ID G1QXN9_NOMLE Unreviewed; 209 AA.
AC G1QXN9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Myelin-oligodendrocyte glycoprotein {ECO:0000256|ARBA:ARBA00019547, ECO:0000256|PIRNR:PIRNR016522};
GN Name=MOG {ECO:0000313|Ensembl:ENSNLEP00000005710.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000005710.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000005710.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000005710.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|PIRNR:PIRNR016522}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR016522}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.
CC {ECO:0000256|PIRNR:PIRNR016522}.
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DR EMBL; ADFV01069153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01069154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01069155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01069156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1QXN9; -.
DR Ensembl; ENSNLET00000006008.2; ENSNLEP00000005710.2; ENSNLEG00000004664.2.
DR GeneTree; ENSGT00940000153527; -.
DR HOGENOM; CLU_013137_10_0_1; -.
DR Proteomes; UP000001073; Chromosome 1a.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-UniRule.
DR CDD; cd05713; IgV_MOG_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR24100; BUTYROPHILIN; 1.
DR PANTHER; PTHR24100:SF71; MYELIN-OLIGODENDROCYTE GLYCOPROTEIN; 1.
DR Pfam; PF07686; V-set; 1.
DR PIRSF; PIRSF016522; MOG; 2.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|PIRNR:PIRNR016522};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|PIRNR:PIRNR016522, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..209
FT /note="Myelin-oligodendrocyte glycoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014178587"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..145
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 209 AA; 23867 MW; F13F7A590D733CAA CRC64;
MASLSRPSLP SCLCSFPLLL LLQVSSSYAG QFRVIGPRHP IRALVGDEVE LPCRISPGKN
ATGMEVGWYR PPFSRVVHLY RNGRDQDGEQ APEYRGRTEL LKDAIGEGKV TLRIQNVRFS
DEGGFTCFFR DHSYQEEAAM ELKVEGKLRA EIENLHRTFD PHFLRVPCWK ITLFVIVPVL
GPLVALIICY NWLHRRLAGQ FLEELRNPF
//
