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Myelin basic protein (MBP)

 MBP_RAT                 Reviewed;         195 AA.
P02688; Q505J1; Q8R4K6; Q9Z1J4; Q9Z1J5; Q9Z1J6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 158.
RecName: Full=Myelin basic protein;
Short=MBP;
Name=Mbp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
Lobell A.M., Wigzell H.;
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=2429678;
Schaich M., Budzinski R.M., Stoffel W.;
"Cloned proteolipid protein and myelin basic protein cDNA.
Transcription of the two genes during myelination.";
Biol. Chem. Hoppe-Seyler 367:825-834(1986).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=6194889; DOI=10.1016/0092-8674(83)90536-6;
Roach A., Boylan K.B., Horvath S., Prusiner S.B., Hood L.E.;
"Characterization of cloned cDNA representing rat myelin basic
protein: absence of expression in brain of shiverer mutant mice.";
Cell 34:799-806(1983).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
STRAIN=Sprague-Dawley;
PubMed=14580679; DOI=10.1016/j.bbaexp.2003.08.010;
Matheus L., Blair G.E.;
"Identification and characterisation of a cDNA encoding a 17-kDa
isoform of rat myelin basic protein.";
Biochim. Biophys. Acta 1630:47-53(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-195 (ISOFORM 4), CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND METHYLATION AT ARG-131.
TISSUE=Brain;
PubMed=4141893; DOI=10.1042/bj1410243;
Dunkley P.R., Carnegie P.R.;
"Amino acid sequence of the smaller basic protein from rat brain
myelin.";
Biochem. J. 141:243-255(1974).
[7]
PROTEIN SEQUENCE OF 11-44; 68-75; 91-129; 138-154 AND 167-177, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 46-112 (ISOFORM 4).
PubMed=4122324; DOI=10.1126/science.179.4072.478;
McFarlin D.E., Blank S.E., Kibler R.F., McKneally S.S., Shapira R.;
"Experimental allergic encephalomyelitis in the rat: response to
encephalitogenic proteins and peptides.";
Science 179:478-480(1973).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 131-195.
STRAIN=Lewis; TISSUE=Brain;
PubMed=7578863; DOI=10.3109/08916939508993341;
Malotka J., Dornmair K.;
"Alternative splicing and cDNA sequence of myelin basic protein gene
of the Lewis rat.";
Autoimmunity 20:67-68(1995).
[10]
PHOSPHORYLATION AT THR-119, AND IDENTIFICATION BY MASS SPECTROMETRY.
Lubec G., Chen W.-Q.;
Submitted (FEB-2007) to UniProtKB.
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15; THR-18; SER-20;
THR-21; THR-36 AND SER-41, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Is, with PLP, the most abundant protein component of the
myelin membrane in the CNS. Has a role in both the formation and
stabilization of this compact multilayer arrangement of bilayers.
Each splice variant and charge isomer may have a specialized
function in the assembly of an optimized, biochemically functional
myelin membrane (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- INTERACTION:
Q62976:Kcnma1; NbExp=4; IntAct=EBI-1638296, EBI-1638146;
-!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane
protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=21.5 kDa;
IsoId=P02688-1; Sequence=Displayed;
Name=2; Synonyms=18.5 kDa, MBP L;
IsoId=P02688-2; Sequence=VSP_003321;
Name=3; Synonyms=17 kDa;
IsoId=P02688-3; Sequence=VSP_003322;
Name=4; Synonyms=14 kDa, MBP S, smaller myelin basic protein;
IsoId=P02688-4; Sequence=VSP_003321, VSP_003322;
Name=5; Synonyms=17 kDa;
IsoId=P02688-5; Sequence=VSP_003321, VSP_025711;
-!- TISSUE SPECIFICITY: Found in both the central and the peripheral
nervous system.
-!- PTM: As in other animals, several charge isomers may be produced
as a result of optional post-translational modifications, such as
phosphorylation of serine or threonine residues, deamidation of
glutamine or asparagine residues, citrullination and methylation
of arginine residues. {ECO:0000269|PubMed:4141893,
ECO:0000269|Ref.10}.
-!- PTM: Arg-131 was found to be 44% monomethylated and 11%
symmetrically dimethylated.
-!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and
MINK1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the myelin basic protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ132895; CAA10804.1; -; mRNA.
EMBL; AJ132896; CAA10805.1; -; mRNA.
EMBL; AJ132897; CAA10806.1; -; mRNA.
EMBL; AJ132898; CAA10807.1; -; mRNA.
EMBL; M25889; AAA41575.1; -; mRNA.
EMBL; K00512; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF439750; AAL84189.1; -; mRNA.
EMBL; BC094522; AAH94522.1; -; mRNA.
EMBL; X72392; -; NOT_ANNOTATED_CDS; mRNA.
PIR; B24351; MBRTS.
RefSeq; NP_001020462.1; NM_001025291.1. [P02688-1]
RefSeq; NP_001020463.1; NM_001025292.1. [P02688-2]
RefSeq; NP_001020464.1; NM_001025293.1. [P02688-3]
RefSeq; NP_001020465.1; NM_001025294.1. [P02688-5]
RefSeq; NP_058722.1; NM_017026.2. [P02688-4]
UniGene; Rn.203146; -.
UniGene; Rn.63285; -.
ProteinModelPortal; P02688; -.
SMR; P02688; -.
BioGrid; 246698; 6.
IntAct; P02688; 2.
MINT; MINT-248798; -.
STRING; 10116.ENSRNOP00000022303; -.
iPTMnet; P02688; -.
PhosphoSitePlus; P02688; -.
SwissPalm; P02688; -.
PaxDb; P02688; -.
PRIDE; P02688; -.
Ensembl; ENSRNOT00000022280; ENSRNOP00000022280; ENSRNOG00000016516. [P02688-3]
Ensembl; ENSRNOT00000022303; ENSRNOP00000022303; ENSRNOG00000016516. [P02688-1]
Ensembl; ENSRNOT00000058295; ENSRNOP00000055097; ENSRNOG00000016516. [P02688-2]
Ensembl; ENSRNOT00000058296; ENSRNOP00000055098; ENSRNOG00000016516. [P02688-5]
GeneID; 24547; -.
KEGG; rno:24547; -.
CTD; 4155; -.
RGD; 3054; Mbp.
eggNOG; ENOG410IIUJ; Eukaryota.
eggNOG; ENOG4111PMJ; LUCA.
GeneTree; ENSGT00390000014772; -.
HOGENOM; HOG000293395; -.
HOVERGEN; HBG008347; -.
InParanoid; P02688; -.
KO; K17269; -.
OMA; LMASQKR; -.
PMAP-CutDB; P02688; -.
PRO; PR:P02688; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000016516; -.
ExpressionAtlas; P02688; baseline and differential.
Genevisible; P02688; RN.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0043218; C:compact myelin; IDA:RGD.
GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0019911; F:structural constituent of myelin sheath; IMP:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0042552; P:myelination; IMP:RGD.
GO; GO:0050771; P:negative regulation of axonogenesis; IMP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0046689; P:response to mercury ion; IEP:RGD.
GO; GO:0032570; P:response to progesterone; IDA:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
InterPro; IPR000548; Myelin_BP.
PANTHER; PTHR11429; PTHR11429; 1.
Pfam; PF01669; Myelin_MBP; 1.
PRINTS; PR00212; MYELINMBP.
PROSITE; PS00569; MYELIN_MBP; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Autoimmune encephalomyelitis;
Cell membrane; Citrullination; Complete proteome;
Direct protein sequencing; Membrane; Methylation; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:4141893}.
CHAIN 2 195 Myelin basic protein.
/FTId=PRO_0000158995.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:4141893}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 15 15 Phosphotyrosine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 18 18 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 26 26 Citrulline. {ECO:0000250}.
MOD_RES 32 32 Citrulline. {ECO:0000250}.
MOD_RES 36 36 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 41 41 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 44 44 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 50 50 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 92 92 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 94 94 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 104 104 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 119 119 Phosphothreonine. {ECO:0000269|Ref.10}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 127 127 Deamidated glutamine. {ECO:0000250}.
MOD_RES 131 131 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:4141893}.
MOD_RES 131 131 Symmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:4141893}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P25274}.
MOD_RES 146 146 N6-acetyllysine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 154 154 Citrulline. {ECO:0000250}.
MOD_RES 172 172 Deamidated glutamine. {ECO:0000250}.
MOD_RES 184 184 Citrulline. {ECO:0000250}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 190 190 Phosphoserine; by UHMK1.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 195 195 Citrulline. {ECO:0000250}.
VAR_SEQ 60 85 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:14580679,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2429678,
ECO:0000303|PubMed:6194889,
ECO:0000303|Ref.1}.
/FTId=VSP_003321.
VAR_SEQ 130 140 Missing (in isoform 5).
{ECO:0000303|PubMed:14580679}.
/FTId=VSP_025711.
VAR_SEQ 141 181 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2429678,
ECO:0000303|PubMed:6194889,
ECO:0000303|Ref.1}.
/FTId=VSP_003322.
CONFLICT 47 48 SG -> GS (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 192 192 M -> I (in Ref. 1; CAA10804/CAA10805/
CAA10806/CAA10807 and 3). {ECO:0000305}.
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


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