ID AGRE1_RAT Reviewed; 932 AA.
AC Q5Y4N8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE RecName: Full=Adhesion G protein-coupled receptor E2;
DE AltName: Full=EGF-like module receptor 1;
DE AltName: Full=EGF-like module-containing mucin-like hormone receptor-like 1;
DE AltName: Full=EMR1 hormone receptor;
DE Flags: Precursor;
GN Name=Adgre1; Synonyms=Emr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway;
RX PubMed=15578266; DOI=10.1007/s00251-004-0729-3;
RA Hamann J.;
RT "The EGF-TM7 family of the rat.";
RL Immunogenetics 56:679-681(2004).
CC -!- FUNCTION: Orphan receptor involved in cell adhesion and probably in
CC cell-cell interactions involved specifically cells of the immune
CC system. May play a role in regulatory T-cells (Treg) development.
CC {ECO:0000250|UniProtKB:Q61549}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14246};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Most adhesion GPCRs proteins undergo autoproteolysis at
CC the GPS domain. ADGRE1 is predicted non-cleavable because of the lack
CC of a consensus catalytic triad sequence within GPS domain.
CC {ECO:0000250|UniProtKB:Q14246}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC Adhesion G-protein coupled receptor (ADGR) subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY686632; AAU95564.1; -; mRNA.
DR RefSeq; NP_001007558.1; NM_001007557.1.
DR AlphaFoldDB; Q5Y4N8; -.
DR SMR; Q5Y4N8; -.
DR STRING; 10116.ENSRNOP00000067220; -.
DR GlyCosmos; Q5Y4N8; 14 sites, No reported glycans.
DR GlyGen; Q5Y4N8; 14 sites.
DR iPTMnet; Q5Y4N8; -.
DR PhosphoSitePlus; Q5Y4N8; -.
DR PaxDb; 10116-ENSRNOP00000067220; -.
DR Ensembl; ENSRNOT00000073926.3; ENSRNOP00000067220.1; ENSRNOG00000046254.3.
DR GeneID; 316137; -.
DR KEGG; rno:316137; -.
DR AGR; RGD:1359214; -.
DR CTD; 2015; -.
DR RGD; 1359214; Adgre1.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161354; -.
DR HOGENOM; CLU_002753_3_7_1; -.
DR InParanoid; Q5Y4N8; -.
DR OrthoDB; 1114672at2759; -.
DR PhylomeDB; Q5Y4N8; -.
DR Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
DR PRO; PR:Q5Y4N8; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000046254; Expressed in spleen and 19 other cell types or tissues.
DR Genevisible; Q5Y4N8; RN.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR CDD; cd15439; 7tmB2_EMR; 1.
DR CDD; cd00054; EGF_CA; 7.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 7.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 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; IPR032471; GAIN_dom_N.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR001740; GPCR_2_EMR1-like_rcpt.
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 PANTHER; PTHR12011:SF449; ADHESION G PROTEIN-COUPLED RECEPTOR E1; 1.
DR PANTHER; PTHR12011; ADHESION G-PROTEIN COUPLED RECEPTOR; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 7.
DR Pfam; PF16489; GAIN; 1.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01128; EMR1HORMONER.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00303; GPS; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS01187; EGF_CA; 5.
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 Adaptive immunity; Calcium; Cell membrane; Disulfide bond; EGF-like domain;
KW G-protein coupled receptor; Glycoprotein; Immunity; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..932
FT /note="Adhesion G protein-coupled receptor E2"
FT /id="PRO_0000250959"
FT TOPO_DOM 16..652
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 653..673
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..681
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 682..702
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..719
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 720..740
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 757..777
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 778..795
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 796..816
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 817..849
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 850..870
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 871..872
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 873..893
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 894..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..69
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 81..119
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 133..172
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 173..210
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 222..260
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 272..307
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 319..354
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 593..642
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT MOTIF 507..509
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 42..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 85..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 92..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 137..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 143..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 160..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 177..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 226..239
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 233..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 276..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 280..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 323..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 330..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 932 AA; 102308 MW; 99C4B11C721EF8DA CRC64;
MWGFWLLLFW GFSGTHRWGM TTLAILGQRL NGVNECQDTT TCPAYATCTD TTESYYCTCK
QGFLPSNGQT NFQGPGVECQ DVNECLRSDS PCGSNSVCTN IPGRARCSCL SGFSSSAGGS
WILGSPGHFL CTDVDECLTI GICPKNSNCS NSVGSYSCTC QSGFVSNGST CEDEDECVTR
NACPEHATCH NTLGSYYCTC NEGLEFSGGG PMFQGLEESC EDVDECSRNS TLCGPSFICI
NTLGSYSCSC PAGFSLSTFQ IPGHPADGNC TDIDECDDIC PSNSSCTNTL GSYFCTCHPG
FASSNGQLNF TDQEVTCEDI DECTQDPFRC GRNSSCTNVP GSYNCSCLPD FRMDPGGSQA
HGNFTCKRIP FKCKEDLIPK SEQIEQCQAG QGRNLDYTSF CTFVNATFTI LDNTCENKSA
PVSLQSAATS VSLMLEQAST WFEFSREETS TLGTILLETV ESTMLAALLT PSGNASQTIR
TEYLEIESKV INEECNEENV SINLKARGDK MDVGCFIIKE SESTGTPGVA FVSFAHMDSV
LDERFFEDGQ ASWKLRMNSH VVGGTVTGER KEDFSKPIVY TLQHIQPKQK SERSICVSWN
TDVEDGRWTP SGCETVEASE THTVCSCNRM TNLAIIMASG ELTMEFSLYI ISYVGTVISL
VCLALAIATF LLFRAVQNHN TYLHLHLCVC LFLAKILFLT GIDKTDNQTA CAIIAGFLHY
LFLACFFWML VEAVMLFLMV RNLKVVNYFS SRNIKMLHLC AFGYGLPVVV VIISATVHPW
GYGMHNRCWL NTETGFIWSF LGPVCMIITI NSALLAWTLW VLRQKLCSVN SEVSKLKDTR
LLTFKAIAQI FILGCSWVLG IFQIGPLASI MAYLFTTINS LQGAFIFLIH CLLNRQVRDE
YRKLLTRKTD LSSHSQTSGI LLSSMPSTSK TG
//
