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MOG_PONAB
ID   MOG_PONAB               Reviewed;         246 AA.
AC   Q5R960;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE   Flags: Precursor;
GN   Name=MOG;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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   -!- 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; CR859533; CAH91700.1; -; mRNA.
DR   RefSeq; NP_001125993.1; NM_001132521.1.
DR   AlphaFoldDB; Q5R960; -.
DR   SMR; Q5R960; -.
DR   STRING; 9601.ENSPPYP00000018325; -.
DR   GeneID; 100172932; -.
DR   KEGG; pon:100172932; -.
DR   CTD; 4340; -.
DR   eggNOG; ENOG502SQC1; Eukaryota.
DR   InParanoid; Q5R960; -.
DR   Proteomes; UP000001595; Unplaced.
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   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..246
FT                   /note="Myelin-oligodendrocyte glycoprotein"
FT                   /id="PRO_0000274530"
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          30..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;  28050 MW;  1822EC6BD7FFE143 CRC64;
     MASLSRPSLP SCLCSFLLLL LQVSSSYAGQ FRVIGPRHPI RALVGDEVEL PCRISPGKNA
     TGMEVGWYRP PFSRVVHLYR NGKDQDGEQA PEYRGRTELL KDAIGEGKVT LRIRNVRFSD
     EGGFTCFFRD HSYQEEAAME LKVEDPFYWV SPGVLVLLAV LPVLLLQIAV GLVFLCLQYR
     LRGKLRAEIE NLHRTFDPHF LRVPCWKITL FVIVPVLGPL VALIICYNWL HRRLAGQFLE
     ELRNPF
 
 
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