MO2R1_RAT
ID MO2R1_RAT Reviewed; 327 AA.
AC Q9ES58; Q6PS97;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 AltName: Full=OX102 antigen;
DE Flags: Precursor;
GN Name=Cd200r1; Synonyms=Mox2r, Ox2r;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-42,
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC STRAIN=PVG;
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 [MRNA] (ISOFORM 2).
RA Suarez A.;
RT "Ox2 receptor precursor transcript variant 1.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC like domains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ES58-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ES58-2; Sequence=VSP_034998, VSP_034999;
CC -!- TISSUE SPECIFICITY: Restricted to cells of the myeloid lineage.
CC {ECO:0000269|PubMed:10981966}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC -!- PTM: Highly N-glycosylated.
CC -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF231392; AAF98555.1; -; Genomic_DNA.
DR EMBL; AY583211; AAS90843.1; -; mRNA.
DR RefSeq; NP_076443.1; NM_023953.1. [Q9ES58-1]
DR AlphaFoldDB; Q9ES58; -.
DR SMR; Q9ES58; -.
DR BioGRID; 249042; 1.
DR STRING; 10116.ENSRNOP00000002799; -.
DR GlyGen; Q9ES58; 8 sites.
DR PaxDb; Q9ES58; -.
DR PRIDE; Q9ES58; -.
DR Ensembl; ENSRNOT00000002799; ENSRNOP00000002799; ENSRNOG00000039048. [Q9ES58-1]
DR GeneID; 64357; -.
DR KEGG; rno:64357; -.
DR UCSC; RGD:61837; rat. [Q9ES58-1]
DR CTD; 131450; -.
DR RGD; 61837; Cd200r1.
DR eggNOG; ENOG502S9IV; Eukaryota.
DR GeneTree; ENSGT00390000014496; -.
DR HOGENOM; CLU_069156_0_0_1; -.
DR InParanoid; Q9ES58; -.
DR OMA; PYTTYVQ; -.
DR OrthoDB; 993609at2759; -.
DR PhylomeDB; Q9ES58; -.
DR TreeFam; TF335960; -.
DR PRO; PR:Q9ES58; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000039048; Expressed in spleen and 17 other tissues.
DR Genevisible; Q9ES58; RN.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IPI:ARUK-UCL.
DR GO; GO:0038023; F:signaling receptor activity; ISO:RGD.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:ARUK-UCL.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IGI:ARUK-UCL.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IGI:ARUK-UCL.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; IGI:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ARUK-UCL.
DR GO; GO:2000405; P:negative regulation of T cell migration; IGI:ARUK-UCL.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; IGI:ARUK-UCL.
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; IPR013106; Ig_V-set.
DR PANTHER; PTHR21462; PTHR21462; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10981966"
FT CHAIN 24..327
FT /note="Cell surface glycoprotein CD200 receptor 1"
FT /id="PRO_0000015130"
FT TOPO_DOM 24..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..145
FT /note="Ig-like V-type"
FT DOMAIN 147..226
FT /note="Ig-like C2-type"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
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 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 81..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 164..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 183..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 148..149
FT /note="VP -> GK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034998"
FT VAR_SEQ 150..327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_034999"
SQ SEQUENCE 327 AA; 35534 MW; BA06E7FFC778610C CRC64;
MLCFWRTSHV AVLLIWGVFA AESSCPDKNQ TMQNNSSTMT EVNTTVFVQM GKKALLCCPS
ISLTKVILIT WTITLRGQPS CIISYKADTR ETHESNCSDR SITWASTPDL APDLQISAVA
LQHEGRYSCD IAVPDGNFQN IYDLQVLVPP EVTHFPGENR TAVCEAIAGK PAAQISWTPD
GDCVAKNESH SNGTVTVRST CHWEQSHVSV VFCVVSHLTT GNQSLSIELG RGGDQLLGSY
IQYIIPSIII LIIIGCICLL KISGCRKCKL PKSGATPDIE EDEMQPYASY TEKSNPLYDT
VTTTEAHPAS QGKVNGTDCL TLSAMGI
