OX2G_MOUSE
ID OX2G_MOUSE Reviewed; 278 AA.
AC O54901; O54816; Q9JHD5;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=OX-2 membrane glycoprotein;
DE AltName: Full=MRC OX-2 antigen;
DE AltName: CD_antigen=CD200;
DE Flags: Precursor;
GN Name=Cd200; Synonyms=Mox2;
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].
RC STRAIN=C3H/HeJ;
RX PubMed=9434094; DOI=10.1016/s0925-4439(97)00058-6;
RA Chen Z., Zeng H., Gorczynski R.M.;
RT "Cloning and characterization of the murine homologue of the rat/human MRC
RT OX-2 gene.";
RL Biochim. Biophys. Acta 1362:6-10(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9457671; DOI=10.1007/s003359900700;
RA Borriello F., Tizard R., Rue E., Reeves R.;
RT "Characterization and localization of Mox2, the gene encoding the murine
RT homolog of the rat MRC OX-2 membrane glycoprotein.";
RL Mamm. Genome 9:114-118(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-225.
RC STRAIN=BALB/cJ;
RA Preston S., Wright G.J., Starr K., Barclay A.N., Brown M.H.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 69-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 31-232 IN COMPLEX WITH CD200R,
RP DISULFIDE BONDS, SUBUNIT, AND MUTAGENESIS OF GLN-37; GLN-57; LEU-60;
RP ILE-61; ASN-74; LEU-122; ASN-124 AND PHE-126.
RX PubMed=23602662; DOI=10.1016/j.str.2013.03.008;
RA Hatherley D., Lea S.M., Johnson S., Barclay A.N.;
RT "Structures of CD200/CD200 receptor family and implications for topology,
RT regulation, and evolution.";
RL Structure 21:820-832(2013).
CC -!- FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell
CC activity in a variety of tissues (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N-terminal Ig-
CC like domains. {ECO:0000269|PubMed:23602662}.
CC -!- INTERACTION:
CC O54901; Q9ES57: Cd200r1; NbExp=3; IntAct=EBI-8328786, EBI-16045630;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
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; AF004023; AAB93980.1; -; mRNA.
DR EMBL; AF029215; AAC15911.1; -; Genomic_DNA.
DR EMBL; AF029214; AAC15911.1; JOINED; Genomic_DNA.
DR EMBL; AF231126; AAF61105.1; -; mRNA.
DR CCDS; CCDS49860.1; -.
DR PDB; 4BFI; X-ray; 3.22 A; B=31-232.
DR PDBsum; 4BFI; -.
DR AlphaFoldDB; O54901; -.
DR SMR; O54901; -.
DR DIP; DIP-60157N; -.
DR IntAct; O54901; 2.
DR STRING; 10090.ENSMUSP00000130518; -.
DR GlyConnect; 2198; 4 N-Linked glycans (2 sites).
DR GlyGen; O54901; 6 sites, 4 N-linked glycans (2 sites).
DR PhosphoSitePlus; O54901; -.
DR jPOST; O54901; -.
DR MaxQB; O54901; -.
DR PaxDb; O54901; -.
DR PeptideAtlas; O54901; -.
DR PRIDE; O54901; -.
DR ProteomicsDB; 294141; -.
DR ABCD; O54901; 23 sequenced antibodies.
DR MGI; MGI:1196990; Cd200.
DR eggNOG; ENOG502S5DU; Eukaryota.
DR InParanoid; O54901; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR ChiTaRS; Cd200; mouse.
DR PRO; PR:O54901; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O54901; protein.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0043031; P:negative regulation of macrophage activation; IMP:CACAO.
DR GO; GO:1905522; P:negative regulation of macrophage migration; ISO:MGI.
DR GO; GO:1904465; P:negative regulation of matrix metallopeptidase secretion; ISO:MGI.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; IMP:ARUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:2000405; P:negative regulation of T cell migration; ISO:MGI.
DR GO; GO:0150072; P:positive regulation of arginase activity; ISO:MGI.
DR GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISO:MGI.
DR GO; GO:0150074; P:positive regulation of protein-glutamine gamma-glutamyltransferase activity; ISO:MGI.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI.
DR GO; GO:0050776; P:regulation of immune response; IEA:InterPro.
DR GO; GO:0150077; P:regulation of neuroinflammatory response; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR033321; CD200.
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 PANTHER; PTHR46841:SF3; PTHR46841:SF3; 1.
DR Pfam; PF00047; ig; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..278
FT /note="OX-2 membrane glycoprotein"
FT /id="PRO_0000015125"
FT TOPO_DOM 31..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..141
FT /note="Ig-like V-type"
FT DOMAIN 142..232
FT /note="Ig-like C2-type"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT DISULFID 118..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT DISULFID 160..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23602662"
FT MUTAGEN 37
FT /note="Q->K: No effect on binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 57
FT /note="Q->K: Enhances binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 60
FT /note="L->K: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 61
FT /note="I->E: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 74
FT /note="N->A: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 122
FT /note="L->A: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 124
FT /note="N->K: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT MUTAGEN 126
FT /note="F->D: Abolishes binding to CD200R."
FT /evidence="ECO:0000269|PubMed:23602662"
FT CONFLICT 22
FT /note="M -> I (in Ref. 2; AAB93980)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..116
FT /note="TLEDE -> HIGDG (in Ref. 2; AAB93980)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> H (in Ref. 2; AAB93980)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> T (in Ref. 2; AAB93980)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="V -> I (in Ref. 2; AAB93980)"
FT /evidence="ECO:0000305"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4BFI"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4BFI"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:4BFI"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:4BFI"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 134..151
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:4BFI"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:4BFI"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4BFI"
SQ 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
