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MOG_CALJA
ID   MOG_CALJA               Reviewed;         245 AA.
AC   Q29ZQ1; Q29ZP8; Q29ZP9; Q29ZQ0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE   Flags: Precursor;
GN   Name=MOG;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
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).
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=4;
CC       Name=1;
CC         IsoId=Q29ZQ1-1; Sequence=Displayed;
CC       Name=2; Synonyms=MOG alpha-4;
CC         IsoId=Q29ZQ1-2; Sequence=VSP_022786;
CC       Name=3; Synonyms=MOG alpha-7Cj;
CC         IsoId=Q29ZQ1-3; Sequence=VSP_022789;
CC       Name=4; Synonyms=MOG alpha-4Cj;
CC         IsoId=Q29ZQ1-4; Sequence=VSP_022787, VSP_022788;
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; AY566834; AAU09333.1; -; mRNA.
DR   EMBL; AY566835; AAU09334.1; -; mRNA.
DR   EMBL; AY566836; AAU09335.1; -; mRNA.
DR   EMBL; AY566837; AAU09336.1; -; mRNA.
DR   RefSeq; NP_001244171.1; NM_001257242.1. [Q29ZQ1-1]
DR   RefSeq; NP_001244172.1; NM_001257243.1. [Q29ZQ1-2]
DR   RefSeq; NP_001244173.1; NM_001257244.1.
DR   AlphaFoldDB; Q29ZQ1; -.
DR   SMR; Q29ZQ1; -.
DR   STRING; 9483.ENSCJAP00000028006; -.
DR   GeneID; 100400400; -.
DR   KEGG; cjc:100400400; -.
DR   CTD; 4340; -.
DR   eggNOG; ENOG502SQC1; Eukaryota.
DR   HOGENOM; CLU_013137_10_4_1; -.
DR   InParanoid; Q29ZQ1; -.
DR   OrthoDB; 1057931at2759; -.
DR   Proteomes; UP000008225; Chromosome 4.
DR   Bgee; ENSCJAG00000043626; Expressed in cerebellum and 1 other tissue.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..245
FT                   /note="Myelin-oligodendrocyte glycoprotein"
FT                   /id="PRO_0000274528"
FT   TOPO_DOM        28..152
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..245
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..143
FT                   /note="Ig-like V-type"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         28..143
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16903876"
FT                   /id="VSP_022786"
FT   VAR_SEQ         28..47
FT                   /note="GQFRVIGPSHPIQALVGDAA -> EMARIKMESRHLNIGVEQSC (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16903876"
FT                   /id="VSP_022787"
FT   VAR_SEQ         48..245
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16903876"
FT                   /id="VSP_022788"
FT   VAR_SEQ         139..176
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16903876"
FT                   /id="VSP_022789"
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
 
 
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