ID   MO2R1_BOVIN             Reviewed;         355 AA.
AC   A5D7V5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=CD200R;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) 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 {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CD200R family. {ECO:0000305}.
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DR   EMBL; BC140695; AAI40696.1; -; mRNA.
DR   RefSeq; NP_001092844.1; NM_001099374.2.
DR   AlphaFoldDB; A5D7V5; -.
DR   SMR; A5D7V5; -.
DR   STRING; 9913.ENSBTAP00000001635; -.
DR   PaxDb; A5D7V5; -.
DR   PRIDE; A5D7V5; -.
DR   Ensembl; ENSBTAT00000001635; ENSBTAP00000001635; ENSBTAG00000001235.
DR   GeneID; 516008; -.
DR   KEGG; bta:516008; -.
DR   CTD; 344807; -.
DR   VEuPathDB; HostDB:ENSBTAG00000001235; -.
DR   eggNOG; ENOG502SPS1; Eukaryota.
DR   GeneTree; ENSGT00390000014496; -.
DR   HOGENOM; CLU_069156_0_0_1; -.
DR   InParanoid; A5D7V5; -.
DR   OMA; PYTTYVQ; -.
DR   OrthoDB; 993609at2759; -.
DR   TreeFam; TF335960; -.
DR   Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000001235; Expressed in monocyte and 85 other tissues.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
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; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..355
FT                   /note="Cell surface glycoprotein CD200 receptor 1"
FT                   /id="PRO_0000346449"
FT   TOPO_DOM        27..267
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          139..257
FT                   /note="Ig-like C2-type"
FT   REGION          35..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        85..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        108..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        191..241
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        210..229
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   355 AA;  39220 MW;  AC9FD1D78B480F42 CRC64;
     MPCTWITSDL QLRLILTLFF VAECLSAGME GTKTSNNSMQ QLDNGNHSSV STTSSTERKQ
     STVTLYAEVK TSLSVLVDTK AVLTCPPVLW PSVLVVTWEI VLRDKPPCFG AYRRDTNQTT
     RGNCTDKRIT WASRPDENPA LQVDPVAITH DGNYTCQIVT SDGNFHHEYH LQVLVPPEVT
     LIQTEKGTAV CKAAAGKPAA QISWTPEGDC DTEQGPYWGD GTVTVQSTCR WGSRHVLNVS
     CSVSHLAGNK SLSIQLSQGA EIPAHLKNLY ITAPIFIILI VVGSIWLLKI SGCRKCKLKK
     TEHTPVVQED EMEPYASYTE KNNPLYDITN RVKTSQVLQS EVDGMNLHTI YVPRV