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Protein

OX-2 membrane glycoprotein

Gene

Cd200

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 - Molecular functioni

GO - Biological processi

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1196990 Cd200

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini31 – 232ExtracellularSequence analysisAdd BLAST202
Transmembranei233 – 259HelicalSequence analysisAdd BLAST27
Topological domaini260 – 278CytoplasmicSequence analysisAdd BLAST19

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi37Q → K: No effect on binding to CD200R. 1 Publication1
Mutagenesisi57Q → K: Enhances binding to CD200R. 1 Publication1
Mutagenesisi60L → K: Abolishes binding to CD200R. 1 Publication1
Mutagenesisi61I → E: Abolishes binding to CD200R. 1 Publication1
Mutagenesisi74N → A: Abolishes binding to CD200R. 1 Publication1
Mutagenesisi122L → A: Abolishes binding to CD200R. 1 Publication1
Mutagenesisi124N → K: Abolishes binding to CD200R. 1 Publication1
Mutagenesisi126F → D: Abolishes binding to CD200R. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000001512531 – 278OX-2 membrane glycoproteinAdd BLAST248

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi51 ↔ 121PROSITE-ProRule annotation1 Publication
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi103N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi110N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi118 ↔ 136PROSITE-ProRule annotation1 Publication
Glycosylationi157N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi160 ↔ 214PROSITE-ProRule annotation1 Publication
Glycosylationi181N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi190N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO54901
PaxDbiO54901
PeptideAtlasiO54901
PRIDEiO54901

PTM databases

PhosphoSitePlusiO54901

Expressioni

Gene expression databases

CleanExiMM_CD200

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd200r1Q9ES573EBI-8328786,EBI-16045630

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-60157N
IntActiO54901, 3 interactors
MINTiO54901
STRINGi10090.ENSMUSP00000130518

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 36Combined sources3
Beta strandi39 – 42Combined sources4
Beta strandi47 – 53Combined sources7
Beta strandi55 – 57Combined sources3
Beta strandi60 – 66Combined sources7
Beta strandi69 – 71Combined sources3
Beta strandi73 – 79Combined sources7
Turni80 – 82Combined sources3
Beta strandi83 – 86Combined sources4
Helixi88 – 90Combined sources3
Turni91 – 93Combined sources3
Beta strandi94 – 98Combined sources5
Beta strandi101 – 110Combined sources10
Helixi113 – 115Combined sources3
Beta strandi117 – 124Combined sources8
Beta strandi134 – 151Combined sources18
Beta strandi156 – 166Combined sources11
Beta strandi169 – 174Combined sources6
Beta strandi180 – 187Combined sources8
Beta strandi189 – 191Combined sources3
Beta strandi193 – 200Combined sources8
Turni204 – 206Combined sources3
Beta strandi212 – 218Combined sources7
Beta strandi221 – 227Combined sources7

3D structure databases

ProteinModelPortaliO54901
SMRiO54901
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 141Ig-like V-typeAdd BLAST111
Domaini142 – 232Ig-like C2-typeAdd BLAST91

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
InterProiView protein in InterPro
IPR033321 CD200
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR013106 Ig_V-set
IPR013151 Immunoglobulin
PANTHERiPTHR23277:SF72 PTHR23277:SF72, 1 hit
PfamiView protein in Pfam
PF00047 ig, 2 hits
SMARTiView protein in SMART
SM00409 IG, 1 hit
SM00406 IGv, 1 hit
SUPFAMiSSF48726 SSF48726, 2 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti22M → I in AAB93980 (PubMed:9457671).Curated1
Sequence conflicti112 – 116TLEDE → HIGDG in AAB93980 (PubMed:9457671).Curated5
Sequence conflicti154D → H in AAB93980 (PubMed:9457671).Curated1
Sequence conflicti171S → T in AAB93980 (PubMed:9457671).Curated1
Sequence conflicti251V → I in AAB93980 (PubMed:9457671).Curated1

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

Similar proteinsi

Entry informationi

Entry nameiOX2G_MOUSE
AccessioniPrimary (citable) accession number: O54901
Secondary accession number(s): O54816, Q9JHD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2002
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 131 of the entry and version 1 of the sequence. See 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

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