MBP_PANTR
ID MBP_PANTR Reviewed; 171 AA.
AC P06906;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=MBP;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX PubMed=51459; DOI=10.1016/0024-3205(75)90506-8;
RA Westall F.C., Thompson M., Kalter S.S.;
RT "The proposed sequence of the encephalitogenic protein from chimpanzee
RT brain.";
RL Life Sci. 17:219-223(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 -!- 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.
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 PIR; A03139; MBCZB.
DR AlphaFoldDB; P06906; -.
DR BMRB; P06906; -.
DR SMR; P06906; -.
DR STRING; 9598.ENSPTRP00000056200; -.
DR iPTMnet; P06906; -.
DR PaxDb; P06906; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR InParanoid; P06906; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0071944; C:cell periphery; IBA:GO_Central.
DR GO; GO:0043218; C:compact myelin; IBA:GO_Central.
DR GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
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..171
FT /note="Myelin basic protein"
FT /id="PRO_0000158992"
FT REGION 44..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 90..91
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 114..115
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:51459"
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 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 80
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 103
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 107
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 107
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 122
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 130
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 148
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 166
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 171
FT /note="Citrulline"
FT /evidence="ECO:0000250"
SQ SEQUENCE 171 AA; 18560 MW; E9FED59DE6933293 CRC64;
ASQKRPSQRH GSKYLATAST MDHARHGFLP RHRDTGILDS IGRFFGGDRG APKRGSGKDS
HHPARTAHYG SLPQKSGHRT QDENPVVHFF KNIVTPRTPP PSQGKGRGLS LSRFSWGAEG
QRPGFGYGGR ASDYKSAHKG FKGAQDAQGT LSKIFKLGGR DSRSGSPMAR R
