OMGP_HUMAN
ID OMGP_HUMAN Reviewed; 440 AA.
AC P23515; E1P659;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Oligodendrocyte-myelin glycoprotein;
DE Flags: Precursor;
GN Name=OMG; Synonyms=OMGP;
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].
RX PubMed=1899288; DOI=10.1128/mcb.11.2.906-912.1991;
RA Viskochil D., Cawthon R.M., O'Connell P., Xu G., Stevens J., Culver M.,
RA Carey J., White R.;
RT "The gene encoding the oligodendrocyte-myelin glycoprotein is embedded
RT within the neurofibromatosis type 1 gene.";
RL Mol. Cell. Biol. 11:906-912(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1688857; DOI=10.1083/jcb.110.2.471;
RA Mikol D.D., Gulcher J., Stefansson K.;
RT "The oligodendrocyte-myelin glycoprotein belongs to a distinct family of
RT proteins and contains the HNK-1 carbohydrate.";
RL J. Cell Biol. 110:471-479(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2277079; DOI=10.1083/jcb.111.6.2673;
RA Mikol D.D., Alexakos M.J., Bayley C.A., Lemons R.S., le Beau M.M.,
RA Stefansson K.;
RT "Structure and chromosomal localization of the gene for the
RT oligodendrocyte-myelin glycoprotein.";
RL J. Cell Biol. 111:2673-2679(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP PROTEIN SEQUENCE OF 25-52.
RX PubMed=3283151; DOI=10.1083/jcb.106.4.1273;
RA Mikol D.D., Stefansson K.;
RT "A phosphatidylinositol-linked peanut agglutinin-binding glycoprotein in
RT central nervous system myelin and on oligodendrocytes.";
RL J. Cell Biol. 106:1273-1279(1988).
RN [7]
RP INTERACTION WITH RTN4R.
RX PubMed=19052207; DOI=10.1523/jneurosci.3828-08.2008;
RA Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
RA Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
RA Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
RA Strittmatter S.M.;
RT "Genetic variants of Nogo-66 receptor with possible association to
RT schizophrenia block myelin inhibition of axon growth.";
RL J. Neurosci. 28:13161-13172(2008).
CC -!- FUNCTION: Cell adhesion molecule contributing to the interactive
CC process required for myelination in the central nervous system.
CC -!- SUBUNIT: Binds to RTN4R. {ECO:0000269|PubMed:19052207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Oligodendrocytes and myelin of the central nervous
CC system.
CC -!- PTM: O-glycosylated in its Ser/Thr-rich repeat domain. {ECO:0000305}.
CC -!- CAUTION: Do not confuse oligodendrocyte-myelin glycoprotein (OMG) with
CC myelin-oligodendrocyte glycoprotein (MOG). {ECO:0000305}.
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DR EMBL; M63623; AAA59970.1; ALT_SEQ; mRNA.
DR EMBL; X57436; CAA40684.1; -; Genomic_DNA.
DR EMBL; X51694; CAA35991.1; ALT_SEQ; mRNA.
DR EMBL; CH471147; EAW80279.1; -; Genomic_DNA.
DR EMBL; CH471147; EAW80280.1; -; Genomic_DNA.
DR EMBL; BC018050; AAH18050.1; -; mRNA.
DR CCDS; CCDS11265.1; -.
DR PIR; A36688; A39613.
DR RefSeq; NP_002535.3; NM_002544.4.
DR AlphaFoldDB; P23515; -.
DR SMR; P23515; -.
DR BioGRID; 111022; 4.
DR IntAct; P23515; 3.
DR MINT; P23515; -.
DR STRING; 9606.ENSP00000247271; -.
DR GlyGen; P23515; 12 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P23515; -.
DR PhosphoSitePlus; P23515; -.
DR BioMuta; OMG; -.
DR DMDM; 129122; -.
DR MassIVE; P23515; -.
DR MaxQB; P23515; -.
DR PaxDb; P23515; -.
DR PeptideAtlas; P23515; -.
DR PRIDE; P23515; -.
DR ProteomicsDB; 54125; -.
DR TopDownProteomics; P23515; -.
DR Antibodypedia; 2187; 298 antibodies from 40 providers.
DR DNASU; 4974; -.
DR Ensembl; ENST00000247271.5; ENSP00000247271.4; ENSG00000126861.5.
DR GeneID; 4974; -.
DR KEGG; hsa:4974; -.
DR MANE-Select; ENST00000247271.5; ENSP00000247271.4; NM_002544.5; NP_002535.3.
DR UCSC; uc002hgj.4; human.
DR CTD; 4974; -.
DR DisGeNET; 4974; -.
DR GeneCards; OMG; -.
DR HGNC; HGNC:8135; OMG.
DR HPA; ENSG00000126861; Group enriched (brain, choroid plexus).
DR MIM; 164345; gene.
DR neXtProt; NX_P23515; -.
DR OpenTargets; ENSG00000126861; -.
DR PharmGKB; PA31922; -.
DR VEuPathDB; HostDB:ENSG00000126861; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000160802; -.
DR HOGENOM; CLU_050697_0_0_1; -.
DR InParanoid; P23515; -.
DR OMA; TLHNNRW; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; P23515; -.
DR TreeFam; TF335688; -.
DR PathwayCommons; P23515; -.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR SignaLink; P23515; -.
DR SIGNOR; P23515; -.
DR BioGRID-ORCS; 4974; 13 hits in 1060 CRISPR screens.
DR GeneWiki; OMG_(gene); -.
DR GenomeRNAi; 4974; -.
DR Pharos; P23515; Tbio.
DR PRO; PR:P23515; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P23515; protein.
DR Bgee; ENSG00000126861; Expressed in olfactory segment of nasal mucosa and 153 other tissues.
DR Genevisible; P23515; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0031102; P:neuron projection regeneration; IBA:GO_Central.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Leucine-rich repeat; Lipoprotein; Membrane; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:3283151"
FT CHAIN 25..417
FT /note="Oligodendrocyte-myelin glycoprotein"
FT /id="PRO_0000021888"
FT PROPEP 418..440
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021889"
FT DOMAIN 25..55
FT /note="LRRNT"
FT REPEAT 56..77
FT /note="LRR 1"
FT REPEAT 79..100
FT /note="LRR 2"
FT REPEAT 101..121
FT /note="LRR 3"
FT REPEAT 124..145
FT /note="LRR 4"
FT REPEAT 147..168
FT /note="LRR 5"
FT REPEAT 169..189
FT /note="LRR 6"
FT REPEAT 192..213
FT /note="LRR 7"
FT REPEAT 216..239
FT /note="LRR 8"
FT REPEAT 229..270
FT /note="Ser/Thr-rich"
FT REPEAT 271..292
FT /note="Ser/Thr-rich"
FT REPEAT 293..335
FT /note="Ser/Thr-rich"
FT REPEAT 336..377
FT /note="Ser/Thr-rich"
FT REPEAT 378..416
FT /note="Ser/Thr-rich"
FT LIPID 417
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 21
FT /note="G -> D (in dbSNP:rs11080149)"
FT /id="VAR_051252"
FT VARIANT 435
FT /note="V -> A (in dbSNP:rs16972169)"
FT /id="VAR_051253"
SQ SEQUENCE 440 AA; 49608 MW; 762FD0E8905EA050 CRC64;
MEYQILKMSL CLFILLFLTP GILCICPLQC ICTERHRHVD CSGRNLSTLP SGLQENIIHL
NLSYNHFTDL HNQLTQYTNL RTLDISNNRL ESLPAHLPRS LWNMSAANNN IKLLDKSDTA
YQWNLKYLDV SKNMLEKVVL IKNTLRSLEV LNLSSNKLWT VPTNMPSKLH IVDLSNNSLT
QILPGTLINL TNLTHLYLHN NKFTFIPDQS FDQLFQLQEI TLYNNRWSCD HKQNITYLLK
WMMETKAHVI GTPCSTQISS LKEHNMYPTP SGFTSSLFTV SGMQTVDTIN SLSVVTQPKV
TKIPKQYRTK ETTFGATLSK DTTFTSTDKA FVPYPEDTST ETINSHEAAA ATLTIHLQDG
MVTNTSLTSS TKSSPTPMTL SITSGMPNNF SEMPQQSTTL NLWREETTTN VKTPLPSVAN
AWKVNASFLL LLNVVVMLAV
