Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q61885 (MOG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin-oligodendrocyte glycoprotein
Gene names
Name:Mog
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. Mediates homophilic cell-cell adhesion. Ref.6

Subunit structure

Homodimer. Ref.6

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Found exclusively in the CNS, where it is localized on the surface of myelin and oligodendrocyte cytoplasmic membranes.

Involvement in disease

Reduced concentrations of Mog are observed in jimpy and quacking dysmyelinating mutant mice.

Sequence similarities

Belongs to the immunoglobulin superfamily. BTN/MOG family.

Contains 1 Ig-like V-type (immunoglobulin-like) domain.

Caution

Do not confuse myelin-oligodendrocyte glycoprotein (MOG) with oligodendrocyte-myelin glycoprotein (OMG).

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.4
Chain29 – 246218Myelin-oligodendrocyte glycoprotein
PRO_0000014889

Regions

Topological domain29 – 156128Extracellular Potential
Transmembrane157 – 17721Helical; Potential
Topological domain178 – 20932Cytoplasmic Potential
Transmembrane210 – 23021Helical; Potential
Topological domain231 – 24616Extracellular Potential
Domain31 – 144114Ig-like V-type

Amino acid modifications

Glycosylation591N-linked (GlcNAc...) Potential
Disulfide bond52 ↔ 126 Ref.6

Experimental info

Sequence conflict211L → LL Ref.2
Sequence conflict321R → G AA sequence Ref.4
Sequence conflict951G → E Ref.3
Sequence conflict1691P → S in AAB08096. Ref.2

Secondary structure

........................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q61885 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 1F1A8A4A0D5CFB89

FASTA24628,271
        10         20         30         40         50         60 
MACLWSFSWP SCFLSLLLLL LQLSCSYAGQ FRVIGPGYPI RALVGDEAEL PCRISPGKNA 

        70         80         90        100        110        120 
TGMEVGWYRS PFSRVVHLYR NGKDQDAEQA PEYRGRTELL KETISEGKVT LRIQNVRFSD 

       130        140        150        160        170        180 
EGGYTCFFRD HSYQEEAAME LKVEDPFYWV NPGVLTLIAL VPTILLQVPV GLVFLFLQHR 

       190        200        210        220        230        240 
LRGKLRAEVE NLHRTFDPHF LRVPCWKITL FVIVPVLGPL VALIICYNWL HRRLAGQFLE 


ELRNPF 

« Hide

References

[1]"Structure and polymorphism of the mouse myelin/oligodendrocyte glycoprotein gene."
Daubas P., Pham-Dinh D., Dautigny A.
Genomics 23:36-41(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129.
[2]"Murine and human MOG are highly conserved: cDNA analysis."
Gardinier M.V., Matthieu J.-M.
Trans. Am. Soc. Neurochem. 24:234-234(1993)
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Myelin/oligodendrocyte glycoprotein is a member of a subset of the immunoglobulin superfamily encoded within the major histocompatibility complex."
Pham-Dinh D., Mattei M.-G., Nussbaum J.-L., Roussel G., Pontarotti P., Roeckel N., Mather I.H., Artzt K., Lindahl K.F., Dautigny A.
Proc. Natl. Acad. Sci. U.S.A. 90:7990-7994(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-246.
Strain: BALB/c.
Tissue: Brain.
[4]"Purification and partial structural and functional characterization of mouse myelin/oligodendrocyte glycoprotein."
Amiguet P., Gardinier M.V., Zanetta J.-P., Matthieu J.-M.
J. Neurochem. 58:1676-1682(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-54.
Strain: BALB/c.
Tissue: Brain.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 33-53; 81-94; 97-101; 118-142; 185-194 AND 234-246, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"The crystal structure of myelin oligodendrocyte glycoprotein, a key autoantigen in multiple sclerosis."
Clements C.S., Reid H.H., Beddoe T., Tynan F.E., Perugini M.A., Johns T.G., Bernard C.C., Rossjohn J.
Proc. Natl. Acad. Sci. U.S.A. 100:11059-11064(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-145, SUBUNIT, FUNCTION, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29503 expand/collapse EMBL AC list , L29498, L29500, L29501, L29499, L29502 Genomic DNA. Translation: AAC42023.1.
U64572 mRNA. Translation: AAB08096.1.
L20942 mRNA. Translation: AAA03180.1.
PIRA55717.
RefSeqNP_034944.2. NM_010814.2.
UniGeneMm.210857.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PY9X-ray1.80A30-145[»]
ProteinModelPortalQ61885.
SMRQ61885. Positions 30-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201465. 2 interactions.
IntActQ61885. 4 interactions.
MINTMINT-1176800.
STRING10090.ENSMUSP00000099726.

PTM databases

PhosphoSiteQ61885.

Proteomic databases

MaxQBQ61885.
PaxDbQ61885.
PRIDEQ61885.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID17441.
KEGGmmu:17441.

Organism-specific databases

CTD4340.
MGIMGI:97435. Mog.

Phylogenomic databases

eggNOGNOG146805.
HOVERGENHBG004565.
InParanoidQ61885.
KOK17270.

Gene expression databases

CleanExMM_MOG.
GenevestigatorQ61885.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013106. Ig_V-set.
IPR003596. Ig_V-set_subgr.
IPR016663. Myelin-oligodendrocyte_glycop.
[Graphical view]
PfamPF07686. V-set. 1 hit.
[Graphical view]
PIRSFPIRSF016522. MOG. 1 hit.
SMARTSM00406. IGv. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ61885.
NextBio292076.
PROQ61885.
SOURCESearch...

Entry information

Entry nameMOG_MOUSE
AccessionPrimary (citable) accession number: Q61885
Secondary accession number(s): P70364, Q62003
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot