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UniProtKB/Swiss-Prot entry P25188


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MBP_CAVPO
Primary accession number P25188
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 56)
Name and origin of the protein
Protein name Myelin basic protein
Synonym MBP
Gene name
Name: MBP
From
Cavia porcellus (Guinea pig) [TaxID: 10141] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Hystricognathi; Caviidae; Cavia.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
PubMed=6202840 [NCBI, ExPASy, EBI, Israel, Japan]
Deibler G.E., Martenson R.E., Krutzsch H.C., Kies M.W.;
"Sequence of guinea pig myelin basic protein.";
J. Neurochem. 43:100-105(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-156.
STRAIN=Hartley;
TISSUE=Spinal cord;
Kim G., Tanuma N., Matsumoto Y.;
"DNA vaccination using Guinea pig myelin basic protein coding region in experimental autoimmune encephalomyelitis.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 45-87.
Shapira R., McKneally S.S., Chou F., 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).
[4]
POST-TRANSLATIONAL MODIFICATIONS.
PubMed=51849 [NCBI, ExPASy, EBI, Israel, Japan]
Deibler G.E., Martenson R.E., Kramer A.J., Kies M.W.;
"The contribution of phosphorylation and loss of COOH-terminal arginine to the microheterogeneity of myelin basic protein.";
J. Biol. Chem. 250:7931-7938(1975).
Comments
  • 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).
  • SUBUNIT: Homodimer (By similarity).
  • 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 5 charge isomers; C1 (the most cationic, least modified, and most abundant form), C2, C3, C4 and C5 (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. C1 and C2 are unphosphorylated, C3 and C4 are monophosphorylated and C5 is phosphorylated at two positions.
  • SIMILARITY: Belongs to the myelin basic protein family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF074337; AAC26130.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37246; A37246.
3D structure databases
HSSP P02686; 1QCL. [HSSP ENTRY / PDB]
ModBase P25188.
Ontologies
GO
GO:0043209; Cellular component: myelin sheath (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR000548; Myelin_BP.
Graphical view of domain structure.
PANTHER PTHR11429; Myelin_BP; 1.
Pfam PF01669; Myelin_MBP; 1.
Pfam graphical view of domain structure.
PRINTS PR00212; MYELINMBP.
ProDom PD004542; Myelin_BP; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00569; MYELIN_MBP; 1.
BLOCKS P25188.
Phylogenomic databases
HOVERGEN P25188; -.
Other
ProtoNet P25188.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Autoimmune encephalomyelitis; Cell membrane; Citrullination; Direct protein sequencing; Membrane; Methylation; Phosphoprotein; Structural protein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   167  167     Myelin basic protein. PRO_0000158988
REGION   45    87  43     Induces experimental autoimmune encephalomyelitis (EAE) 1. 
REGION   114   122  9     Induces experimental autoimmune encephalomyelitis (EAE) 2. 
MOD_RES   1     1        N-acetylalanine. 
MOD_RES   7     7        Phosphoserine (By similarity). 
MOD_RES   12    12        Phosphoserine (By similarity). 
MOD_RES   25    25        Citrulline (By similarity). 
MOD_RES   31    31        Citrulline (By similarity). 
MOD_RES   35    35        Phosphothreonine (By similarity). 
MOD_RES   40    40        Phosphoserine (By similarity). 
MOD_RES   56    56        Phosphoserine (By similarity). 
MOD_RES   69    69        Phosphotyrosine (By similarity). 
MOD_RES   71    71        Phosphoserine (By similarity). 
MOD_RES   94    94        Phosphothreonine (By similarity). 
MOD_RES   97    97        Phosphothreonine (By similarity). 
MOD_RES   102   102        Deamidated glutamine (By similarity). 
MOD_RES   106   106        Symmetric dimethylarginine (By similarity). 
MOD_RES   114   114        Phosphoserine (By similarity). 
MOD_RES   129   129        Citrulline (By similarity). 
MOD_RES   144   144        Deamidated glutamine (By similarity). 
MOD_RES   156   156        Citrulline (By similarity). 
MOD_RES   158   158        Phosphoserine (By similarity). 
MOD_RES   162   162        Phosphoserine (By similarity). 
MOD_RES   167   167        Citrulline (By similarity). 
Sequence information
Length: 167 AA [This is the length of the unprocessed precursor] Molecular weight: 18213 Da [This is the MW of the unprocessed precursor] CRC64: 866D31F1E5ACFEA6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
ASQKRPSQRH GSKYLATAST MDHARHGFLP RHRDTGILDS IGRFFGSDRA APKRGSGKDS 

        70         80         90        100        110        120 
HHAARTTHYG SLPQKSQRSQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ 

       130        140        150        160 
KPGFGYGGRA DYKSKGFKGA HDAQGTLSKI FKLGGRDSRS GSPMARR 

P25188 in FASTA format

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