MBP_PIG
ID MBP_PIG Reviewed; 171 AA.
AC P81558; P98189;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=MBP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, AND METHYLATION AT ARG-107.
RC TISSUE=Brain;
RX PubMed=2578056; DOI=10.1111/j.1471-4159.1985.tb07122.x;
RA Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E.;
RT "Amino acid sequence of porcine myelin basic protein.";
RL J. Neurochem. 44:134-142(1985).
RN [2]
RP ERRATUM OF PUBMED:2578056.
RA Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E.;
RL J. Neurochem. 44:1663-1663(1985).
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. {ECO:0000269|PubMed:2578056}.
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; A61640; MBPGB.
DR AlphaFoldDB; P81558; -.
DR SMR; P81558; -.
DR STRING; 9823.ENSSSCP00000025444; -.
DR iPTMnet; P81558; -.
DR PaxDb; P81558; -.
DR PeptideAtlas; P81558; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR InParanoid; P81558; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
DR DisProt; DP00663; -.
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; Cell membrane; Citrullination; Direct protein sequencing;
KW Membrane; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..171
FT /note="Myelin basic protein"
FT /id="PRO_0000158993"
FT REGION 1..171
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 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: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 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 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 42
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 48
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 68
FT /note="Phosphotyrosine"
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:0000269|PubMed:2578056"
FT MOD_RES 107
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:2578056"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
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; 18487 MW; 287AEDF2F24028D9 CRC64;
ASQKRPSQRH GSKYLASAST MDHARHGFLP RHRDTGIDSL GRFFGADRGA PKRGSGKDGH
HAARTTHYGS LPQKAQHGRP QDENPVVHFF KNIVTPRTPP PSQGKGRGLS LSRFSWGAEG
QKPGFGYGGR APDYKPAHKG LKGAQDAQGT LSKIFKLGGR DSRSGSPMAR R
