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Myelin basic protein (MBP) (20 kDa microtubule-stabilizing protein) (Myelin A1 protein)

 MBP_BOVIN               Reviewed;         169 AA.
P02687; Q9BGM8; Q9TS63; Q9TSA6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 132.
RecName: Full=Myelin basic protein;
Short=MBP;
AltName: Full=20 kDa microtubule-stabilizing protein;
AltName: Full=Myelin A1 protein;
Name=MBP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
PROTEIN SEQUENCE.
PubMed=5096093;
Eylar E.H., Brostoff S.W., Hashim G., Caccam J., Burnett P.;
"Basic A1 protein of the myelin membrane. The complete amino acid
sequence.";
J. Biol. Chem. 246:5770-5784(1971).
[2]
SEQUENCE REVISION.
PubMed=4129204;
Brostoff S.W., Reuter W., Hichens M., Eylar E.H.;
"Specific cleavage of the A1 protein from myelin with cathepsin D.";
J. Biol. Chem. 249:559-567(1974).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-56.
Pietrowski D., Medugorac I., Foerster M.;
"A new MBP allele in Bos taurus is characterized by BseNI PCR-RFLP.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 43-87.
Shapira R., McKneally S.S., Chou F.C.-H., Kibler R.F.;
"Encephalitogenic fragment of myelin basic protein. Amino acid
sequence of bovine, rabbit, guinea pig, monkey, and human fragments.";
J. Biol. Chem. 246:4630-4640(1971).
[5]
PROTEIN SEQUENCE OF 38-58 AND 119-141.
TISSUE=Brain;
PubMed=1382581; DOI=10.1021/bi00152a022;
Pirollet F., Derancourt J., Haiech J., Job D., Margolis R.L.;
"Ca(2+)-calmodulin regulated effectors of microtubule stability in
bovine brain.";
Biochemistry 31:8849-8855(1992).
[6]
PROTEIN SEQUENCE OF 30-42; 74-89 AND 114-129.
PubMed=8530487; DOI=10.1074/jbc.270.51.30551;
Prasad K., Barouch W., Martin B.M., Greene L.E., Eisenberg E.;
"Purification of a new clathrin assembly protein from bovine brain
coated vesicles and its identification as myelin basic protein.";
J. Biol. Chem. 270:30551-30556(1995).
[7]
SYNTHESIS OF ALLERGIC ENCEPHALOMYELITIS INDUCING REGION.
PubMed=5442707; DOI=10.1126/science.168.3936.1220;
Eylar E.H., Caccam J., Jackson J.J., Westall F.C., Robinson A.B.;
"Experimental allergic encephalomyelitis: synthesis of disease-
inducing site of the basic protein.";
Science 168:1220-1223(1970).
[8]
METHYLATION AT ARG-106.
PubMed=4994464; DOI=10.1073/pnas.68.4.765;
Brostoff S.W., Eylar E.H.;
"Localization of methylated arginine in the A1 protein from myelin.";
Proc. Natl. Acad. Sci. U.S.A. 68:765-769(1971).
[9]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=57115;
Chou F.C.-H., Chou C.-H.J., Shapira R., Kibler R.F.;
"Basis of microheterogeneity of myelin basic protein.";
J. Biol. Chem. 251:2671-2679(1976).
[10]
PROTEIN SEQUENCE OF 97-104, AND PHOSPHORYLATION AT THR-97.
PubMed=1700979;
Erickson A.K., Payne D.M., Martino P.A., Rossomando A.J.,
Shabanowitz J., Weber M.J., Hunt D.F., Sturgill T.W.;
"Identification by mass spectrometry of threonine 97 in bovine myelin
basic protein as a specific phosphorylation site for mitogen-activated
protein kinase.";
J. Biol. Chem. 265:19728-19735(1990).
[11]
DEAMIDATION AT GLN-146, AND PHOSPHORYLATION AT SER-54; THR-97; SER-160
AND SER-164.
PubMed=9485392; DOI=10.1021/bi972347t;
Zand R., Li M.X., Jin X., Lubman D.;
"Determination of the sites of posttranslational modifications in the
charge isomers of bovine myelin basic protein by capillary
electrophoresis-mass spectroscopy.";
Biochemistry 37:2441-2449(1998).
[12]
DIMERIZATION.
PubMed=6155143; DOI=10.1021/bi00550a015;
Smith R.;
"Sedimentation analysis of the self-association of bovine myelin basic
protein.";
Biochemistry 19:1826-1831(1980).
[13]
ACETYLATION AT ALA-1 AND LYS-121, METHYLATION AT ARG-106, DEAMIDATION
AT GLN-102 AND GLN-120, CITRULLINATION AT ARG-23; ARG-47; ARG-96 AND
ARG-161, AND PHOSPHORYLATION AT THR-97.
PubMed=22420465; DOI=10.1021/pr201196e;
Zhang C., Walker A.K., Zand R., Moscarello M.A., Yan J.M.,
Andrews P.C.;
"Myelin basic protein undergoes a broader range of modifications in
mammals than in lower vertebrates.";
J. Proteome Res. 11:4791-4802(2012).
[14]
CITRULLINATION AT ARG-41; ARG-63; ARG-96; ARG-106; ARG-112; ARG-129;
ARG-158; ARG-161; ARG-168 AND ARG-169, AND METHYLATION AT ARG-106.
PubMed=23828821; DOI=10.1002/pmic.201300064;
Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
"Identification and Characterization of citrulline-modified brain
proteins by combining HCD and CID fragmentation.";
Proteomics 13:2682-2691(2013).
-!- 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; self-associates in the presence of lysolipid.
-!- INTERACTION:
A2A121:dclk2a (xeno); NbExp=4; IntAct=EBI-908215, EBI-9006039;
Q5S007:LRRK2 (xeno); NbExp=3; IntAct=EBI-908215, EBI-5323863;
P28482:MAPK1 (xeno); NbExp=2; IntAct=EBI-908215, EBI-959949;
-!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane
protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
-!- TISSUE SPECIFICITY: Found in both the central and the peripheral
nervous system.
-!- PTM: At least 6 charge isomers; C1 (the most cationic and least
modified form), C2, C3, C4, C5 and C6 (the least cationic form);
are 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:1700979, ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:4994464}.
-!- 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; AF226693; AAK00645.1; -; mRNA.
PIR; A92089; MBBOB.
UniGene; Bt.64741; -.
DisProt; DP00047; -.
ProteinModelPortal; P02687; -.
SMR; P02687; -.
DIP; DIP-29967N; -.
IntAct; P02687; 37.
STRING; 9913.ENSBTAP00000002984; -.
iPTMnet; P02687; -.
PaxDb; P02687; -.
PRIDE; P02687; -.
eggNOG; ENOG410IIUJ; Eukaryota.
eggNOG; ENOG4111PMJ; LUCA.
HOGENOM; HOG000293395; -.
HOVERGEN; HBG008347; -.
InParanoid; P02687; -.
PMAP-CutDB; P02687; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0043218; C:compact myelin; IBA:GO_Central.
GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
GO; GO:0043209; C:myelin sheath; IDA:CAFA.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0005543; F:phospholipid binding; IDA:CAFA.
GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0042552; P:myelination; IBA:GO_Central.
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; Autoimmune encephalomyelitis; Cell membrane;
Citrullination; Complete proteome; Direct protein sequencing;
Membrane; Methylation; Phosphoprotein; Reference proteome.
CHAIN 1 169 Myelin basic protein.
/FTId=PRO_0000158987.
REGION 43 87 Induces experimental autoimmune
encephalomyelitis (EAE) 1.
REGION 114 122 Induces experimental autoimmune
encephalomyelitis (EAE) 2.
MOD_RES 1 1 N-acetylalanine.
{ECO:0000269|PubMed:22420465}.
MOD_RES 7 7 Phosphoserine; in C5 and C6.
{ECO:0000269|PubMed:9485392}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 12 12 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 18 18 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 23 23 Citrulline; in form C8b.
{ECO:0000269|PubMed:22420465}.
MOD_RES 29 29 Citrulline. {ECO:0000250}.
MOD_RES 33 33 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 41 41 Citrulline; alternate.
{ECO:0000269|PubMed:23828821}.
MOD_RES 41 41 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 47 47 Citrulline; in form C8b.
{ECO:0000269|PubMed:22420465}.
MOD_RES 47 47 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 54 54 Phosphoserine; in C4, C5 and C6.
{ECO:0000269|PubMed:9485392}.
MOD_RES 63 63 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 65 65 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 94 94 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 96 96 Citrulline; in form C2, C3, C8a and C8b.
{ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:23828821}.
MOD_RES 97 97 Phosphothreonine; by MAPK; in C3, C4, C5
and C6. {ECO:0000269|PubMed:1700979,
ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:9485392}.
MOD_RES 102 102 Deamidated glutamine; in form C5.
{ECO:0000269|PubMed:22420465}.
MOD_RES 106 106 Citrulline; alternate.
{ECO:0000269|PubMed:23828821}.
MOD_RES 106 106 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:23828821,
ECO:0000269|PubMed:4994464}.
MOD_RES 106 106 Symmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:23828821,
ECO:0000269|PubMed:4994464}.
MOD_RES 112 112 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P25274}.
MOD_RES 120 120 Deamidated glutamine; in form C3.
{ECO:0000269|PubMed:22420465}.
MOD_RES 121 121 N6-acetyllysine.
{ECO:0000269|PubMed:22420465}.
MOD_RES 129 129 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 146 146 Deamidated glutamine; in form C2.
{ECO:0000269|PubMed:9485392}.
MOD_RES 158 158 Citrulline. {ECO:0000250}.
MOD_RES 160 160 Phosphoserine; in C4 and C6.
{ECO:0000269|PubMed:9485392}.
MOD_RES 161 161 Citrulline; in form C3.
{ECO:0000269|PubMed:22420465,
ECO:0000269|PubMed:23828821}.
MOD_RES 164 164 Phosphoserine; in form C3, C5 and C6.
{ECO:0000269|PubMed:9485392}.
MOD_RES 168 168 Citrulline.
{ECO:0000269|PubMed:23828821}.
MOD_RES 169 169 Citrulline.
{ECO:0000269|PubMed:23828821}.
SEQUENCE 169 AA; 18323 MW; 8E1157B7A1978484 CRC64;
AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH
AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ
KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR


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