MO2R3_MOUSE
ID MO2R3_MOUSE Reviewed; 296 AA.
AC Q5UKY4; Q3V3F9; Q5UKY1; Q5UKY2; Q5UKY3; Q5UKY5; Q6XJV5; Q9D628; Q9D642;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cell surface glycoprotein CD200 receptor 3;
DE AltName: Full=CD200 cell surface glycoprotein receptor-like 3;
DE Short=CD200 receptor-like 3;
DE AltName: Full=CD200 cell surface glycoprotein receptor-like b;
DE Short=CD200RLb;
DE AltName: Full=Cell surface glycoprotein OX2 receptor 3;
DE Flags: Precursor;
GN Name=Cd200r3; Synonyms=Cd200rlb;
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] (ISOFORMS 1; 2; 3; 6; 7 AND 8), FUNCTION,
RP INTERACTION WITH TYROBP, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), 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] (ISOFORMS 5; 8 AND 9).
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-296 (ISOFORM 3), FUNCTION, SUBUNIT, AND
RP 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 [6]
RP IDENTIFICATION, DEVELOPMENTAL STAGE, 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 [7]
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).
CC -!- FUNCTION: According to PubMed:15187158 isoform 4 is a receptor for the
CC CD200 cell surface glycoprotein. According to PubMed:16081818 isoform 4
CC is not a receptor for the CD200/OX2 cell surface glycoprotein. Isoform
CC 1, isoform 2 and isoform 3 are involved in the recruitment or surface
CC expression of the TYROBP receptor. Isoform 6, isoform 7 and isoform 8
CC are not involved in the recruitment or surface expression of the TYROBP
CC receptor. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158,
CC ECO:0000269|PubMed:15471863, ECO:0000269|PubMed:16081818}.
CC -!- SUBUNIT: Isoform 3 interacts with TYROBP. Isoform 8 does not interact
CC with TYROBP. {ECO:0000269|PubMed:12960329,
CC ECO:0000269|PubMed:15471863}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=Cd200r3b;
CC IsoId=Q5UKY4-1; Sequence=Displayed;
CC Name=2; Synonyms=Cd200r3a;
CC IsoId=Q5UKY4-2; Sequence=VSP_035006;
CC Name=3; Synonyms=Cd200r3c;
CC IsoId=Q5UKY4-3; Sequence=VSP_035007;
CC Name=4;
CC IsoId=Q5UKY4-4; Sequence=VSP_035008;
CC Name=5;
CC IsoId=Q5UKY4-5; Sequence=VSP_035004, VSP_035005;
CC Name=6; Synonyms=Cd200r3e;
CC IsoId=Q5UKY4-6; Sequence=VSP_035003;
CC Name=7; Synonyms=Cd200r3d;
CC IsoId=Q5UKY4-7; Sequence=VSP_035003, VSP_035006;
CC Name=8; Synonyms=Cd200r3f;
CC IsoId=Q5UKY4-8; Sequence=VSP_035003, VSP_035007;
CC Name=9;
CC IsoId=Q5UKY4-9; Sequence=VSP_035003, VSP_035008;
CC -!- TISSUE SPECIFICITY: Expressed in uterus and bone marrow-derived mast
CC cells (at protein level). Expressed in uterus, spleen, bone marrow-
CC derived dendritic, basophil and mast cells. Expressed in the lung of
CC N.brasiliensis-infected mice. Weakly expressed in brain, testis, lung
CC and thymus. {ECO:0000269|PubMed:12960329, ECO:0000269|PubMed:15187158,
CC ECO:0000269|PubMed:15274657, ECO:0000269|PubMed:15471863}.
CC -!- DEVELOPMENTAL STAGE: Expressed in uterus at 12.5 dpc (at protein
CC level). {ECO:0000269|PubMed:15274657}.
CC -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
CC -!- CAUTION: According to some authors, isoform 3 (truncated at the N-
CC terminus) is not a receptor for the CD200/OX2 cell surface
CC glycoprotein. {ECO:0000305|PubMed:12960329}.
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DR EMBL; AY703837; AAV40659.1; -; mRNA.
DR EMBL; AY703838; AAV40660.1; -; mRNA.
DR EMBL; AY703839; AAV40661.1; -; mRNA.
DR EMBL; AY703840; AAV40662.1; -; mRNA.
DR EMBL; AY703841; AAV40663.1; -; mRNA.
DR EMBL; AY703842; AAV40664.1; -; mRNA.
DR EMBL; AY230199; AAO84053.1; -; mRNA.
DR EMBL; AK014637; BAB29480.1; -; mRNA.
DR EMBL; AK014671; BAB29497.1; -; mRNA.
DR EMBL; AK040868; BAC30726.1; -; mRNA.
DR EMBL; BC106838; AAI06839.1; -; mRNA.
DR CCDS; CCDS49856.1; -. [Q5UKY4-3]
DR CCDS; CCDS49857.1; -. [Q5UKY4-4]
DR CCDS; CCDS49858.1; -. [Q5UKY4-8]
DR CCDS; CCDS49859.1; -. [Q5UKY4-9]
DR RefSeq; NP_001121604.1; NM_001128132.1. [Q5UKY4-3]
DR RefSeq; NP_001121605.1; NM_001128133.1. [Q5UKY4-8]
DR RefSeq; NP_081854.1; NM_027578.1. [Q5UKY4-9]
DR RefSeq; NP_083294.2; NM_029018.4. [Q5UKY4-4]
DR RefSeq; XP_006522737.1; XM_006522674.3. [Q5UKY4-2]
DR RefSeq; XP_017172641.1; XM_017317152.1. [Q5UKY4-2]
DR RefSeq; XP_017172642.1; XM_017317153.1. [Q5UKY4-2]
DR RefSeq; XP_017172643.1; XM_017317154.1. [Q5UKY4-7]
DR AlphaFoldDB; Q5UKY4; -.
DR SMR; Q5UKY4; -.
DR STRING; 10090.ENSMUSP00000110258; -.
DR GlyGen; Q5UKY4; 2 sites.
DR iPTMnet; Q5UKY4; -.
DR PhosphoSitePlus; Q5UKY4; -.
DR PaxDb; Q5UKY4; -.
DR PRIDE; Q5UKY4; -.
DR DNASU; 74603; -.
DR Ensembl; ENSMUST00000048479; ENSMUSP00000036624; ENSMUSG00000036172. [Q5UKY4-1]
DR Ensembl; ENSMUST00000077178; ENSMUSP00000076421; ENSMUSG00000036172. [Q5UKY4-6]
DR Ensembl; ENSMUST00000114611; ENSMUSP00000110258; ENSMUSG00000036172. [Q5UKY4-3]
DR Ensembl; ENSMUST00000114612; ENSMUSP00000110259; ENSMUSG00000036172. [Q5UKY4-7]
DR Ensembl; ENSMUST00000114613; ENSMUSP00000110260; ENSMUSG00000036172. [Q5UKY4-2]
DR Ensembl; ENSMUST00000114622; ENSMUSP00000110269; ENSMUSG00000036172. [Q5UKY4-8]
DR Ensembl; ENSMUST00000164007; ENSMUSP00000130480; ENSMUSG00000036172. [Q5UKY4-4]
DR Ensembl; ENSMUST00000171779; ENSMUSP00000132938; ENSMUSG00000036172. [Q5UKY4-9]
DR GeneID; 74603; -.
DR KEGG; mmu:74603; -.
DR UCSC; uc007zhx.2; mouse. [Q5UKY4-2]
DR UCSC; uc007zhy.2; mouse. [Q5UKY4-7]
DR UCSC; uc007zhz.2; mouse. [Q5UKY4-1]
DR UCSC; uc007zia.2; mouse. [Q5UKY4-6]
DR UCSC; uc007zib.2; mouse. [Q5UKY4-3]
DR UCSC; uc007zic.2; mouse. [Q5UKY4-8]
DR UCSC; uc007zid.2; mouse. [Q5UKY4-4]
DR UCSC; uc007zie.2; mouse. [Q5UKY4-9]
DR CTD; 74603; -.
DR MGI; MGI:1921853; Cd200r3.
DR VEuPathDB; HostDB:ENSMUSG00000036172; -.
DR eggNOG; ENOG502S9IV; Eukaryota.
DR GeneTree; ENSGT00390000014496; -.
DR InParanoid; Q5UKY4; -.
DR OMA; YISKMAD; -.
DR OrthoDB; 993609at2759; -.
DR PhylomeDB; Q5UKY4; -.
DR TreeFam; TF335960; -.
DR BioGRID-ORCS; 74603; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cd200r3; mouse.
DR PRO; PR:Q5UKY4; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5UKY4; protein.
DR Bgee; ENSMUSG00000036172; Expressed in urinary bladder urothelium and 29 other tissues.
DR ExpressionAtlas; Q5UKY4; baseline and differential.
DR Genevisible; Q5UKY4; 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; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR21462; PTHR21462; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..296
FT /note="Cell surface glycoprotein CD200 receptor 3"
FT /id="PRO_0000346453"
FT TOPO_DOM 26..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 48..162
FT /note="Ig-like V-type"
FT DOMAIN 151..232
FT /note="Ig-like C2-type"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 165..237
FT /note="Missing (in isoform 6, isoform 7, isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:15471863,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_035003"
FT VAR_SEQ 218..226
FT /note="VFCFISHLT -> CVLLYLPFD (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035004"
FT VAR_SEQ 227..296
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035005"
FT VAR_SEQ 273..296
FT /note="SSRDLVFMKERRSKRSVWQREALG -> RSNEEPTTLAPT (in isoform
FT 2 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15471863"
FT /id="VSP_035006"
FT VAR_SEQ 273..296
FT /note="SSRDLVFMKERRSKRSVWQREALG -> RVPEGS (in isoform 3 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12960329,
FT ECO:0000303|PubMed:15471863, ECO:0000303|PubMed:16141072"
FT /id="VSP_035007"
FT VAR_SEQ 273..296
FT /note="SSRDLVFMKERRSKRSVWQREALG -> RWI (in isoform 4 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:15187158,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_035008"
FT CONFLICT 10
FT /note="L -> S (in Ref. 1; AAV40662/AAV40663)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Q -> K (in Ref. 3; BAC30726)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="R -> T (in Ref. 3; BAC30726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 33625 MW; A4EBB9A3FFCCC985 CRC64;
MHALGRTLAL MLLIFITILV PESSCSVKGR EEIPPDDSFP FSDDNIFPDG VGVTMEIEII
TPVSVQIGIK AQLFCHPSPS KEATLRIWEI TPRDWPSCRL PYRAELQQIS KKICTERGTT
RVPAHHQSSD LPIKSMALKH DGHYSCRIET TDGIFQERHS IQVPGENRTV VCEAIASKPA
MQILWTPDED CVTKSKSHND TMIVRSKCHR EKNNGHSVFC FISHLTDNWI LSMEQNRGTT
SILPSLLSIL YVKLAVTVLI VGFAFFQKRN YFSSRDLVFM KERRSKRSVW QREALG
