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Protein

OX-2 membrane glycoprotein

Gene

Cd200

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues (By similarity).By similarity

GO - Biological processi

  • negative regulation of macrophage activation Source: CACAO
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
OX-2 membrane glycoprotein
Alternative name(s):
MRC OX-2 antigen
CD_antigen: CD200
Gene namesi
Name:Cd200
Synonyms:Mox2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1196990. Cd200.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 232202ExtracellularSequence analysisAdd
BLAST
Transmembranei233 – 25927HelicalSequence analysisAdd
BLAST
Topological domaini260 – 27819CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371Q → K: No effect on binding to CD200R. 1 Publication
Mutagenesisi57 – 571Q → K: Enhances binding to CD200R. 1 Publication
Mutagenesisi60 – 601L → K: Abolishes binding to CD200R. 1 Publication
Mutagenesisi61 – 611I → E: Abolishes binding to CD200R. 1 Publication
Mutagenesisi74 – 741N → A: Abolishes binding to CD200R. 1 Publication
Mutagenesisi122 – 1221L → A: Abolishes binding to CD200R. 1 Publication
Mutagenesisi124 – 1241N → K: Abolishes binding to CD200R. 1 Publication
Mutagenesisi126 – 1261F → D: Abolishes binding to CD200R. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 278248OX-2 membrane glycoproteinPRO_0000015125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 121PROSITE-ProRule annotation1 Publication
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence analysis
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi118 ↔ 136PROSITE-ProRule annotation1 Publication
Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence analysis
Disulfide bondi160 ↔ 214PROSITE-ProRule annotation1 Publication
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO54901.
PaxDbiO54901.
PRIDEiO54901.

PTM databases

PhosphoSiteiO54901.

Expressioni

Gene expression databases

CleanExiMM_CD200.

Interactioni

Subunit structurei

CD200 and CD200R1 interact via their respective N-terminal Ig-like domains.1 Publication

Protein-protein interaction databases

DIPiDIP-60157N.
IntActiO54901. 1 interaction.
MINTiMINT-4105943.
STRINGi10090.ENSMUSP00000130518.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 363Combined sources
Beta strandi39 – 424Combined sources
Beta strandi47 – 537Combined sources
Beta strandi55 – 573Combined sources
Beta strandi60 – 667Combined sources
Beta strandi69 – 713Combined sources
Beta strandi73 – 797Combined sources
Turni80 – 823Combined sources
Beta strandi83 – 864Combined sources
Helixi88 – 903Combined sources
Turni91 – 933Combined sources
Beta strandi94 – 985Combined sources
Beta strandi101 – 11010Combined sources
Helixi113 – 1153Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi134 – 15118Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi169 – 1746Combined sources
Beta strandi180 – 1878Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi193 – 2008Combined sources
Turni204 – 2063Combined sources
Beta strandi212 – 2187Combined sources
Beta strandi221 – 2277Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BFIX-ray3.22B31-232[»]
ProteinModelPortaliO54901.
SMRiO54901. Positions 32-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 141111Ig-like V-typeAdd
BLAST
Domaini142 – 23291Ig-like C2-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWZ9. Eukaryota.
ENOG410YRD3. LUCA.
HOGENOMiHOG000035940.
HOVERGENiHBG031790.
InParanoidiO54901.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR033321. CD200.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR23277:SF72. PTHR23277:SF72. 1 hit.
PfamiPF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O54901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSLVFRRPF CHLSTYSLIW GMAAVALSTA QVEVVTQDER KALHTTASLR
60 70 80 90 100
CSLKTSQEPL IVTWQKKKAV SPENMVTYSK THGVVIQPAY KDRINVTELG
110 120 130 140 150
LWNSSITFWN TTLEDEGCYM CLFNTFGSQK VSGTACLTLY VQPIVHLHYN
160 170 180 190 200
YFEDHLNITC SATARPAPAI SWKGTGTGIE NSTESHFHSN GTTSVTSILR
210 220 230 240 250
VKDPKTQVGK EVICQVLYLG NVIDYKQSLD KGFWFSVPLL LSIVSLVILL
260 270
VLISILLYWK RHRNQERGES SQGMQRMK
Length:278
Mass (Da):31,256
Last modified:June 1, 1998 - v1
Checksum:i0D06A2DE0C60DF5A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221M → I in AAB93980 (PubMed:9457671).Curated
Sequence conflicti112 – 1165TLEDE → HIGDG in AAB93980 (PubMed:9457671).Curated
Sequence conflicti154 – 1541D → H in AAB93980 (PubMed:9457671).Curated
Sequence conflicti171 – 1711S → T in AAB93980 (PubMed:9457671).Curated
Sequence conflicti251 – 2511V → I in AAB93980 (PubMed:9457671).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004023 mRNA. Translation: AAB93980.1.
AF029215, AF029214 Genomic DNA. Translation: AAC15911.1.
AF231126 mRNA. Translation: AAF61105.1.
CCDSiCCDS49860.1.
UniGeneiMm.245851.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004023 mRNA. Translation: AAB93980.1.
AF029215, AF029214 Genomic DNA. Translation: AAC15911.1.
AF231126 mRNA. Translation: AAF61105.1.
CCDSiCCDS49860.1.
UniGeneiMm.245851.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BFIX-ray3.22B31-232[»]
ProteinModelPortaliO54901.
SMRiO54901. Positions 32-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60157N.
IntActiO54901. 1 interaction.
MINTiMINT-4105943.
STRINGi10090.ENSMUSP00000130518.

PTM databases

PhosphoSiteiO54901.

Proteomic databases

MaxQBiO54901.
PaxDbiO54901.
PRIDEiO54901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1196990. Cd200.

Phylogenomic databases

eggNOGiENOG410IWZ9. Eukaryota.
ENOG410YRD3. LUCA.
HOGENOMiHOG000035940.
HOVERGENiHBG031790.
InParanoidiO54901.

Miscellaneous databases

ChiTaRSiCd200. mouse.
PROiO54901.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CD200.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR033321. CD200.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR013151. Immunoglobulin.
[Graphical view]
PANTHERiPTHR23277:SF72. PTHR23277:SF72. 1 hit.
PfamiPF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00406. IGv. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the murine homologue of the rat/human MRC OX-2 gene."
    Chen Z., Zeng H., Gorczynski R.M.
    Biochim. Biophys. Acta 1362:6-10(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeJ.
  2. "Characterization and localization of Mox2, the gene encoding the murine homolog of the rat MRC OX-2 membrane glycoprotein."
    Borriello F., Tizard R., Rue E., Reeves R.
    Mamm. Genome 9:114-118(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  3. Preston S., Wright G.J., Starr K., Barclay A.N., Brown M.H.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-225.
    Strain: BALB/cJ.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 69-80, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart and Lung.
  6. "Structures of CD200/CD200 receptor family and implications for topology, regulation, and evolution."
    Hatherley D., Lea S.M., Johnson S., Barclay A.N.
    Structure 21:820-832(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.22 ANGSTROMS) OF 31-232 IN COMPLEX WITH CD200R, DISULFIDE BONDS, SUBUNIT, MUTAGENESIS OF GLN-37; GLN-57; LEU-60; ILE-61; ASN-74; LEU-122; ASN-124 AND PHE-126.

Entry informationi

Entry nameiOX2G_MOUSE
AccessioniPrimary (citable) accession number: O54901
Secondary accession number(s): O54816, Q9JHD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.