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OX-2 membrane glycoprotein (MRC OX-2 antigen) (CD antigen CD200)

 OX2G_MOUSE              Reviewed;         278 AA.
O54901; O54816; Q9JHD5;
28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
23-MAY-2018, entry version 131.
RecName: Full=OX-2 membrane glycoprotein;
AltName: Full=MRC OX-2 antigen;
AltName: CD_antigen=CD200;
Flags: Precursor;
Name=Cd200; Synonyms=Mox2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/HeJ;
PubMed=9434094; DOI=10.1016/S0925-4439(97)00058-6;
Chen Z., Zeng H., Gorczynski R.M.;
"Cloning and characterization of the murine homologue of the rat/human
MRC OX-2 gene.";
Biochim. Biophys. Acta 1362:6-10(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129;
PubMed=9457671; DOI=10.1007/s003359900700;
Borriello F., Tizard R., Rue E., Reeves R.;
"Characterization and localization of Mox2, the gene encoding the
murine homolog of the rat MRC OX-2 membrane glycoprotein.";
Mamm. Genome 9:114-118(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-225.
STRAIN=BALB/cJ;
Preston S., Wright G.J., Starr K., Barclay A.N., Brown M.H.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 69-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 31-232 IN COMPLEX WITH
CD200R, DISULFIDE BONDS, SUBUNIT, AND MUTAGENESIS OF GLN-37; GLN-57;
LEU-60; ILE-61; ASN-74; LEU-122; ASN-124 AND PHE-126.
PubMed=23602662; DOI=10.1016/j.str.2013.03.008;
Hatherley D., Lea S.M., Johnson S., Barclay A.N.;
"Structures of CD200/CD200 receptor family and implications for
topology, regulation, and evolution.";
Structure 21:820-832(2013).
-!- FUNCTION: Costimulates T-cell proliferation. May regulate myeloid
cell activity in a variety of tissues (By similarity).
{ECO:0000250}.
-!- SUBUNIT: CD200 and CD200R1 interact via their respective N-
terminal Ig-like domains. {ECO:0000269|PubMed:23602662}.
-!- INTERACTION:
Q9ES57:Cd200r1; NbExp=3; IntAct=EBI-8328786, EBI-16045630;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF004023; AAB93980.1; -; mRNA.
EMBL; AF029215; AAC15911.1; -; Genomic_DNA.
EMBL; AF029214; AAC15911.1; JOINED; Genomic_DNA.
EMBL; AF231126; AAF61105.1; -; mRNA.
CCDS; CCDS49860.1; -.
UniGene; Mm.245851; -.
PDB; 4BFI; X-ray; 3.22 A; B=31-232.
PDBsum; 4BFI; -.
ProteinModelPortal; O54901; -.
SMR; O54901; -.
DIP; DIP-60157N; -.
IntAct; O54901; 3.
MINT; O54901; -.
STRING; 10090.ENSMUSP00000130518; -.
PhosphoSitePlus; O54901; -.
MaxQB; O54901; -.
PaxDb; O54901; -.
PeptideAtlas; O54901; -.
PRIDE; O54901; -.
MGI; MGI:1196990; Cd200.
eggNOG; ENOG410IWZ9; Eukaryota.
eggNOG; ENOG410YRD3; LUCA.
HOGENOM; HOG000035940; -.
HOVERGEN; HBG031790; -.
InParanoid; O54901; -.
ChiTaRS; Cd200; mouse.
PRO; PR:O54901; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CD200; -.
GO; GO:0005913; C:cell-cell adherens junction; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
GO; GO:0043031; P:negative regulation of macrophage activation; IMP:CACAO.
GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR033321; CD200.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR013151; Immunoglobulin.
PANTHER; PTHR23277:SF72; PTHR23277:SF72; 1.
Pfam; PF00047; ig; 2.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 2.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 278 OX-2 membrane glycoprotein.
/FTId=PRO_0000015125.
TOPO_DOM 31 232 Extracellular. {ECO:0000255}.
TRANSMEM 233 259 Helical. {ECO:0000255}.
TOPO_DOM 260 278 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 141 Ig-like V-type.
DOMAIN 142 232 Ig-like C2-type.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 157 157 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 51 121 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23602662}.
DISULFID 118 136 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23602662}.
DISULFID 160 214 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:23602662}.
MUTAGEN 37 37 Q->K: No effect on binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 57 57 Q->K: Enhances binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 60 60 L->K: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 61 61 I->E: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 74 74 N->A: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 122 122 L->A: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 124 124 N->K: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
MUTAGEN 126 126 F->D: Abolishes binding to CD200R.
{ECO:0000269|PubMed:23602662}.
CONFLICT 22 22 M -> I (in Ref. 2; AAB93980).
{ECO:0000305}.
CONFLICT 112 116 TLEDE -> HIGDG (in Ref. 2; AAB93980).
{ECO:0000305}.
CONFLICT 154 154 D -> H (in Ref. 2; AAB93980).
{ECO:0000305}.
CONFLICT 171 171 S -> T (in Ref. 2; AAB93980).
{ECO:0000305}.
CONFLICT 251 251 V -> I (in Ref. 2; AAB93980).
{ECO:0000305}.
STRAND 34 36 {ECO:0000244|PDB:4BFI}.
STRAND 39 42 {ECO:0000244|PDB:4BFI}.
STRAND 47 53 {ECO:0000244|PDB:4BFI}.
STRAND 55 57 {ECO:0000244|PDB:4BFI}.
STRAND 60 66 {ECO:0000244|PDB:4BFI}.
STRAND 69 71 {ECO:0000244|PDB:4BFI}.
STRAND 73 79 {ECO:0000244|PDB:4BFI}.
TURN 80 82 {ECO:0000244|PDB:4BFI}.
STRAND 83 86 {ECO:0000244|PDB:4BFI}.
HELIX 88 90 {ECO:0000244|PDB:4BFI}.
TURN 91 93 {ECO:0000244|PDB:4BFI}.
STRAND 94 98 {ECO:0000244|PDB:4BFI}.
STRAND 101 110 {ECO:0000244|PDB:4BFI}.
HELIX 113 115 {ECO:0000244|PDB:4BFI}.
STRAND 117 124 {ECO:0000244|PDB:4BFI}.
STRAND 134 151 {ECO:0000244|PDB:4BFI}.
STRAND 156 166 {ECO:0000244|PDB:4BFI}.
STRAND 169 174 {ECO:0000244|PDB:4BFI}.
STRAND 180 187 {ECO:0000244|PDB:4BFI}.
STRAND 189 191 {ECO:0000244|PDB:4BFI}.
STRAND 193 200 {ECO:0000244|PDB:4BFI}.
TURN 204 206 {ECO:0000244|PDB:4BFI}.
STRAND 212 218 {ECO:0000244|PDB:4BFI}.
STRAND 221 227 {ECO:0000244|PDB:4BFI}.
SEQUENCE 278 AA; 31256 MW; 0D06A2DE0C60DF5A 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 VLISILLYWK RHRNQERGES SQGMQRMK


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