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MOG_HUMAN
ID   MOG_HUMAN               Reviewed;         247 AA.
AC   Q16653; A6NDR4; A6NNJ9; A8MY31; B0UZR9; E9PGF0; F8W9D5; O00713; O00714;
AC   O00715; Q13054; Q13055; Q14855; Q29ZN8; Q56UY0; Q5JNX7; Q5JNY1; Q5JNY2;
AC   Q5JNY4; Q5SSB5; Q5SSB6; Q5STL9; Q5STM0; Q5STM1; Q5STM2; Q5STM5; Q5SUK5;
AC   Q5SUK7; Q5SUK8; Q5SUK9; Q5SUL0; Q5SUL1; Q8IYG5; Q92891; Q92892; Q92893;
AC   Q92894; Q92895; Q93053; Q96KU9; Q96KV0; Q96KV1; Q99605;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Myelin-oligodendrocyte glycoprotein;
DE   Flags: Precursor;
GN   Name=MOG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANT VAL-174.
RX   PubMed=7790876; DOI=10.1046/j.1471-4159.1995.65010309.x;
RA   Hilton A.A., Slavin A.J., Hilton D.J., Bernard C.C.A.;
RT   "Characterization of cDNA and genomic clones encoding human myelin
RT   oligodendrocyte glycoprotein.";
RL   J. Neurochem. 65:309-318(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-174.
RC   TISSUE=Brain;
RX   PubMed=7964757; DOI=10.1046/j.1471-4159.1994.63062353.x;
RA   Pham-Dinh D., Allinquant B., Ruberg M., della Gaspera B., Nussbaum J.-L.,
RA   Dautigny A.;
RT   "Characterization and expression of the cDNA coding for the human
RT   myelin/oligodendrocyte glycoprotein.";
RL   J. Neurochem. 63:2353-2356(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-171 AND VAL-174.
RX   PubMed=8530032; DOI=10.1006/geno.1995.1137;
RA   Roth M.-P., Malfroy L., Offer C., Sevin J., Enault G., Borot N.,
RA   Pontarotti P., Coppin H.;
RT   "The human myelin oligodendrocyte glycoprotein (MOG) gene: complete
RT   nucleotide sequence and structural characterization.";
RL   Genomics 28:241-250(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANT VAL-174.
RX   PubMed=8666381; DOI=10.1006/geno.1995.9995;
RA   Pham-Dinh D., Della Gaspera B., de Rosbo N.K., Dautigny A.;
RT   "Structure of the human myelin/oligodendrocyte glycoprotein gene and
RT   multiple alternative spliced isoforms.";
RL   Genomics 29:345-352(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 30-247 (ISOFORM 10), AND VARIANT VAL-174.
RX   PubMed=8915905;
RX   DOI=10.1002/(sici)1097-4547(19961015)46:2<271::aid-jnr16>3.0.co;2-5;
RA   Ballenthin P.A., Gardinier M.V.;
RT   "Myelin/oligodendrocyte glycoprotein is alternatively spliced in humans but
RT   not mice.";
RL   J. Neurosci. Res. 46:271-281(1996).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-174.
RC   TISSUE=Brain cortex;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS LEU-171 AND
RP   VAL-174.
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-174.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13), AND VARIANT VAL-174.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-206 (ISOFORM 11), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 3-108 (ISOFORM 12), ALTERNATIVE SPLICING, AND VARIANT VAL-174.
RA   Delarasse C., Della Gaspera B., Genain C., Pham-Dinh D.;
RT   "Alternative splicing of the MOG gene across species.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH RUBELLA VIRUS E2
RP   GLYCOPROTEIN.
RX   PubMed=21880773; DOI=10.1128/jvi.05398-11;
RA   Cong H., Jiang Y., Tien P.;
RT   "Identification of the myelin oligodendrocyte glycoprotein as a cellular
RT   receptor for rubella virus.";
RL   J. Virol. 85:11038-11047(2011).
RN   [12]
RP   STRUCTURE BY NMR OF 64-84.
RX   PubMed=9210466; DOI=10.1111/j.1432-1033.1997.t01-2-00059.x;
RA   Albouz-Abo S., Wilson J.C., Bernard C.C.A., von Itzstein M.;
RT   "A conformational study of the human and rat encephalitogenic myelin
RT   oligodendrocyte glycoprotein peptides 35-55.";
RL   Eur. J. Biochem. 246:59-70(1997).
RN   [13]
RP   VARIANT NRCLP7 CYS-133.
RX   PubMed=21907016; DOI=10.1016/j.ajhg.2011.08.007;
RA   Hor H., Bartesaghi L., Kutalik Z., Vicario J.L., de Andres C., Pfister C.,
RA   Lammers G.J., Guex N., Chrast R., Tafti M., Peraita-Adrados R.;
RT   "A missense mutation in myelin oligodendrocyte glycoprotein as a cause of
RT   familial narcolepsy with cataplexy.";
RL   Am. J. Hum. Genet. 89:474-479(2011).
CC   -!- FUNCTION: Mediates homophilic cell-cell adhesion (By similarity). Minor
CC       component of the myelin sheath. May be involved in completion and/or
CC       maintenance of the myelin sheath and in cell-cell communication.
CC       {ECO:0000250}.
CC   -!- FUNCTION: (Microbial infection) Acts as a receptor for rubella virus.
CC       {ECO:0000269|PubMed:21880773}.
CC   -!- SUBUNIT: Homodimer (By similarity). May form heterodimers between the
CC       different isoforms (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with rubella virus E2
CC       glycoprotein. {ECO:0000269|PubMed:21880773}.
CC   -!- INTERACTION:
CC       Q16653-13; P42858: HTT; NbExp=12; IntAct=EBI-24226707, EBI-466029;
CC       Q16653-13; P0DN84: STRIT1; NbExp=3; IntAct=EBI-24226707, EBI-12200293;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000305}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 7]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 8]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 9]: Cell membrane {ECO:0000305}; Single-
CC       pass type I membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=Alpha-1;
CC         IsoId=Q16653-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-2;
CC         IsoId=Q16653-2; Sequence=VSP_002543;
CC       Name=3; Synonyms=Alpha-3;
CC         IsoId=Q16653-3; Sequence=VSP_002542;
CC       Name=4; Synonyms=Alpha-4;
CC         IsoId=Q16653-4; Sequence=VSP_002539;
CC       Name=5; Synonyms=Beta-1;
CC         IsoId=Q16653-5; Sequence=VSP_002545;
CC       Name=6; Synonyms=Beta-2;
CC         IsoId=Q16653-6; Sequence=VSP_002543, VSP_002545;
CC       Name=7; Synonyms=Beta-3;
CC         IsoId=Q16653-7; Sequence=VSP_002542, VSP_002545;
CC       Name=8; Synonyms=Beta-4;
CC         IsoId=Q16653-8; Sequence=VSP_002544, VSP_002545;
CC       Name=9;
CC         IsoId=Q16653-9; Sequence=VSP_002540, VSP_002541;
CC       Name=10;
CC         IsoId=Q16653-10; Sequence=VSP_040344, VSP_040345;
CC       Name=11;
CC         IsoId=Q16653-11; Sequence=VSP_046856;
CC       Name=12;
CC         IsoId=Q16653-12; Sequence=VSP_002539, VSP_002542;
CC       Name=13; Synonyms=X1;
CC         IsoId=Q16653-13; Sequence=VSP_055600;
CC   -!- TISSUE SPECIFICITY: Found exclusively in the CNS, where it is localized
CC       on the surface of myelin and oligodendrocyte cytoplasmic membranes.
CC   -!- DISEASE: Narcolepsy 7 (NRCLP7) [MIM:614250]: Neurological disabling
CC       sleep disorder, characterized by excessive daytime sleepiness, sleep
CC       fragmentation, symptoms of abnormal rapid-eye-movement (REM) sleep,
CC       cataplexy, hypnagogic hallucinations, and sleep paralysis. Cataplexy is
CC       a sudden loss of muscle tone triggered by emotions, which is the most
CC       valuable clinical feature used to diagnose narcolepsy. Human narcolepsy
CC       is primarily a sporadically occurring disorder but familial clustering
CC       has been observed. {ECO:0000269|PubMed:21907016}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 9]: Not functionally active. May be expressed
CC       at low level in the adult. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 10]: May be produced at very low levels due to
CC       a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {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}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Myelin oligodendrocyte glycoprotein
CC       entry;
CC       URL="https://en.wikipedia.org/wiki/Myelin_oligodendrocyte_glycoprotein";
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DR   EMBL; X74511; CAA52617.1; -; mRNA.
DR   EMBL; Z48051; CAA88109.1; -; Genomic_DNA.
DR   EMBL; U18840; AAC50361.1; -; mRNA.
DR   EMBL; U18843; AAC50362.1; -; mRNA.
DR   EMBL; U18798; AAC50876.1; -; mRNA.
DR   EMBL; U18799; AAC50877.1; -; mRNA.
DR   EMBL; U18800; AAB36870.1; -; mRNA.
DR   EMBL; U18801; AAC50878.1; -; mRNA.
DR   EMBL; U18803; AAC50879.1; -; mRNA.
DR   EMBL; U64564; AAB08088.1; -; mRNA.
DR   EMBL; U64565; AAB08089.1; -; mRNA.
DR   EMBL; U64566; AAB08090.1; -; mRNA.
DR   EMBL; U64567; AAB08091.1; -; mRNA.
DR   EMBL; U64568; AAB08092.1; -; mRNA.
DR   EMBL; U64569; AAB08093.1; -; mRNA.
DR   EMBL; U64570; AAB08094.1; -; mRNA.
DR   EMBL; U64571; AAB08095.1; -; mRNA.
DR   EMBL; AK312892; BAG35739.1; -; mRNA.
DR   EMBL; AL050328; CAB89267.1; -; Genomic_DNA.
DR   EMBL; AL050328; CAB89268.1; -; Genomic_DNA.
DR   EMBL; AL050328; CAB89269.1; -; Genomic_DNA.
DR   EMBL; AL050328; CAB89270.1; -; Genomic_DNA.
DR   EMBL; AL050328; CAB89271.1; -; Genomic_DNA.
DR   EMBL; AL645936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL669813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL929591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX120002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX927250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR388408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR936483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03213.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03214.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03216.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03217.1; -; Genomic_DNA.
DR   EMBL; BC035938; AAH35938.1; -; mRNA.
DR   EMBL; AY566847; AAU09338.1; -; mRNA.
DR   EMBL; AY566853; AAU09343.1; -; mRNA.
DR   CCDS; CCDS34366.1; -. [Q16653-7]
DR   CCDS; CCDS34367.1; -. [Q16653-6]
DR   CCDS; CCDS34368.1; -. [Q16653-11]
DR   CCDS; CCDS34369.1; -. [Q16653-3]
DR   CCDS; CCDS34370.1; -. [Q16653-1]
DR   CCDS; CCDS4667.1; -. [Q16653-5]
DR   CCDS; CCDS47394.1; -. [Q16653-2]
DR   CCDS; CCDS47395.2; -. [Q16653-4]
DR   CCDS; CCDS54977.1; -. [Q16653-12]
DR   CCDS; CCDS87379.1; -. [Q16653-13]
DR   PIR; S58394; S58394.
DR   RefSeq; NP_001008229.1; NM_001008228.2. [Q16653-3]
DR   RefSeq; NP_001008230.1; NM_001008229.2. [Q16653-11]
DR   RefSeq; NP_001163889.1; NM_001170418.1. [Q16653-12]
DR   RefSeq; NP_002424.3; NM_002433.4. [Q16653-5]
DR   RefSeq; NP_996532.2; NM_206809.3. [Q16653-1]
DR   RefSeq; NP_996533.2; NM_206810.3. [Q16653-6]
DR   RefSeq; NP_996534.2; NM_206811.3. [Q16653-7]
DR   RefSeq; NP_996535.2; NM_206812.3. [Q16653-2]
DR   RefSeq; NP_996537.3; NM_206814.5. [Q16653-4]
DR   RefSeq; XP_005249188.1; XM_005249131.3.
DR   AlphaFoldDB; Q16653; -.
DR   SMR; Q16653; -.
DR   BioGRID; 110482; 23.
DR   IntAct; Q16653; 5.
DR   MINT; Q16653; -.
DR   STRING; 9606.ENSP00000366095; -.
DR   GlyGen; Q16653; 1 site.
DR   iPTMnet; Q16653; -.
DR   PhosphoSitePlus; Q16653; -.
DR   SwissPalm; Q16653; -.
DR   BioMuta; MOG; -.
DR   DMDM; 317373391; -.
DR   MassIVE; Q16653; -.
DR   PaxDb; Q16653; -.
DR   PeptideAtlas; Q16653; -.
DR   PRIDE; Q16653; -.
DR   ProteomicsDB; 20308; -.
DR   ProteomicsDB; 30306; -.
DR   ProteomicsDB; 61003; -. [Q16653-1]
DR   ProteomicsDB; 61004; -. [Q16653-10]
DR   ProteomicsDB; 61005; -. [Q16653-2]
DR   ProteomicsDB; 61006; -. [Q16653-3]
DR   ProteomicsDB; 61007; -. [Q16653-4]
DR   ProteomicsDB; 61008; -. [Q16653-5]
DR   ProteomicsDB; 61009; -. [Q16653-6]
DR   ProteomicsDB; 61010; -. [Q16653-7]
DR   ProteomicsDB; 61011; -. [Q16653-8]
DR   ProteomicsDB; 61012; -. [Q16653-9]
DR   ProteomicsDB; 63907; -.
DR   ProteomicsDB; 63921; -.
DR   ProteomicsDB; 71170; -.
DR   Antibodypedia; 44829; 403 antibodies from 42 providers.
DR   DNASU; 4340; -.
DR   Ensembl; ENST00000259891.11; ENSP00000259891.7; ENSG00000137345.19.
DR   Ensembl; ENST00000359539.7; ENSP00000352534.3; ENSG00000137345.19.
DR   Ensembl; ENST00000376888.6; ENSP00000366085.2; ENSG00000204655.12. [Q16653-4]
DR   Ensembl; ENST00000376891.8; ENSP00000366088.4; ENSG00000204655.12. [Q16653-11]
DR   Ensembl; ENST00000376894.8; ENSP00000366091.4; ENSG00000204655.12. [Q16653-13]
DR   Ensembl; ENST00000376898.7; ENSP00000366095.3; ENSG00000204655.12. [Q16653-5]
DR   Ensembl; ENST00000376917.8; ENSP00000366115.3; ENSG00000204655.12. [Q16653-1]
DR   Ensembl; ENST00000383521.6; ENSP00000373013.2; ENSG00000237834.9.
DR   Ensembl; ENST00000383525.7; ENSP00000373017.3; ENSG00000237834.9.
DR   Ensembl; ENST00000383630.7; ENSP00000373126.3; ENSG00000137345.19.
DR   Ensembl; ENST00000383631.6; ENSP00000373127.2; ENSG00000137345.19.
DR   Ensembl; ENST00000396701.6; ENSP00000379929.2; ENSG00000204655.12. [Q16653-6]
DR   Ensembl; ENST00000396704.7; ENSP00000379932.3; ENSG00000204655.12. [Q16653-3]
DR   Ensembl; ENST00000400669.5; ENSP00000383510.1; ENSG00000237834.9.
DR   Ensembl; ENST00000400671.5; ENSP00000383512.1; ENSG00000237834.9.
DR   Ensembl; ENST00000400688.5; ENSP00000383526.1; ENSG00000137345.19.
DR   Ensembl; ENST00000400691.6; ENSP00000383528.2; ENSG00000137345.19.
DR   Ensembl; ENST00000412760.6; ENSP00000404245.2; ENSG00000237834.9.
DR   Ensembl; ENST00000414889.6; ENSP00000403380.2; ENSG00000234623.9.
DR   Ensembl; ENST00000415546.6; ENSP00000404149.2; ENSG00000234096.9.
DR   Ensembl; ENST00000417019.6; ENSP00000404537.2; ENSG00000234096.9.
DR   Ensembl; ENST00000419274.5; ENSP00000411489.1; ENSG00000236561.9.
DR   Ensembl; ENST00000419309.6; ENSP00000395005.2; ENSG00000236561.9.
DR   Ensembl; ENST00000420045.5; ENSP00000390682.1; ENSG00000234096.9.
DR   Ensembl; ENST00000423895.6; ENSP00000390632.2; ENSG00000230885.9.
DR   Ensembl; ENST00000425145.6; ENSP00000397101.2; ENSG00000234623.9.
DR   Ensembl; ENST00000426782.5; ENSP00000410699.1; ENSG00000230885.9.
DR   Ensembl; ENST00000427289.6; ENSP00000414489.2; ENSG00000230885.9.
DR   Ensembl; ENST00000428719.5; ENSP00000397723.1; ENSG00000234096.9.
DR   Ensembl; ENST00000430264.5; ENSP00000403058.1; ENSG00000234623.9.
DR   Ensembl; ENST00000430351.5; ENSP00000410268.1; ENSG00000234096.9.
DR   Ensembl; ENST00000431798.6; ENSP00000410866.2; ENSG00000204655.12. [Q16653-2]
DR   Ensembl; ENST00000432271.6; ENSP00000389221.2; ENSG00000234623.9.
DR   Ensembl; ENST00000433500.5; ENSP00000413364.1; ENSG00000236561.9.
DR   Ensembl; ENST00000434177.5; ENSP00000398197.1; ENSG00000234623.9.
DR   Ensembl; ENST00000438803.6; ENSP00000414862.2; ENSG00000236561.9.
DR   Ensembl; ENST00000439634.5; ENSP00000404957.1; ENSG00000234096.9.
DR   Ensembl; ENST00000439884.6; ENSP00000398394.2; ENSG00000237834.9.
DR   Ensembl; ENST00000440561.5; ENSP00000409534.1; ENSG00000230885.9.
DR   Ensembl; ENST00000442244.5; ENSP00000391516.1; ENSG00000236561.9.
DR   Ensembl; ENST00000442444.6; ENSP00000414146.2; ENSG00000137345.19.
DR   Ensembl; ENST00000442629.5; ENSP00000399240.1; ENSG00000234623.9.
DR   Ensembl; ENST00000444674.6; ENSP00000390469.2; ENSG00000230885.9.
DR   Ensembl; ENST00000447285.6; ENSP00000401609.2; ENSG00000236561.9.
DR   Ensembl; ENST00000448816.5; ENSP00000397837.1; ENSG00000237834.9.
DR   Ensembl; ENST00000449096.6; ENSP00000391898.2; ENSG00000234096.9.
DR   Ensembl; ENST00000452233.5; ENSP00000394873.1; ENSG00000234623.9.
DR   Ensembl; ENST00000452744.6; ENSP00000389022.2; ENSG00000232641.10.
DR   Ensembl; ENST00000457090.5; ENSP00000415883.1; ENSG00000236561.9.
DR   Ensembl; ENST00000457626.5; ENSP00000402139.1; ENSG00000230885.9.
DR   Ensembl; ENST00000458179.5; ENSP00000413370.1; ENSG00000230885.9.
DR   Ensembl; ENST00000490427.5; ENSP00000420350.1; ENSG00000204655.12. [Q16653-12]
DR   Ensembl; ENST00000494692.5; ENSP00000417405.1; ENSG00000204655.12. [Q16653-7]
DR   Ensembl; ENST00000547083.1; ENSP00000449213.1; ENSG00000137345.19.
DR   Ensembl; ENST00000548017.1; ENSP00000448732.1; ENSG00000234096.9.
DR   Ensembl; ENST00000550849.1; ENSP00000449683.1; ENSG00000237834.9.
DR   Ensembl; ENST00000551175.1; ENSP00000448879.1; ENSG00000234623.9.
DR   Ensembl; ENST00000551993.1; ENSP00000446871.1; ENSG00000230885.9.
DR   Ensembl; ENST00000553111.1; ENSP00000447099.1; ENSG00000236561.9.
DR   GeneID; 4340; -.
DR   KEGG; hsa:4340; -.
DR   MANE-Select; ENST00000376917.8; ENSP00000366115.3; NM_206809.4; NP_996532.2.
DR   UCSC; uc003nmy.3; human. [Q16653-1]
DR   CTD; 4340; -.
DR   DisGeNET; 4340; -.
DR   GeneCards; MOG; -.
DR   HGNC; HGNC:7197; MOG.
DR   HPA; ENSG00000204655; Tissue enriched (brain).
DR   MalaCards; MOG; -.
DR   MIM; 159465; gene.
DR   MIM; 614250; phenotype.
DR   neXtProt; NX_Q16653; -.
DR   OpenTargets; ENSG00000204655; -.
DR   Orphanet; 2073; Narcolepsy type 1.
DR   PharmGKB; PA30905; -.
DR   VEuPathDB; HostDB:ENSG00000204655; -.
DR   eggNOG; ENOG502SQC1; Eukaryota.
DR   GeneTree; ENSGT00940000153527; -.
DR   HOGENOM; CLU_2196027_0_0_1; -.
DR   InParanoid; Q16653; -.
DR   OMA; CWKVALF; -.
DR   OrthoDB; 1057931at2759; -.
DR   PhylomeDB; Q16653; -.
DR   TreeFam; TF331083; -.
DR   PathwayCommons; Q16653; -.
DR   SignaLink; Q16653; -.
DR   BioGRID-ORCS; 4340; 224 hits in 1070 CRISPR screens.
DR   ChiTaRS; MOG; human.
DR   GeneWiki; Myelin_oligodendrocyte_glycoprotein; -.
DR   GenomeRNAi; 4340; -.
DR   Pharos; Q16653; Tbio.
DR   PRO; PR:Q16653; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q16653; protein.
DR   Bgee; ENSG00000137345; Expressed in collection of basal ganglia and 4 other tissues.
DR   ExpressionAtlas; Q16653; baseline and differential.
DR   Genevisible; Q16653; HS.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR   GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disease variant;
KW   Disulfide bond; Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Immunoglobulin domain; Membrane; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..247
FT                   /note="Myelin-oligodendrocyte glycoprotein"
FT                   /id="PRO_0000014888"
FT   TOPO_DOM        30..154
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        176..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          32..145
FT                   /note="Ig-like V-type"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         30..145
FT                   /note="Missing (in isoform 4 and isoform 12)"
FT                   /evidence="ECO:0000303|Ref.10"
FT                   /id="VSP_002539"
FT   VAR_SEQ         146..171
FT                   /note="DPFYWVSPGVLVLLAVLPVLLLQITV -> VSHSVTQDWLQWHDHGSLQPPP
FT                   PRLK (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:8915905"
FT                   /id="VSP_040344"
FT   VAR_SEQ         172..247
FT                   /note="Missing (in isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:8915905"
FT                   /id="VSP_040345"
FT   VAR_SEQ         198..247
FT                   /note="DPHFLRVPCWKITLFVIVPVLGPLVALIICYNWLHRRLAGQFLEELRNPF
FT                   -> VFHLEALSG (in isoform 11)"
FT                   /evidence="ECO:0000303|Ref.10"
FT                   /id="VSP_046856"
FT   VAR_SEQ         198..243
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002544"
FT   VAR_SEQ         198..236
FT                   /note="Missing (in isoform 2 and isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002543"
FT   VAR_SEQ         198..236
FT                   /note="DPHFLRVPCWKITLFVIVPVLGPLVALIICYNWLHRRLA -> ESFGVLGPQ
FT                   VKEPKKT (in isoform 3, isoform 7 and isoform 12)"
FT                   /evidence="ECO:0000303|Ref.10"
FT                   /id="VSP_002542"
FT   VAR_SEQ         198..203
FT                   /note="DPHFLR -> GKFRHV (in isoform 9)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002540"
FT   VAR_SEQ         204..247
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002541"
FT   VAR_SEQ         244..247
FT                   /note="RNPF -> LFHLEALSG (in isoform 5, isoform 6, isoform
FT                   7 and isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002545"
FT   VAR_SEQ         245..247
FT                   /note="NPF -> KFSSLCYKQRIKSQERETEATRGRGGLLRDHIPRGKEELESLGGG
FT                   KTPPGR (in isoform 13)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055600"
FT   VARIANT         133
FT                   /note="S -> C (in NRCLP7; dbSNP:rs387906655)"
FT                   /evidence="ECO:0000269|PubMed:21907016"
FT                   /id="VAR_066415"
FT   VARIANT         171
FT                   /note="V -> L (in dbSNP:rs2857766)"
FT                   /evidence="ECO:0000269|PubMed:14574404,
FT                   ECO:0000269|PubMed:8530032"
FT                   /id="VAR_056056"
FT   VARIANT         174
FT                   /note="I -> V (in dbSNP:rs3130253)"
FT                   /evidence="ECO:0000269|PubMed:14574404,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:7790876, ECO:0000269|PubMed:7964757,
FT                   ECO:0000269|PubMed:8530032, ECO:0000269|PubMed:8666381,
FT                   ECO:0000269|PubMed:8915905, ECO:0000269|Ref.10,
FT                   ECO:0000269|Ref.8"
FT                   /id="VAR_060215"
SQ   SEQUENCE   247 AA;  28193 MW;  846EBA5D412C080C CRC64;
     MASLSRPSLP SCLCSFLLLL LLQVSSSYAG QFRVIGPRHP IRALVGDEVE LPCRISPGKN
     ATGMEVGWYR PPFSRVVHLY RNGKDQDGDQ APEYRGRTEL LKDAIGEGKV TLRIRNVRFS
     DEGGFTCFFR DHSYQEEAAM ELKVEDPFYW VSPGVLVLLA VLPVLLLQIT VGLIFLCLQY
     RLRGKLRAEI ENLHRTFDPH FLRVPCWKIT LFVIVPVLGP LVALIICYNW LHRRLAGQFL
     EELRNPF
 
 
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