LOCUS       NP_002535                440 aa            linear   PRI 27-APR-2025
DEFINITION  oligodendrocyte-myelin glycoprotein precursor [Homo sapiens].
ACCESSION   NP_002535
VERSION     NP_002535.3
DBSOURCE    REFSEQ: accession NM_002544.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 440)
  AUTHORS   Park,G.H., Lee,S.J., Yim,H., Han,J.H., Kim,H.J., Sohn,Y.B., Ko,J.M.
            and Jeong,S.Y.
  TITLE     TAGLN expression is upregulated in NF1-associated malignant
            peripheral nerve sheath tumors by hypomethylation in its promoter
            and subpromoter regions
  JOURNAL   Oncol Rep 32 (4), 1347-1354 (2014)
   PUBMED   25109740
REFERENCE   2  (residues 1 to 440)
  AUTHORS   Terzi,Y.K., Oguzkan-Balci,S., Anlar,B., Erdogan-Bakar,E. and
            Ayter,S.
  TITLE     Learning disability and oligodendrocyte myelin glycoprotein (OMGP)
            gene in neurofibromatosis type 1
  JOURNAL   Turk J Pediatr 53 (1), 75-78 (2011)
   PUBMED   21534343
  REMARK    GeneRIF: The results do not support a relationship between the OMGP
            gene and the learning disability phenotype observed in
            neurofibromatosis type 1.
REFERENCE   3  (residues 1 to 440)
  AUTHORS   Martins-de-Souza,D., Gattaz,W.F., Schmitt,A., Rewerts,C.,
            Marangoni,S., Novello,J.C., Maccarrone,G., Turck,C.W. and
            Dias-Neto,E.
  TITLE     Alterations in oligodendrocyte proteins, calcium homeostasis and
            new potential markers in schizophrenia anterior temporal lobe are
            revealed by shotgun proteome analysis
  JOURNAL   J Neural Transm (Vienna) 116 (3), 275-289 (2009)
   PUBMED   19034380
  REMARK    GeneRIF: Data show that oligodendrocyte-myelin glycoprotein is
            downregulated in schizophrenia anterior temporal lobe revealed by
            shotgun proteome analysis.
REFERENCE   4  (residues 1 to 440)
  AUTHORS   Douglas,J., Cilliers,D., Coleman,K., Tatton-Brown,K., Barker,K.,
            Bernhard,B., Burn,J., Huson,S., Josifova,D., Lacombe,D., Malik,M.,
            Mansour,S., Reid,E., Cormier-Daire,V., Cole,T. and Rahman,N.
  CONSRTM   Childhood Overgrowth Collaboration
  TITLE     Mutations in RNF135, a gene within the NF1 microdeletion region,
            cause phenotypic abnormalities including overgrowth
  JOURNAL   Nat Genet 39 (8), 963-965 (2007)
   PUBMED   17632510
REFERENCE   5  (residues 1 to 440)
  AUTHORS   Zhou,X.F. and Li,H.Y.
  TITLE     Roles of glial p75NTR in axonal regeneration
  JOURNAL   J Neurosci Res 85 (8), 1601-1605 (2007)
   PUBMED   17335080
  REMARK    Review article
REFERENCE   6  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Rongnoparut,P., Allwardt,B.A., Marton,L.S. and
            Stefansson,K.
  TITLE     The oligodendrocyte-myelin glycoprotein of mouse: primary structure
            and gene structure
  JOURNAL   Genomics 17 (3), 604-610 (1993)
   PUBMED   8244377
REFERENCE   7  (residues 1 to 440)
  AUTHORS   Viskochil,D., Cawthon,R., O'Connell,P., Xu,G.F., Stevens,J.,
            Culver,M., Carey,J. and White,R.
  TITLE     The gene encoding the oligodendrocyte-myelin glycoprotein is
            embedded within the neurofibromatosis type 1 gene
  JOURNAL   Mol Cell Biol 11 (2), 906-912 (1991)
   PUBMED   1899288
REFERENCE   8  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Alexakos,M.J., Bayley,C.A., Lemons,R.S., Le Beau,M.M.
            and Stefansson,K.
  TITLE     Structure and chromosomal localization of the gene for the
            oligodendrocyte-myelin glycoprotein
  JOURNAL   J Cell Biol 111 (6 Pt 1), 2673-2679 (1990)
   PUBMED   2277079
REFERENCE   9  (residues 1 to 440)
  AUTHORS   Mikol,D.D., Gulcher,J.R. and Stefansson,K.
  TITLE     The oligodendrocyte-myelin glycoprotein belongs to a distinct
            family of proteins and contains the HNK-1 carbohydrate
  JOURNAL   J Cell Biol 110 (2), 471-479 (1990)
   PUBMED   1688857
REFERENCE   10 (residues 1 to 440)
  AUTHORS   Mikol,D.D. and Stefansson,K.
  TITLE     A phosphatidylinositol-linked peanut agglutinin-binding
            glycoprotein in central nervous system myelin and on
            oligodendrocytes
  JOURNAL   J Cell Biol 106 (4), 1273-1279 (1988)
   PUBMED   3283151
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            DA206834.1, BC018050.1 and AC134669.4.
            
            On Sep 22, 2004 this sequence version replaced NP_002535.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK222663.1, SRR1660805.165268.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA2142348
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000247271.5/ ENSP00000247271.4
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..440
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q11.2"
     Protein         1..440
                     /product="oligodendrocyte-myelin glycoprotein precursor"
                     /calculated_mol_wt=46823
     sig_peptide     1..24
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=2804
     mat_peptide     25..417
                     /product="Oligodendrocyte-myelin glycoprotein.
                     /id=PRO_0000021888"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
                     /calculated_mol_wt=44356
     Region          <37..>226
                     /region_name="LRR"
                     /note="Leucine-rich repeat (LRR) protein [Transcription];
                     COG4886"
                     /db_xref="CDD:443914"
     Region          37..56
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            45
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          56..77
                     /region_name="LRR 1"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            61
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          79..100
                     /region_name="LRR 2"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          80..100
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..124
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          101..121
                     /region_name="LRR 3"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            103
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          124..145
                     /region_name="LRR 4"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          125..147
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          147..168
                     /region_name="LRR 5"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          148..168
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Site            152
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          169..192
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          169..189
                     /region_name="LRR 6"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            176
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Site            189
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          192..213
                     /region_name="LRR 7"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            192
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          193..216
                     /region_name="leucine-rich repeat"
                     /note="leucine-rich repeat [structural motif]"
                     /db_xref="CDD:275380"
     Region          216..239
                     /region_name="LRR 8"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          229..270
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            234
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          271..292
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          293..335
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Region          336..377
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            364
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Region          378..416
                     /region_name="Ser/Thr-rich"
                     /note="propagated from UniProtKB/Swiss-Prot (P23515.2)"
     Site            389
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     Site            425
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (P23515.2)"
     CDS             1..440
                     /gene="OMG"
                     /gene_synonym="OMGP"
                     /coded_by="NM_002544.5:91..1413"
                     /db_xref="CCDS:CCDS11265.1"
                     /db_xref="GeneID:4974"
                     /db_xref="HGNC:HGNC:8135"
                     /db_xref="MIM:164345"
ORIGIN      
        1 meyqilkmsl clfillfltp gilcicplqc icterhrhvd csgrnlstlp sglqeniihl
       61 nlsynhftdl hnqltqytnl rtldisnnrl eslpahlprs lwnmsaannn iklldksdta
      121 yqwnlkyldv sknmlekvvl ikntlrslev lnlssnklwt vptnmpsklh ivdlsnnslt
      181 qilpgtlinl tnlthlylhn nkftfipdqs fdqlfqlqei tlynnrwscd hkqnityllk
      241 wmmetkahvi gtpcstqiss lkehnmyptp sgftsslftv sgmqtvdtin slsvvtqpkv
      301 tkipkqyrtk ettfgatlsk dttftstdka fvpypedtst etinsheaaa atltihlqdg
      361 mvtntsltss tkssptpmtl sitsgmpnnf sempqqsttl nlwreetttn vktplpsvan
      421 awkvnasfll llnvvvmlav
//
