ID U3E6A3_CALJA Unreviewed; 245 AA.
AC U3E6A3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Myelin-oligodendrocyte glycoprotein {ECO:0000256|ARBA:ARBA00019547, ECO:0000256|PIRNR:PIRNR016522};
GN Name=MOG {ECO:0000313|EMBL:JAB46433.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB46433.1};
RN [1] {ECO:0000313|EMBL:JAB46433.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:JAB46433.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB30276.1}, and Hippocampus
RC {ECO:0000313|EMBL:JAB13889.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
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; GAMS01009247; JAB13889.1; -; mRNA.
DR EMBL; GAMS01009246; JAB13890.1; -; mRNA.
DR EMBL; GAMS01009245; JAB13891.1; -; mRNA.
DR EMBL; GAMR01003656; JAB30276.1; -; mRNA.
DR EMBL; GAMR01003655; JAB30277.1; -; mRNA.
DR EMBL; GAMP01006322; JAB46433.1; -; mRNA.
DR RefSeq; NP_001244171.1; NM_001257242.1.
DR AlphaFoldDB; U3E6A3; -.
DR SMR; U3E6A3; -.
DR GeneID; 100400400; -.
DR KEGG; cjc:100400400; -.
DR CTD; 4340; -.
DR HOGENOM; CLU_013137_10_4_1; -.
DR OrthoDB; 2943983at2759; -.
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; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00406; IGv; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion {ECO:0000256|PIRNR:PIRNR016522};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|PIRNR:PIRNR016522, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..245
FT /note="Myelin-oligodendrocyte glycoprotein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010152548"
FT TRANSMEM 146..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..143
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 245 AA; 27920 MW; 2E7B648605A79811 CRC64;
MASLSKPSLP SYLCFLLLLL HVSSSYGGQF RVIGPSHPIQ ALVGDAAELP CRISPGKNAT
GMEVGWYRSP FSRVVHLYRN GKDQDGEQAP EYRGRTELLK DDIGEGKVTL KIRNVRFPDE
GGFTCFFRDH SYQEEAAMQL KVEDPFYWVS PGVLVLLAVL PVLFLQITVG LVFLYLQHRL
RGKLRAEIEN LHRTFDPHFL RVPCWKITLF VIVPVLGPLV ALIICYNWLH RRLAGQFLEE
LRNPF
//
