OMGP_MOUSE
ID OMGP_MOUSE Reviewed; 440 AA.
AC Q63912;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Oligodendrocyte-myelin glycoprotein;
DE Flags: Precursor;
GN Name=Omg; Synonyms=Omgp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J;
RX PubMed=8244377; DOI=10.1006/geno.1993.1379;
RA Mikol D.D., Rongnoparut P., Allwardt B.A., Marton L.S., Stefansson K.;
RT "The oligodendrocyte-myelin glycoprotein of mouse: primary structure and
RT gene structure.";
RL Genomics 17:604-610(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [3]
RP INTERACTION WITH RTN4R.
RX PubMed=12068310; DOI=10.1038/nature00867;
RA Wang K.C., Koprivica V., Kim J.A., Sivasankaran R., Guo Y., Neve R.L.,
RA He Z.;
RT "Oligodendrocyte-myelin glycoprotein is a Nogo receptor ligand that
RT inhibits neurite outgrowth.";
RL Nature 417:941-944(2002).
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:12068310}.
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; S67043; AAB28991.2; -; Genomic_DNA.
DR EMBL; BC024757; AAH24757.1; -; mRNA.
DR PIR; A47530; A47530.
DR RefSeq; NP_062282.2; NM_019409.2.
DR AlphaFoldDB; Q63912; -.
DR SMR; Q63912; -.
DR BioGRID; 201963; 2.
DR IntAct; Q63912; 2.
DR MINT; Q63912; -.
DR STRING; 10090.ENSMUSP00000132918; -.
DR GlyConnect; 2569; 16 N-Linked glycans (3 sites).
DR GlyGen; Q63912; 11 sites, 16 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q63912; -.
DR MaxQB; Q63912; -.
DR PaxDb; Q63912; -.
DR PeptideAtlas; Q63912; -.
DR PRIDE; Q63912; -.
DR ProteomicsDB; 293846; -.
DR DNASU; 18377; -.
DR GeneID; 18377; -.
DR KEGG; mmu:18377; -.
DR CTD; 4974; -.
DR MGI; MGI:106586; Omg.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q63912; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q63912; -.
DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation).
DR BioGRID-ORCS; 18377; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Omg; mouse.
DR PRO; PR:Q63912; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q63912; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043209; C:myelin sheath; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0022010; P:central nervous system myelination; ISO:MGI.
DR GO; GO:0031102; P:neuron projection regeneration; IMP:MGI.
DR GO; GO:0048683; P:regulation of collateral sprouting of intact axon in response to injury; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 2.
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; 4.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Glycoprotein; GPI-anchor;
KW Leucine-rich repeat; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..417
FT /note="Oligodendrocyte-myelin glycoprotein"
FT /id="PRO_0000021890"
FT PROPEP 418..440
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021891"
FT DOMAIN 25..55
FT /note="LRRNT"
FT REPEAT 56..78
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"
SQ SEQUENCE 440 AA; 49284 MW; 2F23047A41FC458A CRC64;
MEYQILKMSS CLFILLFLTP GILCICPLQC TCTERHRHVD CSGRNLTTLP PGLQENIIHL
NLSYNHFTDL HNQLTPYTNL RTLDISNNRL ESLPAQLPRS LWNMSAANNN IKLLDKSDTA
YQWNLKYLDV SKNMLEKVVL IKNTLRSLEV LNLSSNKLWT VPTNMPSKLH IVDLSNNSLT
QILPGTLINL TNLTHLYLHN NKFTFIPEQS FDQLLQLQEI TLHNNRWSCD HKQNITYLLK
WVMETKAHVI GTPCSKQVSS LKEQSMYPTP PGFTSSLFTM SEMQTVDTIN SLSMVTQPKV
TKTPKQYRGK ETTFGVTLSK DTTFSSTDRA VVAYPEDTPT EMTNSHEAAA ATLTIHLQDG
MSSNASLTSA TKSPPSPVTL SIARGMPNNF SEMPRQSTTL NLRREETTAN GNTRPPSAAS
AWKVNASLLL MLNAVVMLAG
