with chondroitin sulfate is calcium-dependent. Interacts with CD55 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000024916.

Structurei

3D structure databases

ProteinModelPortaliQ2Q426.
SMRiQ2Q426. Positions 26-149.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 6342EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini64 – 10340EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini116 – 15944EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini160 – 19839EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini209 – 24739EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini472 – 52251GPSPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 524Poly-Ser
Compositional biasi537 – 61983Leu-richAdd
BLAST

Domaini

The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk.By similarity
Binding to chondroitin sulfate is mediated by the fourth EGF domain.By similarity

Sequence similaritiesi

Contains 5 EGF-like domains.PROSITE-ProRule annotation
Contains 1 GPS domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
HOVERGENiHBG048917.
InParanoidiQ2Q426.
KOiK08443.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR017981. GPCR_2-like.
IPR003056. GPCR_2_CD97.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 4 hits.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSiPR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 4 hits.
SM00303. GPS. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 4 hits.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q2Q426-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGRVFLAFC VWLTLLGAET QDSRDCARWC PENSSCVNAT ACRCNPGFSS
60 70 80 90 100
SSEIFTSPTE ICDDINECVP PSKVSCGKSS DCRNTEGSYD CVCNPGYELV
110 120 130 140 150
SGAKTFKNES ENTCQDVDEC QQNPRLCKSY GTCVNTLGSF TCQCLPGFKF
160 170 180 190 200
KPEDPKLCTD VNECTSGQNP CHSSTHCLNN VGSYQCRCRP GWQPIPGSPN
210 220 230 240 250
GPNNTICEDV DECSSGLHQC DNSTVCFNTV GSYTCRCRPG WEPKHGIPNN
260 270 280 290 300
QKDTVCKDMN FPTWTLPPGV HSQTLSQFFN KVQDLDRDFK TSSAKVTIQS
310 320 330 340 350
ILKELDELLE APGDLETLPR FQQHCVATHL LDGLEDVLRG LSKNPSIGLL
360 370 380 390 400
NFSYPAGTEF SLEVQKQVDR NVTLRQNQAT MQLHWNLAQK SGDPGPSVVG
410 420 430 440 450
LVSVPGMGKL LAEAPLVSEP ENQVVRNETH QGLLPILLSD VISAFLSNND
460 470 480 490 500
TQNLSSPVTF IFSHRSVIPR RKVLCVFWEH GQNGCGHWAT TGCSTMDTRD
510 520 530 540 550
TSTICRCTHL SSFAVLMAPY DVQEEDPVLT VITYMGLSLS LLCLLLAALT
560 570 580 590 600
FLLCKAIQNI STSLHLQLSL CLLLAHLLFL VAIDRTEHEV LCAIIASALH
610 620 630 640 650
YLYLAAFTWM LLEALYLFLT ARNLMVVNYS SINRFTKKLM FPVAYGVPAV
660 670 680 690 700
TVAISAASRP HLYGTPSRCW LQPEKGFIWG FLGPVCAIFS VNLALLLVTL
710 720 730 740 750
WILKNRLSSL NNEVSTLQNT RMLAFKATAQ LFILGCTWCL GILQVGPAAR
760 770 780 790 800
VMAYLFTIIN SLQGVFIFLV YCLLSQQVRE QYRKWSKGFR KLRTESEMHT
810 820
LSSSAKRDTP KPSTPGLLGL QS
Length:822
Mass (Da):90,787
Last modified:January 24, 2006 - v1
Checksum:i17129FD44C2170CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ227271 mRNA. Translation: ABB53642.1.
RefSeqiNP_001033751.1. NM_001038662.1.
UniGeneiMmu.9556.

Genome annotation databases

GeneIDi654420.
KEGGimcc:654420.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ227271 mRNA. Translation: ABB53642.1.
RefSeqiNP_001033751.1. NM_001038662.1.
UniGeneiMmu.9556.

3D structure databases

ProteinModelPortaliQ2Q426.
SMRiQ2Q426. Positions 26-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9544.ENSMMUP00000024916.

Protein family/group databases

MEROPSiP02.001.
GPCRDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi654420.
KEGGimcc:654420.

Organism-specific databases

CTDi30817.

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
HOVERGENiHBG048917.
InParanoidiQ2Q426.
KOiK08443.

Family and domain databases

InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR017981. GPCR_2-like.
IPR003056. GPCR_2_CD97.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR009030. Growth_fac_rcpt_.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 4 hits.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSiPR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 4 hits.
SM00303. GPS. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 4 hits.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGRE2_MACMU
AccessioniPrimary (citable) accession number: Q2Q426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 24, 2006
Last modified: June 8, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.