MOG_MOUSE
ID MOG_MOUSE Reviewed; 246 AA.
AC Q61885; P70364; Q62003;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE Flags: Precursor;
GN Name=Mog;
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 [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=7829100; DOI=10.1006/geno.1994.1456;
RA Daubas P., Pham-Dinh D., Dautigny A.;
RT "Structure and polymorphism of the mouse myelin/oligodendrocyte
RT glycoprotein gene.";
RL Genomics 23:36-41(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Gardinier M.V., Matthieu J.-M.;
RT "Murine and human MOG are highly conserved: cDNA analysis.";
RL Trans. Am. Soc. Neurochem. 24:234-234(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 29-246.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8367453; DOI=10.1073/pnas.90.17.7990;
RA Pham-Dinh D., Mattei M.-G., Nussbaum J.-L., Roussel G., Pontarotti P.,
RA Roeckel N., Mather I.H., Artzt K., Lindahl K.F., Dautigny A.;
RT "Myelin/oligodendrocyte glycoprotein is a member of a subset of the
RT immunoglobulin superfamily encoded within the major histocompatibility
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7990-7994(1993).
RN [4]
RP PROTEIN SEQUENCE OF 29-54, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1373175; DOI=10.1111/j.1471-4159.1992.tb10040.x;
RA Amiguet P., Gardinier M.V., Zanetta J.-P., Matthieu J.-M.;
RT "Purification and partial structural and functional characterization of
RT mouse myelin/oligodendrocyte glycoprotein.";
RL J. Neurochem. 58:1676-1682(1992).
RN [5]
RP PROTEIN SEQUENCE OF 33-53; 81-94; 97-101; 118-142; 185-194 AND 234-246, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-145, SUBUNIT, FUNCTION, AND
RP DISULFIDE BOND.
RX PubMed=12960396; DOI=10.1073/pnas.1833158100;
RA Clements C.S., Reid H.H., Beddoe T., Tynan F.E., Perugini M.A., Johns T.G.,
RA Bernard C.C., Rossjohn J.;
RT "The crystal structure of myelin oligodendrocyte glycoprotein, a key
RT autoantigen in multiple sclerosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11059-11064(2003).
CC -!- FUNCTION: Minor component of the myelin sheath. May be involved in
CC completion and/or maintenance of the myelin sheath and in cell-cell
CC communication. Mediates homophilic cell-cell adhesion.
CC {ECO:0000269|PubMed:12960396}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12960396}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Found exclusively in the CNS, where it is localized
CC on the surface of myelin and oligodendrocyte cytoplasmic membranes.
CC Reduced expression levels are observed in jimpy and quacking
CC dysmyelinating mutant mice. {ECO:0000269|PubMed:1373175}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000305}.
CC -!- CAUTION: Do not confuse myelin-oligodendrocyte glycoprotein (MOG) with
CC oligodendrocyte-myelin glycoprotein (OMG). {ECO:0000305}.
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DR EMBL; L29503; AAC42023.1; -; Genomic_DNA.
DR EMBL; L29498; AAC42023.1; JOINED; Genomic_DNA.
DR EMBL; L29500; AAC42023.1; JOINED; Genomic_DNA.
DR EMBL; L29501; AAC42023.1; JOINED; Genomic_DNA.
DR EMBL; L29499; AAC42023.1; JOINED; Genomic_DNA.
DR EMBL; L29502; AAC42023.1; JOINED; Genomic_DNA.
DR EMBL; U64572; AAB08096.1; -; mRNA.
DR EMBL; L20942; AAA03180.1; -; mRNA.
DR PIR; A55717; A55717.
DR RefSeq; NP_034944.2; NM_010814.2.
DR PDB; 1PY9; X-ray; 1.80 A; A=30-145.
DR PDBsum; 1PY9; -.
DR AlphaFoldDB; Q61885; -.
DR SMR; Q61885; -.
DR BioGRID; 201465; 7.
DR IntAct; Q61885; 4.
DR MINT; Q61885; -.
DR STRING; 10090.ENSMUSP00000099726; -.
DR GlyConnect; 2520; 15 N-Linked glycans (1 site).
DR GlyGen; Q61885; 1 site, 14 N-linked glycans (1 site).
DR iPTMnet; Q61885; -.
DR PhosphoSitePlus; Q61885; -.
DR SwissPalm; Q61885; -.
DR MaxQB; Q61885; -.
DR PaxDb; Q61885; -.
DR PRIDE; Q61885; -.
DR ProteomicsDB; 290275; -.
DR DNASU; 17441; -.
DR GeneID; 17441; -.
DR KEGG; mmu:17441; -.
DR CTD; 4340; -.
DR MGI; MGI:97435; Mog.
DR eggNOG; ENOG502SQC1; Eukaryota.
DR InParanoid; Q61885; -.
DR OrthoDB; 1057931at2759; -.
DR BioGRID-ORCS; 17441; 2 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q61885; -.
DR PRO; PR:Q61885; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61885; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR016663; Myelin-oligodendrocyte_glycop.
DR Pfam; PF07686; V-set; 1.
DR PIRSF; PIRSF016522; MOG; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:1373175"
FT CHAIN 29..246
FT /note="Myelin-oligodendrocyte glycoprotein"
FT /id="PRO_0000014889"
FT TOPO_DOM 29..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 31..144
FT /note="Ig-like V-type"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:12960396"
FT CONFLICT 21
FT /note="L -> LL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="R -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="G -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="P -> S (in Ref. 2; AAB08096)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1PY9"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1PY9"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:1PY9"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1PY9"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1PY9"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:1PY9"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:1PY9"
SQ SEQUENCE 246 AA; 28271 MW; 1F1A8A4A0D5CFB89 CRC64;
MACLWSFSWP SCFLSLLLLL LQLSCSYAGQ FRVIGPGYPI RALVGDEAEL PCRISPGKNA
TGMEVGWYRS PFSRVVHLYR NGKDQDAEQA PEYRGRTELL KETISEGKVT LRIQNVRFSD
EGGYTCFFRD HSYQEEAAME LKVEDPFYWV NPGVLTLIAL VPTILLQVPV GLVFLFLQHR
LRGKLRAEVE NLHRTFDPHF LRVPCWKITL FVIVPVLGPL VALIICYNWL HRRLAGQFLE
ELRNPF
