ID   MOG_BOVIN               Reviewed;         246 AA.
AC   P55803; A5PKD0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE   Flags: Precursor;
GN   Name=MOG;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-70.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 29-36.
RC   TISSUE=Brain;
RX   PubMed=8371836; DOI=10.1007/bf00998280;
RA   Birling M.C., Roussel G., Nussbaum F., Nussbaum J.-L.;
RT   "Biochemical and immunohistochemical studies with specific polyclonal
RT   antibodies directed against bovine myelin/oligodendrocyte glycoprotein.";
RL   Neurochem. Res. 18:937-945(1993).
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   -!- 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; L21757; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC142443; AAI42444.1; -; mRNA.
DR   PIR; A47712; A47712.
DR   AlphaFoldDB; P55803; -.
DR   SMR; P55803; -.
DR   STRING; 9913.ENSBTAP00000042496; -.
DR   PaxDb; P55803; -.
DR   Ensembl; ENSBTAT00000045079; ENSBTAP00000042496; ENSBTAG00000017818.
DR   VEuPathDB; HostDB:ENSBTAG00000017818; -.
DR   VGNC; VGNC:57316; MOG.
DR   eggNOG; ENOG502SQC1; Eukaryota.
DR   GeneTree; ENSGT00940000153527; -.
DR   InParanoid; P55803; -.
DR   OMA; CWKVALF; -.
DR   TreeFam; TF331083; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000017818; Expressed in hypothalamus and 105 other tissues.
DR   ExpressionAtlas; P55803; baseline.
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: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   Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:8371836"
FT   CHAIN           29..246
FT                   /note="Myelin-oligodendrocyte glycoprotein"
FT                   /id="PRO_0000014887"
FT   TOPO_DOM        29..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..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          29..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"
SQ   SEQUENCE   246 AA;  28028 MW;  363C76AB1A33DE41 CRC64;
     MASLLSSSLP SCLPSLLFLL LQLTSSSAGQ FRVIGPGHPI RALVGDEVEL PCRISPGKNA
     TGMEVGWYRP PFSRVVHLYR NGKDQDEEQA PEYRGRTQLL KETIGEGKVT LRIRNVRFSD
     EGGFTCFFRD HSYQEEAAME LKVEDPFYWI NPGVLVLIAV LPVLLLQITV GLVFLCLQRR
     LRGKLWAEIE NLHRTFDPHF LMVPCWKITL FVIVPVLGPL VALIICYNWL HRRLAGQFLE
     ELRNPF