ID   MOG_MACFA               Reviewed;         247 AA.
AC   Q9BGS7; Q29ZP2; Q7YRD9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE   Flags: Precursor;
GN   Name=MOG; ORFNames=QflA-14648;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=16903876; DOI=10.1111/j.1471-4159.2006.04053.x;
RA   Delarasse C., Della Gaspera B., Lu C.W., Lachapelle F., Gelot A.,
RA   Rodriguez D., Dautigny A., Genain C., Pham-Dinh D.;
RT   "Complex alternative splicing of the myelin oligodendrocyte glycoprotein
RT   gene is unique to human and non-human primates.";
RL   J. Neurochem. 98:1707-1717(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BGS7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BGS7-2; Sequence=VSP_022790;
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; AF399846; AAQ03032.1; -; mRNA.
DR   EMBL; AY566843; AAU10108.1; -; mRNA.
DR   EMBL; AB056396; BAB33052.1; -; mRNA.
DR   RefSeq; NP_001271785.1; NM_001284856.1. [Q9BGS7-1]
DR   RefSeq; XP_005553734.1; XM_005553677.2. [Q9BGS7-2]
DR   AlphaFoldDB; Q9BGS7; -.
DR   SMR; Q9BGS7; -.
DR   STRING; 9541.XP_005553734.1; -.
DR   Ensembl; ENSMFAT00000000166; ENSMFAP00000001639; ENSMFAG00000037244. [Q9BGS7-1]
DR   GeneID; 102118842; -.
DR   KEGG; mcf:102118842; -.
DR   CTD; 4340; -.
DR   VEuPathDB; HostDB:ENSMFAG00000037244; -.
DR   eggNOG; ENOG502SQC1; Eukaryota.
DR   GeneTree; ENSGT00940000153527; -.
DR   Proteomes; UP000233100; Chromosome 4.
DR   Bgee; ENSMFAG00000037244; Expressed in frontal cortex and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..247
FT                   /note="Myelin-oligodendrocyte glycoprotein"
FT                   /id="PRO_0000274529"
FT   TOPO_DOM        30..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          31..145
FT                   /note="Ig-like V-type"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         244..247
FT                   /note="RNPF -> IFHLETLPG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16903876"
FT                   /id="VSP_022790"
SQ   SEQUENCE   247 AA;  28208 MW;  7058C48E3A98C393 CRC64;
     MASLSRPSLP SCLCSFLLLL LLQVSSSYAG QFRVIGPRQP IRALVGDEVE LPCRISPGKN
     ATGMEVGWYR PPFSRVVHLY RNGRDQDGEQ APEYRGRTEL LKDAIGEGKV TLRIRNVRFS
     DEGGFTCFFR DHSYQEEAAI ELKVEDPFYW VSPAVLVLLA VLPVLLLQIT VGLVFLCLQY
     RLRGKLRAEI ENLHRTFDPH FLRVPCWKIT LFVIVPVLGP LVALIICYNW LHRRLAGQFL
     EELRNPF