AGRE1_MOUSE
ID AGRE1_MOUSE Reviewed; 931 AA.
AC Q61549;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Adhesion G protein-coupled receptor E1;
DE AltName: Full=Cell surface glycoprotein F4/80;
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, Gpf480;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Peritoneal cavity;
RX PubMed=8550607; DOI=10.1074/jbc.271.1.486;
RA McKnight A.J., Macfarlane A.J., Dri P., Turley L., Willis A.C., Gordon S.;
RT "Molecular cloning of F4/80, a murine macrophage-restricted cell surface
RT glycoprotein with homology to the G-protein-linked transmembrane 7 hormone
RT receptor family.";
RL J. Biol. Chem. 271:486-489(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9169125; DOI=10.1006/geno.1997.4674;
RA Lin H.H., Stubbs L.J., Mucenski M.L.;
RT "Identification and characterization of a seven transmembrane hormone
RT receptor using differential display.";
RL Genomics 41:301-308(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15883173; DOI=10.1084/jem.20042307;
RA Lin H.H., Faunce D.E., Stacey M., Terajewicz A., Nakamura T.,
RA Zhang-Hoover J., Kerley M., Mucenski M.L., Gordon S., Stein-Streilein J.;
RT "The macrophage F4/80 receptor is required for the induction of antigen-
RT specific efferent regulatory T cells in peripheral tolerance.";
RL J. Exp. Med. 201:1615-1625(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Orphan receptor involved in cell adhesion and probably in
CC cell-cell interactions specifically involving cells of the immune
CC system. May play a role in regulatory T-cells (Treg) development.
CC {ECO:0000269|PubMed:15883173}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14246};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In macrophages; but absent from those which are
CC localized within T-cell areas of lymph nodes and spleen. Low level of
CC expression on blood monocytes.
CC -!- DISRUPTION PHENOTYPE: Deficient mice fail to develop peripheral
CC tolerance after inoculation with antigen because of a lack of efferent
CC regulatory T-cell development. {ECO:0000269|PubMed:15883173}.
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}.
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DR EMBL; X93328; CAA63720.1; -; mRNA.
DR EMBL; U66888; AAC53184.1; -; mRNA.
DR EMBL; BC075688; AAH75688.1; -; mRNA.
DR CCDS; CCDS50160.1; -.
DR RefSeq; NP_034260.1; NM_010130.4.
DR RefSeq; XP_006523664.1; XM_006523601.1.
DR AlphaFoldDB; Q61549; -.
DR BioGRID; 199441; 1.
DR IntAct; Q61549; 1.
DR MINT; Q61549; -.
DR STRING; 10090.ENSMUSP00000083971; -.
DR MEROPS; P02.951; -.
DR GlyGen; Q61549; 10 sites.
DR iPTMnet; Q61549; -.
DR PhosphoSitePlus; Q61549; -.
DR MaxQB; Q61549; -.
DR PaxDb; Q61549; -.
DR PRIDE; Q61549; -.
DR ProteomicsDB; 296129; -.
DR Antibodypedia; 11973; 715 antibodies from 41 providers.
DR DNASU; 13733; -.
DR Ensembl; ENSMUST00000004850; ENSMUSP00000004850; ENSMUSG00000004730.
DR Ensembl; ENSMUST00000086763; ENSMUSP00000083971; ENSMUSG00000004730.
DR GeneID; 13733; -.
DR KEGG; mmu:13733; -.
DR UCSC; uc008det.2; mouse.
DR CTD; 2015; -.
DR MGI; MGI:106912; Adgre1.
DR VEuPathDB; HostDB:ENSMUSG00000004730; -.
DR eggNOG; KOG4193; Eukaryota.
DR GeneTree; ENSGT00940000161354; -.
DR HOGENOM; CLU_002753_3_7_1; -.
DR InParanoid; Q61549; -.
DR OMA; PGRFICT; -.
DR OrthoDB; 124090at2759; -.
DR PhylomeDB; Q61549; -.
DR TreeFam; TF316380; -.
DR Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR BioGRID-ORCS; 13733; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Adgre1; mouse.
DR PRO; PR:Q61549; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q61549; protein.
DR Bgee; ENSMUSG00000004730; Expressed in stroma of bone marrow and 224 other tissues.
DR ExpressionAtlas; Q61549; baseline and differential.
DR Genevisible; Q61549; MM.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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 Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR026823; cEGF.
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; 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 Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 5.
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; SSF57184; SSF57184; 2.
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 1: Evidence at protein 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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..931
FT /note="Adhesion G protein-coupled receptor E1"
FT /id="PRO_0000012874"
FT TOPO_DOM 28..644
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 645..672
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..679
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 680..701
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 702..711
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 712..735
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 755..776
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..792
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 793..821
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 840..859
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 860..874
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 875..897
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 898..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..80
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 81..132
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..221
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 222..271
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 272..318
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 319..367
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 592..641
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT MOTIF 506..508
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 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 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
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 59..79
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 109..131
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 200..220
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 250..270
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 297..317
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"
FT DISULFID 347..366
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 931 AA; 102130 MW; 52963A667E8B76B5 CRC64;
MWGFWLLLFW GFSGMYRWGM TTLPTLGQTL GGVNECQDTT TCPAYATCTD TTDSYYCTCK
RGFLSSNGQT NFQGPGVECQ DVNECLQSDS PCGPNSVCTN ILGRAKCSCL RGFSSSTGKD
WILGSLDNFL CADVDECLTI GICPKYSNCS NSVGSYSCTC QPGFVLNGSI CEDEDECVTR
DVCPEHATCH NTLGSYYCTC NSGLESSGGG PMFQGLDESC EDVDECSRNS TLCGPTFICI
NTLGSYSCSC PAGFSLPTFQ ILGHPADGNC TDIDECDDTC PLNSSCTNTI GSYFCTCHPG
FASSNGQLNF KDLEVTCEDI DECTQDPLQC GLNSVCTNVP GSYICGCLPD FQMDPEGSQG
YGNFNCKRIL FKCKEDLILQ SEQIQQCQAV QGRDLGYASF CTLVNATFTI LDNTCENKSA
PVSLQSAATS VSLVLEQATT WFELSKEETS TLGTILLETV ESTMLAALLI PSGNASQMIQ
TEYLDIESKV INEECKENES INLAARGDKM NVGCFIIKES VSTGAPGVAF VSFAHMESVL
NERFFEDGQS FRKLRMNSRV VGGTVTGEKK EDFSKPIIYT LQHIQPKQKS ERPICVSWNT
DVEDGRWTPS GCEIVEASET HTVCSCNRMA NLAIIMASGE LTMEFSLYII SHVGTVISLV
CLALAIATFL LCRAVQNHNT YMHLHLCVCL FLAKILFLTG IDKTDNQTAC AIIAGFLHYL
FLACFFWMLV EAVMLFLMVR NLKVVNYFSS RNIKMLHLCA FGYGLPVLVV IISASVQPRG
YGMHNRCWLN TETGFIWSFL GPVCMIITIN SVLLAWTLWV LRQKLCSVSS EVSKLKDTRL
LTFKAIAQIF ILGCSWVLGI FQIGPLASIM AYLFTIINSL QGAFIFLIHC LLNRQVRDEY
KKLLTRKTDL SSHSQTSGIL LSSMPSTSKM G
