MBP_CAVPO
ID MBP_CAVPO Reviewed; 167 AA.
AC P25188;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=MBP;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6202840; DOI=10.1111/j.1471-4159.1984.tb06683.x;
RA Deibler G.E., Martenson R.E., Krutzsch H.C., Kies M.W.;
RT "Sequence of guinea pig myelin basic protein.";
RL J. Neurochem. 43:100-105(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-156.
RC STRAIN=Hartley; TISSUE=Spinal cord;
RA Kim G., Tanuma N., Matsumoto Y.;
RT "DNA vaccination using Guinea pig myelin basic protein coding region in
RT experimental autoimmune encephalomyelitis.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 45-87.
RA Shapira R., McKneally S.S., Chou F., Kibler R.F.;
RT "Encephalitogenic fragment of myelin basic protein. Amino acid sequence of
RT bovine, rabbit, guinea pig, monkey, and human fragments.";
RL J. Biol. Chem. 246:4630-4640(1971).
RN [4]
RP POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=51849; DOI=10.1016/s0021-9258(19)40905-8;
RA Deibler G.E., Martenson R.E., Kramer A.J., Kies M.W.;
RT "The contribution of phosphorylation and loss of COOH-terminal arginine to
RT the microheterogeneity of myelin basic protein.";
RL J. Biol. Chem. 250:7931-7938(1975).
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 -!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Cytoplasmic side of myelin.
CC -!- TISSUE SPECIFICITY: Found in both the central and the peripheral
CC nervous system.
CC -!- PTM: At least 5 charge isomers; C1 (the most cationic, least modified,
CC and most abundant form), C2, C3, C4 and C5 (the least cationic form);
CC are produced as a result of optional post-translational modifications
CC such as phosphorylation of serine or threonine residues, deamidation of
CC glutamine or asparagine residues, citrullination and methylation of
CC arginine residues. C1 and C2 are unphosphorylated, C3 and C4 are
CC monophosphorylated and C5 is phosphorylated at two positions
CC (PubMed:51849). {ECO:0000269|PubMed:51849}.
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}.
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DR EMBL; AF074337; AAC26130.1; -; mRNA.
DR PIR; A37246; A37246.
DR AlphaFoldDB; P25188; -.
DR BMRB; P25188; -.
DR SMR; P25188; -.
DR STRING; 10141.ENSCPOP00000007579; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR InParanoid; P25188; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0043209; C:myelin sheath; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IEA:InterPro.
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; Autoimmune encephalomyelitis; Cell membrane; Citrullination;
KW Direct protein sequencing; Membrane; Methylation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..167
FT /note="Myelin basic protein"
FT /id="PRO_0000158988"
FT REGION 45..87
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 1"
FT REGION 46..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..122
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 2"
FT REGION 136..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 89..90
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 113..114
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 14
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 25
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 31
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 35
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 49
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 69
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 102
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 106
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 129
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 144
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 156
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 162
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 167
FT /note="Citrulline"
FT /evidence="ECO:0000250"
SQ SEQUENCE 167 AA; 18213 MW; 866D31F1E5ACFEA6 CRC64;
ASQKRPSQRH GSKYLATAST MDHARHGFLP RHRDTGILDS IGRFFGSDRA APKRGSGKDS
HHAARTTHYG SLPQKSQRSQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ
KPGFGYGGRA DYKSKGFKGA HDAQGTLSKI FKLGGRDSRS GSPMARR
