MO2R4_MOUSE
ID MO2R4_MOUSE Reviewed; 270 AA.
AC Q6XJV4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cell surface glycoprotein CD200 receptor 4;
DE AltName: Full=CD200 cell surface glycoprotein receptor-like 4;
DE Short=CD200 receptor-like 4;
DE AltName: Full=CD200 cell surface glycoprotein receptor-like a;
DE Short=CD200RLa;
DE AltName: Full=Cell surface glycoprotein OX2 receptor 4;
DE Flags: Precursor;
GN Name=Cd200r4;
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], FUNCTION, SUBUNIT, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 FUNCTION.
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 [5]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
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 [6]
RP FUNCTION.
RX PubMed=16081818; DOI=10.4049/jimmunol.175.4.2469;
RA Hatherley D., Cherwinski H.M., Moshref M., Barclay A.N.;
RT "Recombinant CD200 protein does not bind activating proteins closely
RT related to CD200 receptor.";
RL J. Immunol. 175:2469-2474(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-238, DISULFIDE BONDS, AND
RP MUTAGENESIS OF ASN-87; LYS-90 AND LEU-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: Involved in the recruitment or surface expression of the
CC TYROBP receptor. {ECO:0000269|PubMed:12960329,
CC ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15471863,
CC ECO:0000269|PubMed:16081818}.
CC -!- SUBUNIT: Interacts with TYROBP. {ECO:0000269|PubMed:12960329}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in monocytes, NK cells and a
CC subset of NKT cells. Weakly expressed in granulocytes and B-cells (at
CC protein level). Expressed in brain, lung, testis, thymus, intestine and
CC uterus. Expressed in bone marrow derived-macrophage and dendritic cells
CC and mast cells. {ECO:0000269|PubMed:12960329,
CC ECO:0000269|PubMed:15187158, ECO:0000269|PubMed:15274657}.
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}.
CC -!- CAUTION: According to some authors (PubMed:15187158), CD200R4 is a
CC receptor for the CD200/OX2 cell surface glycoprotein, but it was later
CC found (PubMed:23602662) to miss key amino-acids for binding to CD200.
CC {ECO:0000305|PubMed:15187158, ECO:0000305|PubMed:23602662}.
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DR EMBL; AY230200; AAO84054.1; -; mRNA.
DR EMBL; BC131946; AAI31947.1; -; mRNA.
DR EMBL; BC131972; AAI31973.1; -; mRNA.
DR CCDS; CCDS37346.1; -.
DR RefSeq; NP_997127.1; NM_207244.2.
DR RefSeq; XP_006522191.1; XM_006522128.2.
DR RefSeq; XP_006522192.1; XM_006522129.2.
DR RefSeq; XP_006522193.1; XM_006522130.2.
DR PDB; 4BFE; X-ray; 2.50 A; A/B/C=26-238.
DR PDBsum; 4BFE; -.
DR AlphaFoldDB; Q6XJV4; -.
DR SMR; Q6XJV4; -.
DR DIP; DIP-60158N; -.
DR IntAct; Q6XJV4; 1.
DR STRING; 10090.ENSMUSP00000135299; -.
DR GlyGen; Q6XJV4; 3 sites.
DR PaxDb; Q6XJV4; -.
DR PRIDE; Q6XJV4; -.
DR ProteomicsDB; 295573; -.
DR DNASU; 239849; -.
DR Ensembl; ENSMUST00000114626; ENSMUSP00000110273; ENSMUSG00000062082.
DR Ensembl; ENSMUST00000176819; ENSMUSP00000135299; ENSMUSG00000062082.
DR GeneID; 239849; -.
DR KEGG; mmu:239849; -.
DR UCSC; uc007zht.1; mouse.
DR CTD; 239849; -.
DR MGI; MGI:3036289; Cd200r4.
DR VEuPathDB; HostDB:ENSMUSG00000062082; -.
DR eggNOG; ENOG502S9IV; Eukaryota.
DR GeneTree; ENSGT00390000014496; -.
DR InParanoid; Q6XJV4; -.
DR OMA; WKIRPRT; -.
DR OrthoDB; 993609at2759; -.
DR PhylomeDB; Q6XJV4; -.
DR TreeFam; TF335960; -.
DR BioGRID-ORCS; 239849; 0 hits in 40 CRISPR screens.
DR ChiTaRS; Cd200r4; mouse.
DR PRO; PR:Q6XJV4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6XJV4; protein.
DR Bgee; ENSMUSG00000062082; Expressed in vault of skull and 32 other tissues.
DR ExpressionAtlas; Q6XJV4; baseline and differential.
DR Genevisible; Q6XJV4; 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:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; IEA:InterPro.
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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..270
FT /note="Cell surface glycoprotein CD200 receptor 4"
FT /id="PRO_0000346454"
FT TOPO_DOM 26..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..145
FT /note="Ig-like V-type"
FT DOMAIN 134..229
FT /note="Ig-like C2-type"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
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 87
FT /note="N->K: Acquires binding to CD200; when associated
FT with T-90 and F-138."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 90
FT /note="K->T: Acquires binding to CD200; when associated
FT with K-87 and F-138."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 138
FT /note="L->F: Acquires binding to CD200; when associated
FT with K-87 and T-90."
FT /evidence="ECO:0000269|PubMed:23602662"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:4BFE"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:4BFE"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4BFE"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 158..171
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:4BFE"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4BFE"
SQ SEQUENCE 270 AA; 29625 MW; EEB05080B95AF6E2 CRC64;
MHALGRIPTL TLLIFINIFV SGSSCTDENQ TIQNDSSSSL TQVNTTMSVQ MDKKALLCCF
SSPLINAVLI TWIIKHRHLP SCTIAYNLDK KTNETSCLGR NITWASTPDH SPELQISAVA
LQHEGTYTCE IVTPEGNLEK VYDLQVLVPP EVTYFPGKNR TAVCEAMAGK PAAQISWTPD
GDCVTKSESH SNGTVTVRST CHWEQNNVSV VSCLVSHSTG NQSLSIELSQ GTMTTPRSLL
TILYVKMALL VIILLNVGFA FFQKRNFART
