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   27-MAR-2024, entry version 189.
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   SMR; Q61549; -.
DR   BioGRID; 199441; 2.
DR   IntAct; Q61549; 1.
DR   MINT; Q61549; -.
DR   STRING; 10090.ENSMUSP00000083971; -.
DR   MEROPS; P02.951; -.
DR   GlyCosmos; Q61549; 10 sites, No reported glycans.
DR   GlyGen; Q61549; 10 sites.
DR   iPTMnet; Q61549; -.
DR   PhosphoSitePlus; Q61549; -.
DR   MaxQB; Q61549; -.
DR   PaxDb; 10090-ENSMUSP00000083971; -.
DR   ProteomicsDB; 296129; -.
DR   Antibodypedia; 11973; 892 antibodies from 42 providers.
DR   DNASU; 13733; -.
DR   Ensembl; ENSMUST00000004850.8; ENSMUSP00000004850.8; ENSMUSG00000004730.16.
DR   Ensembl; ENSMUST00000086763.13; ENSMUSP00000083971.6; ENSMUSG00000004730.16.
DR   GeneID; 13733; -.
DR   KEGG; mmu:13733; -.
DR   UCSC; uc008det.2; mouse.
DR   AGR; MGI:106912; -.
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; KCRCQVG; -.
DR   OrthoDB; 1114672at2759; -.
DR   PhylomeDB; Q61549; -.
DR   TreeFam; TF316380; -.
DR   Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR   BioGRID-ORCS; 13733; 0 hits in 76 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 225 other cell types or tissues.
DR   ExpressionAtlas; Q61549; baseline and differential.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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   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; 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; 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; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 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.
DR   Genevisible; Q61549; MM.
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
//