MBP_HORSE
ID MBP_HORSE Reviewed; 172 AA.
AC P83487;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=MBP;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000305};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION AT
RP ARG-108.
RC TISSUE=Spinal cord;
RX PubMed=12176067; DOI=10.1016/s0003-9861(02)00340-5;
RA Wood D.D., She Y.M., Freer A.D., Harauz G., Moscarello M.A.;
RT "Primary structure of equine myelin basic protein by mass spectrometry.";
RL Arch. Biochem. Biophys. 405:137-146(2002).
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|UniProtKB:P02687}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P02687}.
CC -!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein;
CC Cytoplasmic side. Note=Cytoplasmic side of myelin.
CC -!- PTM: At least 5 charge isomers; C1 (the most cationic and least
CC modified form), C2, C3, C4 and C8; are produced as a result of optional
CC post-translational modifications, such as phosphorylation and
CC methylation. {ECO:0000269|PubMed:12176067}.
CC -!- PTM: The C-terminal arginine is partially cleaved in C2. One or both of
CC the C-terminal arginines are partially cleaved in C3. The two C-
CC terminal arginines are partially cleaved in C4 (PubMed:12176067).
CC {ECO:0000269|PubMed:12176067}.
CC -!- PTM: Arg-108 was found to be 25% monomethylated and 4% symmetrically
CC dimethylated. {ECO:0000269|PubMed:12176067}.
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 AlphaFoldDB; P83487; -.
DR SMR; P83487; -.
DR iPTMnet; P83487; -.
DR PaxDb; P83487; -.
DR InParanoid; P83487; -.
DR Proteomes; UP000002281; 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.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Direct protein sequencing; Membrane;
KW Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..172
FT /note="Myelin basic protein"
FT /id="PRO_0000158989"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 91..92
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 115..116
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 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 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 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:12176067"
FT MOD_RES 108
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:12176067"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 167
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000250|UniProtKB:P02687"
SQ SEQUENCE 172 AA; 18725 MW; C60CCDECD0833509 CRC64;
ASQKRPSQRH GSKYLASAST MDHARHGFLP RHRDTGILDS LGRFFGGDRG VPKRGSGKDG
HHAARTTHYG SLPQKSRDGR PQDENPVVHF FKINVTPRTP PPSQGKGRGL SLSRFSWGAE
GQKPGFGYGA RASDYKSTHK GLKGVHDAQG TLSRIFKLGG RDSRSGSPMA RR
