ID   E9QMY1_MOUSE            Unreviewed;       269 AA.
AC   E9QMY1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=CD200 molecule {ECO:0000313|Ensembl:ENSMUSP00000023341.9};
GN   Name=Cd200 {ECO:0000313|Ensembl:ENSMUSP00000023341.9,
GN   ECO:0000313|MGI:MGI:1196990};
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 {ECO:0000313|Ensembl:ENSMUSP00000023341.9, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000023341.9, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000023341.9,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000023341.9}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000023341.9};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; E9QMY1; -.
DR   SMR; E9QMY1; -.
DR   jPOST; E9QMY1; -.
DR   MaxQB; E9QMY1; -.
DR   PeptideAtlas; E9QMY1; -.
DR   ProteomicsDB; 323024; -.
DR   Antibodypedia; 16297; 1068 antibodies from 42 providers.
DR   Ensembl; ENSMUST00000023341.15; ENSMUSP00000023341.9; ENSMUSG00000022661.15.
DR   AGR; MGI:1196990; -.
DR   MGI; MGI:1196990; Cd200.
DR   VEuPathDB; HostDB:ENSMUSG00000022661; -.
DR   GeneTree; ENSGT00530000063970; -.
DR   HOGENOM; CLU_064101_0_0_1; -.
DR   ChiTaRS; Cd200; mouse.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022661; Expressed in subparaventricular zone and 267 other cell types or tissues.
DR   ExpressionAtlas; E9QMY1; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; IEA:InterPro.
DR   GO; GO:0043031; P:negative regulation of macrophage activation; IEA:InterPro.
DR   GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR   CDD; cd05846; IgV_1_MRC-OX-2_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR033321; CD200_Ig_V_dom.
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   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR047164; OX2G-like.
DR   PANTHER; PTHR46841; OX-2 MEMBRANE GLYCOPROTEIN; 1.
DR   PANTHER; PTHR46841:SF3; OX-2 MEMBRANE GLYCOPROTEIN; 1.
DR   Pfam; PF00047; ig; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Proteomics identification {ECO:0007829|EPD:E9QMY1,
KW   ECO:0007829|MaxQB:E9QMY1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..269
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003243344"
FT   TRANSMEM        233..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          30..138
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
SQ   SEQUENCE   269 AA;  30292 MW;  06A531F397D46675 CRC64;
     MGSLVFRRPF CHLSTYSLIW GMAAVALSTA QVEVVTQDER KALHTTASLR CSLKTSQEPL
     IVTWQKKKAV SPENMVTYSK THGVVIQPAY KDRINVTELG LWNSSITFWN TTLEDEGCYM
     CLFNTFGSQK VSGTACLTLY VQPIVHLHYN YFEDHLNITC SATARPAPAI SWKGTGTGIE
     NSTESHFHSN GTTSVTSILR VKDPKTQVGK EVICQVLYLG NVIDYKQSLD KGFWFSVPLL
     LSIVSLVILL ILISILLYWK RHRNQEREL
//