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