MO2R1_MOUSE
ID MO2R1_MOUSE Reviewed; 326 AA.
AC Q9ES57;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cell surface glycoprotein CD200 receptor 1;
DE AltName: Full=CD200 cell surface glycoprotein receptor;
DE AltName: Full=Cell surface glycoprotein OX2 receptor 1;
DE Flags: Precursor;
GN Name=Cd200r1; Synonyms=Mox2r, Ox2r;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=10981966; DOI=10.1016/s1074-7613(00)00023-6;
RA Wright G.J., Puklavec M.J., Willis A.C., Hoek R.M., Sedgwick J.D.,
RA Brown M.H., Barclay A.N.;
RT "Lymphoid/neuronal cell surface OX2 glycoprotein recognizes a novel
RT receptor on macrophages implicated in the control of their function.";
RL Immunity 13:233-242(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hematopoietic;
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 [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12960329; DOI=10.4049/jimmunol.171.6.3034;
RA Wright G.J., Cherwinski H., Foster-Cuevas M., Brooke G., Puklavec M.J.,
RA Bigler M., Song Y., Jenmalm M., Gorman D., McClanahan T., Liu M.-R.,
RA Brown M.H., Sedgwick J.D., Phillips J.H., Barclay A.N.;
RT "Characterization of the CD200 receptor family in mice and humans and their
RT interactions with CD200.";
RL J. Immunol. 171:3034-3046(2003).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15274657; DOI=10.1111/j.1600-0897.2004.00192.x;
RA Gorczynski R.M., Chen Z., Clark D.A., Kai Y., Lee L., Nachman J., Wong S.,
RA Marsden P.;
RT "Structural and functional heterogeneity in the CD200R family of
RT immunoregulatory molecules and their expression at the feto-maternal
RT interface.";
RL Am. J. Reprod. Immunol. 52:147-163(2004).
RN [5]
RP TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=15471863; DOI=10.1074/jbc.m406997200;
RA Voehringer D., Rosen D.B., Lanier L.L., Locksley R.M.;
RT "CD200 receptor family members represent novel DAP12-associated activating
RT receptors on basophils and mast cells.";
RL J. Biol. Chem. 279:54117-54123(2004).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15187158; DOI=10.4049/jimmunol.172.12.7744;
RA Gorczynski R., Chen Z., Kai Y., Lee L., Wong S., Marsden P.A.;
RT "CD200 is a ligand for all members of the CD200R family of immunoregulatory
RT molecules.";
RL J. Immunol. 172:7744-7749(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP REVIEW.
RX PubMed=24388216; DOI=10.1016/b978-0-12-800100-4.00005-2;
RA Vaine C.A., Soberman R.J.;
RT "The CD200-CD200R1 inhibitory signaling pathway: immune regulation and
RT host-pathogen interactions.";
RL Adv. Immunol. 121:191-211(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 26-232 IN COMPLEX WITH CD200,
RP SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44; ASN-93 AND ASN-192, AND
RP MUTAGENESIS OF PHE-138.
RX PubMed=23602662; DOI=10.1016/j.str.2013.03.008;
RA Hatherley D., Lea S.M., Johnson S., Barclay A.N.;
RT "Structures of CD200/CD200 receptor family and implications for topology,
RT regulation, and evolution.";
RL Structure 21:820-832(2013).
CC -!- FUNCTION: Inhibitory receptor for the CD200/OX2 cell surface
CC glycoprotein. Limits inflammation by inhibiting the expression of pro-
CC inflammatory molecules including TNF-alpha, interferons, and inducible
CC nitric oxide synthase (iNOS) in response to selected stimuli.
CC {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158}.
CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC like domains. {ECO:0000269|PubMed:23602662}.
CC -!- INTERACTION:
CC Q9ES57; O54901: Cd200; NbExp=3; IntAct=EBI-16045630, EBI-8328786;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed in granulocytes, monocytes, most T-cells
CC and a subset of NK, NKT and B-cells (at protein level). Expressed in
CC the spleen, lung, liver, testis, bone marrow, lymph nodes, spinal cord,
CC kidney, uterus and small intestine. Expressed in mast and dendritic
CC cells. Expressed in the lung of N. brasiliensis-infected mice.
CC {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158,
CC ECO:0000269|PubMed:15274657, ECO:0000269|PubMed:15471863}.
CC -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
CC -!- CAUTION: May be expressed in adult splenic cells (PubMed:15187158), as
CC the antibody used could not discriminate between CD200R1 and CD200R4.
CC May be expressed in uterus at 12.5 dpc (at protein level)
CC (PubMed:15274657), as the antibody used could not discriminate between
CC CD200R1 and CD200R4. {ECO:0000305|PubMed:15187158,
CC ECO:0000305|PubMed:15274657}.
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DR EMBL; AF231393; AAF98556.1; -; Genomic_DNA.
DR EMBL; BC052682; AAH52682.1; -; mRNA.
DR CCDS; CCDS28189.1; -.
DR RefSeq; NP_067300.1; NM_021325.3.
DR PDB; 4BFG; X-ray; 2.08 A; A=26-228.
DR PDB; 4BFI; X-ray; 3.22 A; A=26-228.
DR PDBsum; 4BFG; -.
DR PDBsum; 4BFI; -.
DR AlphaFoldDB; Q9ES57; -.
DR SMR; Q9ES57; -.
DR BioGRID; 208327; 1.
DR DIP; DIP-60159N; -.
DR IntAct; Q9ES57; 1.
DR STRING; 10090.ENSMUSP00000053822; -.
DR GlyGen; Q9ES57; 11 sites.
DR iPTMnet; Q9ES57; -.
DR PhosphoSitePlus; Q9ES57; -.
DR EPD; Q9ES57; -.
DR MaxQB; Q9ES57; -.
DR PaxDb; Q9ES57; -.
DR PeptideAtlas; Q9ES57; -.
DR PRIDE; Q9ES57; -.
DR ProteomicsDB; 252583; -.
DR DNASU; 57781; -.
DR Ensembl; ENSMUST00000057488; ENSMUSP00000053822; ENSMUSG00000022667.
DR GeneID; 57781; -.
DR KEGG; mmu:57781; -.
DR UCSC; uc007zhr.2; mouse.
DR CTD; 131450; -.
DR MGI; MGI:1889024; Cd200r1.
DR VEuPathDB; HostDB:ENSMUSG00000022667; -.
DR eggNOG; ENOG502S9IV; Eukaryota.
DR GeneTree; ENSGT00390000014496; -.
DR HOGENOM; CLU_069156_0_0_1; -.
DR InParanoid; Q9ES57; -.
DR OMA; PYTTYVQ; -.
DR OrthoDB; 993609at2759; -.
DR PhylomeDB; Q9ES57; -.
DR TreeFam; TF335960; -.
DR BioGRID-ORCS; 57781; 1 hit in 70 CRISPR screens.
DR PRO; PR:Q9ES57; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9ES57; protein.
DR Bgee; ENSMUSG00000022667; Expressed in granulocyte and 76 other tissues.
DR ExpressionAtlas; Q9ES57; baseline and differential.
DR Genevisible; Q9ES57; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:1905522; P:negative regulation of macrophage migration; ISO:MGI.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:2000405; P:negative regulation of T cell migration; ISO:MGI.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR040012; CD200R.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR21462; PTHR21462; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..326
FT /note="Cell surface glycoprotein CD200 receptor 1"
FT /id="PRO_0000015129"
FT TOPO_DOM 26..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 51..136
FT /note="Ig-like V-type"
FT DOMAIN 138..229
FT /note="Ig-like C2-type"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23602662"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23602662"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23602662"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT DISULFID 82..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT DISULFID 164..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT DISULFID 183..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT MUTAGEN 138
FT /note="F->L: 7-fold reduction in binding to CD200."
FT /evidence="ECO:0000269|PubMed:23602662"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:4BFG"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4BFG"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4BFG"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:4BFG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:4BFG"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4BFG"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4BFG"
SQ SEQUENCE 326 AA; 35505 MW; 025B3959602F82A3 CRC64;
MFCFWRTSAL AVLLIWGVFV AGSSCTDKNQ TTQNNSSSPL TQVNTTVSVQ IGTKALLCCF
SIPLTKAVLI TWIIKLRGLP SCTIAYKVDT KTNETSCLGR NITWASTPDH SPELQISAVT
LQHEGTYTCE TVTPEGNFEK NYDLQVLVPP EVTYFPEKNR SAVCEAMAGK PAAQISWSPD
GDCVTTSESH SNGTVTVRST CHWEQNNVSD VSCIVSHLTG NQSLSIELSR GGNQSLRPYI
PYIIPSIIIL IIIGCICLLK ISGFRKCKLP KLEATSAIEE DEMQPYASYT EKSNPLYDTV
TKVEAFPVSQ GEVNGTDCLT LSAIGI
