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Myelin basic protein (MBP)

 MBP_PIG                 Reviewed;         171 AA.
P81558; P98189;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 1.
25-OCT-2017, entry version 85.
RecName: Full=Myelin basic protein;
Short=MBP;
Name=MBP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
PROTEIN SEQUENCE, AND METHYLATION AT ARG-107.
TISSUE=Brain;
PubMed=2578056; DOI=10.1111/j.1471-4159.1985.tb07122.x;
Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E.;
"Amino acid sequence of porcine myelin basic protein.";
J. Neurochem. 44:134-142(1985).
[2]
ERRATUM.
Kira J., Deibler G.E., Krutzsch H.C., Martenson R.E.;
J. Neurochem. 44:1663-1663(1985).
-!- 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). {ECO:0000250}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane
protein; Cytoplasmic side. Note=Cytoplasmic side of myelin.
-!- PTM: As in other animals, several charge isomers may be 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. {ECO:0000269|PubMed:2578056}.
-!- PTM: Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and
MINK1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the myelin basic protein family.
{ECO:0000305}.
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PIR; A61640; MBPGB.
UniGene; Ssc.4876; -.
DisProt; DP00663; -.
SMR; P81558; -.
STRING; 9823.ENSSSCP00000025444; -.
iPTMnet; P81558; -.
PaxDb; P81558; -.
PeptideAtlas; P81558; -.
PRIDE; P81558; -.
eggNOG; ENOG410IIUJ; Eukaryota.
eggNOG; ENOG4111PMJ; LUCA.
HOVERGEN; HBG008347; -.
InParanoid; P81558; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0071944; C:cell periphery; IBA:GO_Central.
GO; GO:0043218; C:compact myelin; IBA:GO_Central.
GO; GO:0033269; C:internode region of axon; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IDA:CAFA.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0042552; P:myelination; IBA:GO_Central.
InterPro; IPR000548; Myelin_BP.
PANTHER; PTHR11429; PTHR11429; 1.
Pfam; PF01669; Myelin_MBP; 1.
PRINTS; PR00212; MYELINMBP.
PROSITE; PS00569; MYELIN_MBP; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Citrullination; Complete proteome;
Direct protein sequencing; Membrane; Methylation; Phosphoprotein;
Reference proteome.
CHAIN 1 171 Myelin basic protein.
/FTId=PRO_0000158993.
MOD_RES 1 1 N-acetylalanine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 14 14 Phosphotyrosine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 20 20 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 25 25 Citrulline. {ECO:0000250}.
MOD_RES 31 31 Citrulline. {ECO:0000250}.
MOD_RES 35 35 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 42 42 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 48 48 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 66 66 Phosphothreonine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 68 68 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04370}.
MOD_RES 95 95 Phosphothreonine.
{ECO:0000250|UniProtKB:P02688}.
MOD_RES 98 98 Phosphothreonine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 103 103 Deamidated glutamine. {ECO:0000250}.
MOD_RES 107 107 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:2578056}.
MOD_RES 107 107 Symmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:2578056}.
MOD_RES 115 115 Phosphoserine.
{ECO:0000250|UniProtKB:P25274}.
MOD_RES 122 122 N6-acetyllysine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 130 130 Citrulline. {ECO:0000250}.
MOD_RES 148 148 Deamidated glutamine. {ECO:0000250}.
MOD_RES 160 160 Citrulline. {ECO:0000250}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 166 166 Phosphoserine; by UHMK1.
{ECO:0000250|UniProtKB:P02687}.
MOD_RES 171 171 Citrulline. {ECO:0000250}.
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


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