MOG_RAT
ID MOG_RAT Reviewed; 245 AA.
AC Q63345;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE Flags: Precursor;
GN Name=Mog;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF N-TERMINUS.
RX PubMed=1453482; DOI=10.1002/jnr.490330123;
RA Gardinier M.V., Amiguet P., Linington C., Matthieu J.-M.;
RT "Myelin/oligodendrocyte glycoprotein is a unique member of the
RT immunoglobulin superfamily.";
RL J. Neurosci. Res. 33:177-187(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-245.
RC 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 [3]
RP PROTEIN SEQUENCE OF 32-68; 83-93; 129-141; 186-193 AND 233-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-58, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [5]
RP STRUCTURE BY NMR OF 62-82.
RX PubMed=9210466; DOI=10.1111/j.1432-1033.1997.t01-2-00059.x;
RA Albouz-Abo S., Wilson J.C., Bernard C.C.A., von Itzstein M.;
RT "A conformational study of the human and rat encephalitogenic myelin
RT oligodendrocyte glycoprotein peptides 35-55.";
RL Eur. J. Biochem. 246:59-70(1997).
CC -!- FUNCTION: Mediates homophilic cell-cell adhesion (By similarity). Minor
CC component of the myelin sheath. May be involved in completion and/or
CC maintenance of the myelin sheath and in cell-cell communication.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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 -!- DEVELOPMENTAL STAGE: A peak of expression has been observed between
CC postnatal days 15 and 25, coinciding with the period of active
CC myelination.
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; M99485; AAA41628.1; -; mRNA.
DR EMBL; L21995; AAF74786.1; -; mRNA.
DR PIR; B47712; B47712.
DR PDB; 1PKO; X-ray; 1.45 A; A=28-152.
DR PDB; 1PKQ; X-ray; 3.00 A; E/J=28-152.
DR PDB; 3CSP; X-ray; 1.70 A; A=27-152.
DR PDBsum; 1PKO; -.
DR PDBsum; 1PKQ; -.
DR PDBsum; 3CSP; -.
DR AlphaFoldDB; Q63345; -.
DR SMR; Q63345; -.
DR IntAct; Q63345; 1.
DR MINT; Q63345; -.
DR STRING; 10116.ENSRNOP00000001008; -.
DR GlyGen; Q63345; 1 site, 76 N-linked glycans (1 site).
DR iPTMnet; Q63345; -.
DR PhosphoSitePlus; Q63345; -.
DR SwissPalm; Q63345; -.
DR PaxDb; Q63345; -.
DR PRIDE; Q63345; -.
DR ABCD; Q63345; 12 sequenced antibodies.
DR UCSC; RGD:3102; rat.
DR RGD; 3102; Mog.
DR eggNOG; ENOG502SQC1; Eukaryota.
DR InParanoid; Q63345; -.
DR PhylomeDB; Q63345; -.
DR EvolutionaryTrace; Q63345; -.
DR PRO; PR:Q63345; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
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:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
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..27
FT /evidence="ECO:0000269|PubMed:1453482"
FT CHAIN 28..245
FT /note="Myelin-oligodendrocyte glycoprotein"
FT /id="PRO_0000014890"
FT TOPO_DOM 28..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 30..139
FT /note="Ig-like"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 51..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1PKO"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3CSP"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1PKO"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1PKO"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:1PKO"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1PKO"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:1PKO"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:1PKO"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:1PKO"
SQ SEQUENCE 245 AA; 27882 MW; C97F8AD60D6A32B4 CRC64;
MAGVWSLSLP SCLLSLLLLL QLSRSYAGQF RVIGPGHPIR ALVGDEAELP CRISPGKNAT
GMEVGWYRSP FSRVVHLYRN GKDQDAEQAP EYRGRTELLK ESIGEGKVAL RIQNVRFSDE
GGYTCFFRDH SYQEEAAVEL KVEDPFYWIN PGVLALIALV PMLLLQVSVG LVFLFLQHRL
RGKLRAEVEN LHRTFDPHFL RVPCWKITLF VIVPVLGPLV ALIICYNWLH RRLAGQFLEE
LRNPF
