LOCUS       NP_001020462             195 aa            linear   ROD 24-JUN-2024
DEFINITION  myelin basic protein isoform 1 [Rattus norvegicus].
ACCESSION   NP_001020462
VERSION     NP_001020462.1
DBSOURCE    REFSEQ: accession NM_001025291.1
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 195)
  AUTHORS   Zhang,Z., Wang,J., Song,Z., Wang,Y., Cheng,Z., Guo,Q., Wang,E.,
            Jian,Y. and Wu,L.
  TITLE     Downregulation of microRNA-199a-5p alleviated lidocaine-induced
            sensory dysfunction and spinal cord myelin lesions in a rat model
  JOURNAL   Toxicol Lett 336, 1-10 (2021)
   PUBMED   33166664
REFERENCE   2  (residues 1 to 195)
  AUTHORS   Darling,J.S. and Daniel,J.M.
  TITLE     Pubertal hormones mediate sex differences in levels of myelin basic
            protein in the orbitofrontal cortex of adult rats
  JOURNAL   Neuroscience 406, 487-495 (2019)
   PUBMED   30926549
  REMARK    GeneRIF: Gonadectomy prior to puberty onset resulted in a
            significant reduction of myelin basic protein levels in the
            orbitofrontal cortex in females but not males.
REFERENCE   3  (residues 1 to 195)
  AUTHORS   Oberoi,R., Chu,T., Mellen,N., Jagadapillai,R., Ouyang,H.,
            Devlin,L.A. and Cai,J.
  TITLE     Diverse changes in myelin protein expression in rat brain after
            perinatal methadone exposure
  JOURNAL   Acta Neurobiol Exp (Wars) 79 (4), 367-373 (2019)
   PUBMED   31885393
  REMARK    GeneRIF: All pups with exposure to methadone demonstrated decreased
            expression of MBP in the cerebral cortex and hippocampus.In the
            cerebellum, PLP expression was downregulated without apparent
            alteration of CNP and MBP expression. PLP and MBP expression, but
            not CNP expression, were significantly inhibited in the brainstem.
REFERENCE   4  (residues 1 to 195)
  AUTHORS   Chin,J.P., Chen,C.M., Lee,T.H., Chou,C.W. and Lu,C.Y.
  TITLE     Angiostrongylus Cantonensis-Conditioned Culture Medium Induces
            Myelin Basic Protein Alterations via Erk1/2 and NF-kappaB
            Activation in Rat RSC96 Schwann Cells
  JOURNAL   Chin J Physiol 61 (3), 137-143 (2018)
   PUBMED   29742816
  REMARK    GeneRIF: Angiostrongylus cantonensis-conditioned culture medium
            induced suppression of the Erk1/2-NF-kappaB signaling pathway
            leading to reduced MBP production in RSC96 Schwann cells.
REFERENCE   5  (residues 1 to 195)
  AUTHORS   Herbert,A.L., Fu,M.M., Drerup,C.M., Gray,R.S., Harty,B.L.,
            Ackerman,S.D., O'Reilly-Pol,T., Johnson,S.L., Nechiporuk,A.V.,
            Barres,B.A. and Monk,K.R.
  TITLE     Dynein/dynactin is necessary for anterograde transport of Mbp mRNA
            in oligodendrocytes and for myelination in vivo
  JOURNAL   Proc Natl Acad Sci U S A 114 (43), E9153-E9162 (2017)
   PUBMED   29073112
  REMARK    GeneRIF: A role for the retrograde dynein/dynactin motor complex in
            anterograde mbp mRNA transport.
REFERENCE   6  (residues 1 to 195)
  AUTHORS   Griffiths,I.R., Scott,I., McCulloch,M.C., Barrie,J.A., McPhilemy,K.
            and Cattanach,B.M.
  TITLE     Rumpshaker mouse: a new X-linked mutation affecting myelination:
            evidence for a defect in PLP expression
  JOURNAL   J Neurocytol 19 (2), 273-283 (1990)
   PUBMED   1694232
REFERENCE   7  (residues 1 to 195)
  AUTHORS   Boylan,K.B., Takahashi,N., Paty,D.W., Sadovnick,A.D., Diamond,M.,
            Hood,L.E. and Prusiner,S.B.
  TITLE     DNA length polymorphism 5' to the myelin basic protein gene is
            associated with multiple sclerosis
  JOURNAL   Ann Neurol 27 (3), 291-297 (1990)
   PUBMED   1691612
REFERENCE   8  (residues 1 to 195)
  AUTHORS   Brunner,C., Lassmann,H., Waehneldt,T.V., Matthieu,J.M. and
            Linington,C.
  TITLE     Differential ultrastructural localization of myelin basic protein,
            myelin/oligodendroglial glycoprotein, and 2',3'-cyclic nucleotide
            3'-phosphodiesterase in the CNS of adult rats
  JOURNAL   J Neurochem 52 (1), 296-304 (1989)
   PUBMED   2462020
REFERENCE   9  (residues 1 to 195)
  AUTHORS   Schaich,M., Budzinski,R.M. and Stoffel,W.
  TITLE     Cloned proteolipid protein and myelin basic protein cDNA.
            Transcription of the two genes during myelination
  JOURNAL   Biol Chem Hoppe Seyler 367 (8), 825-834 (1986)
   PUBMED   2429678
REFERENCE   10 (residues 1 to 195)
  AUTHORS   McFarlin,D.E., Blank,S.E., Kibler,R.F., McKneally,S. and Shapira,R.
  TITLE     Experimental allergic encephalomyelitis in the rat: response to
            encephalitogenic proteins and peptides
  JOURNAL   Science 179 (4072), 478-480 (1973)
   PUBMED   4122324
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CB586909.1, AJ132898.1,
            AF439750.1, M25889.1 and AI145512.1.
            
            Summary: The protein encoded by the classic Mbp gene is a major
            constituent of the myelin sheath of oligodendrocytes and Schwann
            cells in the nervous system. However, Mbp-related transcripts are
            also present in the bone marrow and the immune system. These mRNAs
            arise from the long Mbp gene (otherwise called 'Golli-Mbp') that
            contains 3 additional exons located upstream of the classic Mbp
            exons. Alternative splicing from the Golli and the Mbp
            transcription start sites gives rise to 2 sets of Mbp-related
            transcripts and gene products. The Golli mRNAs contain 3 exons
            unique to Golli-Mbp, spliced in-frame to 1 or more Mbp exons. They
            encode hybrid proteins that have N-terminal Golli aa sequence
            linked to Mbp aa sequence. The second family of transcripts contain
            only Mbp exons and produce the well characterized myelin basic
            proteins. This complex gene structure is conserved among species
            suggesting that the Mbp transcription unit is an integral part of
            the Golli transcription unit and that this arrangement is important
            for the function and/or regulation of these genes. Mutation of the
            Mbp gene is associated with the 'shiverer' and 'myelin deficient'
            phenotypes in mouse. [provided by RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) encodes the longest of the
            classic Mbp isoforms (1).
            
            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 :: JX131663.1, FQ101754.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760384, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..195
                     /organism="Rattus norvegicus"
                     /strain="LEW"
                     /db_xref="taxon:10116"
                     /chromosome="18"
                     /map="18q12.3"
     Protein         1..195
                     /product="myelin basic protein isoform 1"
                     /note="myelin basic protein S; myelin basic protein
                     Golli-mbp; Golli-Mbp; MBP S"
                     /calculated_mol_wt=21371
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000269|PubMed:4141893; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            8
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            13
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            15
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Region          16..194
                     /region_name="Myelin_MBP"
                     /note="Myelin basic protein; pfam01669"
                     /db_xref="CDD:460288"
     Site            18
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            21
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            36
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            41
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:22673903; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            44
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Region          45..79
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02688.3)"
     Site            50
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            57
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            92
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            94
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            101
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            104
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P04370; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            114..115
                     /site_type="cleavage"
                     /note="Cleavage, by CTSG.
                     /evidence=ECO:0000250|UniProtKB:P02686; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Region          117..139
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P02688.3)"
     Site            119
                     /site_type="phosphorylation"
                     /note="Phosphothreonine. /evidence=ECO:0000269|Ref.10;
                     propagated from UniProtKB/Swiss-Prot (P02688.3)"
     Site            122
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            131
                     /site_type="methylation"
                     /note="Omega-N-methylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:4141893; Symmetric
                     dimethylarginine, alternate.
                     /evidence=ECO:0000269|PubMed:4141893; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            138..139
                     /site_type="cleavage"
                     /note="Cleavage, by CTSG.
                     /evidence=ECO:0000250|UniProtKB:P02686; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            139
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P25274; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            146
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     Site            190
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by UHMK1.
                     /evidence=ECO:0000250|UniProtKB:P02687; propagated from
                     UniProtKB/Swiss-Prot (P02688.3)"
     CDS             1..195
                     /gene="Mbp"
                     /gene_synonym="Mbps"
                     /coded_by="NM_001025291.1:78..665"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:24547"
                     /db_xref="RGD:3054"
ORIGIN      
        1 masqkrpsqr hgskylatas tmdharhgfl prhrdtgild sigrffsgdr gapkrgsgkv
       61 pwlkqsrspl psharsrpgl chmykdshtr tthygslpqk sqrtqdenpv vhffknivtp
      121 rtpppsqgkg rglslsrfsw gaegqkpgfg yggrasdyks ahkgfkgayd aqgtlskifk
      181 lggrdsrsgs pmarr
//
