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 16-SEP-2015, entry version 121. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT MRC 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 RT murine 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/c; 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/6; 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 RT expression."; RL Cell 143:1174-1189(2010). RN [6] RP X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 31-232 IN COMPLEX WITH RP CD200R, DISULFIDE BONDS, SUBUNIT, AND MUTAGENESIS OF GLN-37; GLN-57; RP LEU-60; 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 RT topology, regulation, and evolution."; RL Structure 21:820-832(2013). CC -!- FUNCTION: Costimulates T-cell proliferation. May regulate myeloid CC cell activity in a variety of tissues (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: CD200 and CD200R1 interact via their respective N- CC terminal Ig-like domains. {ECO:0000269|PubMed:23602662}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like) CC domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) CC domain. {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; 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 UniGene; Mm.245851; -. DR PDB; 4BFI; X-ray; 3.22 A; B=31-232. DR PDBsum; 4BFI; -. DR ProteinModelPortal; O54901; -. DR SMR; O54901; 32-232. DR DIP; DIP-60157N; -. DR IntAct; O54901; 1. DR MINT; MINT-4105943; -. DR STRING; 10090.ENSMUSP00000130518; -. DR PhosphoSite; O54901; -. DR MaxQB; O54901; -. DR PaxDb; O54901; -. DR PRIDE; O54901; -. DR MGI; MGI:1196990; Cd200. DR eggNOG; NOG72791; -. DR HOGENOM; HOG000035940; -. DR HOVERGEN; HBG031790; -. DR InParanoid; O54901; -. DR ChiTaRS; Cd200; mouse. DR PRO; PR:O54901; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_CD200; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043031; P:negative regulation of macrophage activation; IMP:CACAO. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013106; Ig_V-set. DR InterPro; IPR013151; Immunoglobulin. DR Pfam; PF00047; ig; 2. 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; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 278 OX-2 membrane glycoprotein. FT /FTId=PRO_0000015125. FT TOPO_DOM 31 232 Extracellular. {ECO:0000255}. FT TRANSMEM 233 259 Helical. {ECO:0000255}. FT TOPO_DOM 260 278 Cytoplasmic. {ECO:0000255}. FT DOMAIN 31 141 Ig-like V-type. FT DOMAIN 142 232 Ig-like C2-type. FT CARBOHYD 95 95 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 103 103 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 110 110 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 157 157 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 181 181 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 190 190 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 51 121 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:23602662}. FT DISULFID 118 136 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:23602662}. FT DISULFID 160 214 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:23602662}. FT MUTAGEN 37 37 Q->K: No effect on binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 57 57 Q->K: Enhances binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 60 60 L->K: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 61 61 I->E: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 74 74 N->A: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 122 122 L->A: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 124 124 N->K: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT MUTAGEN 126 126 F->D: Abolishes binding to CD200R. FT {ECO:0000269|PubMed:23602662}. FT CONFLICT 22 22 M -> I (in Ref. 2; AAB93980). FT {ECO:0000305}. FT CONFLICT 112 116 TLEDE -> HIGDG (in Ref. 2; AAB93980). FT {ECO:0000305}. FT CONFLICT 154 154 D -> H (in Ref. 2; AAB93980). FT {ECO:0000305}. FT CONFLICT 171 171 S -> T (in Ref. 2; AAB93980). FT {ECO:0000305}. FT CONFLICT 251 251 V -> I (in Ref. 2; AAB93980). FT {ECO:0000305}. FT STRAND 34 36 {ECO:0000244|PDB:4BFI}. FT STRAND 39 42 {ECO:0000244|PDB:4BFI}. FT STRAND 47 53 {ECO:0000244|PDB:4BFI}. FT STRAND 55 57 {ECO:0000244|PDB:4BFI}. FT STRAND 60 66 {ECO:0000244|PDB:4BFI}. FT STRAND 69 71 {ECO:0000244|PDB:4BFI}. FT STRAND 73 79 {ECO:0000244|PDB:4BFI}. FT TURN 80 82 {ECO:0000244|PDB:4BFI}. FT STRAND 83 86 {ECO:0000244|PDB:4BFI}. FT HELIX 88 90 {ECO:0000244|PDB:4BFI}. FT TURN 91 93 {ECO:0000244|PDB:4BFI}. FT STRAND 94 98 {ECO:0000244|PDB:4BFI}. FT STRAND 101 110 {ECO:0000244|PDB:4BFI}. FT HELIX 113 115 {ECO:0000244|PDB:4BFI}. FT STRAND 117 124 {ECO:0000244|PDB:4BFI}. FT STRAND 134 151 {ECO:0000244|PDB:4BFI}. FT STRAND 156 166 {ECO:0000244|PDB:4BFI}. FT STRAND 169 174 {ECO:0000244|PDB:4BFI}. FT STRAND 180 187 {ECO:0000244|PDB:4BFI}. FT STRAND 189 191 {ECO:0000244|PDB:4BFI}. FT STRAND 193 200 {ECO:0000244|PDB:4BFI}. FT TURN 204 206 {ECO:0000244|PDB:4BFI}. FT STRAND 212 218 {ECO:0000244|PDB:4BFI}. FT STRAND 221 227 {ECO:0000244|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 //