MBP_RAT
ID MBP_RAT Reviewed; 195 AA.
AC P02688; Q505J1; Q8R4K6; Q9Z1J4; Q9Z1J5; Q9Z1J6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=Mbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RA Lobell A.M., Wigzell H.;
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=2429678; DOI=10.1515/bchm3.1986.367.2.825;
RA Schaich M., Budzinski R.M., Stoffel W.;
RT "Cloned proteolipid protein and myelin basic protein cDNA. Transcription of
RT the two genes during myelination.";
RL Biol. Chem. Hoppe-Seyler 367:825-834(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=6194889; DOI=10.1016/0092-8674(83)90536-6;
RA Roach A., Boylan K.B., Horvath S., Prusiner S.B., Hood L.E.;
RT "Characterization of cloned cDNA representing rat myelin basic protein:
RT absence of expression in brain of shiverer mutant mice.";
RL Cell 34:799-806(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC STRAIN=Sprague-Dawley;
RX PubMed=14580679; DOI=10.1016/j.bbaexp.2003.08.010;
RA Matheus L., Blair G.E.;
RT "Identification and characterisation of a cDNA encoding a 17-kDa isoform of
RT rat myelin basic protein.";
RL Biochim. Biophys. Acta 1630:47-53(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 2-195 (ISOFORM 4), CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND METHYLATION AT ARG-131.
RC TISSUE=Brain;
RX PubMed=4141893; DOI=10.1042/bj1410243;
RA Dunkley P.R., Carnegie P.R.;
RT "Amino acid sequence of the smaller basic protein from rat brain myelin.";
RL Biochem. J. 141:243-255(1974).
RN [7]
RP PROTEIN SEQUENCE OF 11-44; 68-75; 91-129; 138-154 AND 167-177, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 46-112 (ISOFORM 4).
RX PubMed=4122324; DOI=10.1126/science.179.4072.478;
RA McFarlin D.E., Blank S.E., Kibler R.F., McKneally S.S., Shapira R.;
RT "Experimental allergic encephalomyelitis in the rat: response to
RT encephalitogenic proteins and peptides.";
RL Science 179:478-480(1973).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-195.
RC STRAIN=Lewis; TISSUE=Brain;
RX PubMed=7578863; DOI=10.3109/08916939508993341;
RA Malotka J., Dornmair K.;
RT "Alternative splicing and cDNA sequence of myelin basic protein gene of the
RT Lewis rat.";
RL Autoimmunity 20:67-68(1995).
RN [10]
RP PHOSPHORYLATION AT THR-119, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15; THR-18; SER-20; THR-21;
RP THR-36 AND SER-41, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Is, with PLP, the most abundant protein component of the
CC myelin membrane in the CNS. Has a role in both the formation and
CC stabilization of this compact multilayer arrangement of bilayers. Each
CC splice variant and charge isomer may have a specialized function in the
CC assembly of an optimized, biochemically functional myelin membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P02688; Q62976: Kcnma1; NbExp=4; IntAct=EBI-1638296, EBI-1638146;
CC -!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Cytoplasmic side of myelin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=21.5 kDa;
CC IsoId=P02688-1; Sequence=Displayed;
CC Name=2; Synonyms=18.5 kDa, MBP L;
CC IsoId=P02688-2; Sequence=VSP_003321;
CC Name=3; Synonyms=17 kDa;
CC IsoId=P02688-3; Sequence=VSP_003322;
CC Name=4; Synonyms=14 kDa, MBP S, smaller myelin basic protein;
CC IsoId=P02688-4; Sequence=VSP_003321, VSP_003322;
CC Name=5; Synonyms=17 kDa;
CC IsoId=P02688-5; Sequence=VSP_003321, VSP_025711;
CC -!- TISSUE SPECIFICITY: Found in both the central and the peripheral
CC nervous system.
CC -!- PTM: As in other animals, several charge isomers may be produced as a
CC result of optional post-translational modifications, such as
CC phosphorylation of serine or threonine residues, deamidation of
CC glutamine or asparagine residues, citrullination and methylation of
CC arginine residues. {ECO:0000269|PubMed:4141893, ECO:0000269|Ref.10}.
CC -!- PTM: Arg-131 was found to be 44% monomethylated and 11% symmetrically
CC dimethylated.
CC -!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1.
CC {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved in B cell lysosomes by cathepsin CTSG
CC which degrades the major immunogenic MBP epitope and prevents the
CC activation of MBP-specific autoreactive T cells.
CC {ECO:0000250|UniProtKB:P02686}.
CC -!- SIMILARITY: Belongs to the myelin basic protein family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ132895; CAA10804.1; -; mRNA.
DR EMBL; AJ132896; CAA10805.1; -; mRNA.
DR EMBL; AJ132897; CAA10806.1; -; mRNA.
DR EMBL; AJ132898; CAA10807.1; -; mRNA.
DR EMBL; M25889; AAA41575.1; -; mRNA.
DR EMBL; K00512; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF439750; AAL84189.1; -; mRNA.
DR EMBL; BC094522; AAH94522.1; -; mRNA.
DR EMBL; X72392; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B24351; MBRTS.
DR RefSeq; NP_001020462.1; NM_001025291.1. [P02688-1]
DR RefSeq; NP_001020463.1; NM_001025292.1. [P02688-2]
DR RefSeq; NP_001020464.1; NM_001025293.1. [P02688-3]
DR RefSeq; NP_001020465.1; NM_001025294.1. [P02688-5]
DR RefSeq; NP_058722.1; NM_017026.2. [P02688-4]
DR AlphaFoldDB; P02688; -.
DR BMRB; P02688; -.
DR SMR; P02688; -.
DR BioGRID; 246698; 8.
DR IntAct; P02688; 3.
DR MINT; P02688; -.
DR STRING; 10116.ENSRNOP00000022303; -.
DR CarbonylDB; P02688; -.
DR iPTMnet; P02688; -.
DR PhosphoSitePlus; P02688; -.
DR SwissPalm; P02688; -.
DR PaxDb; P02688; -.
DR PRIDE; P02688; -.
DR DNASU; 24547; -.
DR GeneID; 24547; -.
DR KEGG; rno:24547; -.
DR CTD; 4155; -.
DR RGD; 3054; Mbp.
DR VEuPathDB; HostDB:ENSRNOG00000016516; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR HOGENOM; CLU_102586_0_0_1; -.
DR InParanoid; P02688; -.
DR OMA; TKIFKMG; -.
DR OrthoDB; 872191at2759; -.
DR PRO; PR:P02688; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000016516; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P02688; baseline and differential.
DR Genevisible; P02688; RN.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0043218; C:compact myelin; IDA:RGD.
DR GO; GO:0033269; C:internode region of axon; ISO:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035633; P:maintenance of blood-brain barrier; ISO:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0061024; P:membrane organization; ISO:RGD.
DR GO; GO:0042552; P:myelination; IMP:RGD.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IMP:RGD.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:RGD.
DR GO; GO:2000343; P:positive regulation of chemokine (C-X-C motif) ligand 2 production; ISO:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:1904685; P:positive regulation of metalloendopeptidase activity; ISO:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0046689; P:response to mercury ion; IEP:RGD.
DR GO; GO:0032570; P:response to progesterone; IDA:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR InterPro; IPR000548; Myelin_BP.
DR PANTHER; PTHR11429; PTHR11429; 1.
DR Pfam; PF01669; Myelin_MBP; 1.
DR PRINTS; PR00212; MYELINMBP.
DR PROSITE; PS00569; MYELIN_MBP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Autoimmune encephalomyelitis;
KW Cell membrane; Citrullination; Direct protein sequencing; Membrane;
KW Methylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4141893"
FT CHAIN 2..195
FT /note="Myelin basic protein"
FT /id="PRO_0000158995"
FT REGION 45..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 114..115
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 138..139
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:4141893"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 15
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 26
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 32
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 44
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 50
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 92
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 94
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 127
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:4141893"
FT MOD_RES 131
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:4141893"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 154
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 172
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 190
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 195
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT VAR_SEQ 60..85
FT /note="Missing (in isoform 2, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14580679,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:2429678,
FT ECO:0000303|PubMed:6194889, ECO:0000303|Ref.1"
FT /id="VSP_003321"
FT VAR_SEQ 130..140
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14580679"
FT /id="VSP_025711"
FT VAR_SEQ 141..181
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2429678, ECO:0000303|PubMed:6194889,
FT ECO:0000303|Ref.1"
FT /id="VSP_003322"
FT CONFLICT 47..48
FT /note="SG -> GS (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="M -> I (in Ref. 1; CAA10804/CAA10805/CAA10806/
FT CAA10807 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21502 MW; F1A43933EC9D4CFF CRC64;
MASQKRPSQR HGSKYLATAS TMDHARHGFL PRHRDTGILD SIGRFFSGDR GAPKRGSGKV
PWLKQSRSPL PSHARSRPGL CHMYKDSHTR TTHYGSLPQK SQRTQDENPV VHFFKNIVTP
RTPPPSQGKG RGLSLSRFSW GAEGQKPGFG YGGRASDYKS AHKGFKGAYD AQGTLSKIFK
LGGRDSRSGS PMARR
