MBP_RABIT
ID MBP_RABIT Reviewed; 168 AA.
AC P25274;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
DE AltName: Full=Myelin A1 protein;
DE AltName: Full=Myelin P1 protein;
GN Name=MBP;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PRELIMINARY PROTEIN SEQUENCE.
RC TISSUE=Sciatic nerve;
RX PubMed=4662101; DOI=10.1016/0003-9861(72)90377-3;
RA Brostoff S.W., Eylar E.H.;
RT "The proposed amino acid sequence of the P1 protein of rabbit sciatic nerve
RT myelin.";
RL Arch. Biochem. Biophys. 153:590-598(1972).
RN [2]
RP PROTEIN SEQUENCE OF 45-86.
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 [3]
RP PHOSPHORYLATION AT SER-7; SER-56; THR-96; SER-113 AND SER-163, AND
RP METHYLATION AT ARG-105.
RX PubMed=6185481; DOI=10.1016/s0021-9258(18)33140-5;
RA Martenson R.E., Law M.J., Deibler G.E.;
RT "Identification of multiple in vivo phosphorylation sites in rabbit myelin
RT basic protein.";
RL J. Biol. Chem. 258:930-937(1983).
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: 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:6185481}.
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; P25274; -.
DR STRING; 9986.ENSOCUP00000016532; -.
DR iPTMnet; P25274; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR InParanoid; P25274; -.
DR Proteomes; UP000001811; Unplaced.
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..168
FT /note="Myelin basic protein"
FT /id="PRO_0000158994"
FT REGION 42..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..86
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE)"
FT SITE 88..89
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 112..113
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:0000269|PubMed:6185481"
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:0000269|PubMed:6185481"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:6185481"
FT MOD_RES 101
FT /note="Deamidated glutamine; partial"
FT /evidence="ECO:0000250"
FT MOD_RES 105
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:6185481"
FT MOD_RES 105
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:6185481"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:6185481"
FT MOD_RES 120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 128
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 145
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 157
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02687"
FT MOD_RES 163
FT /note="Phosphoserine; by UHMK1"
FT /evidence="ECO:0000269|PubMed:6185481"
FT MOD_RES 168
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="S -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18217 MW; EC3C97ACD2C08EA6 CRC64;
ASQKRPSQRH GSKYLATAST MDHARHGFLP RHRDTGILDS IGRFFSSDRG APKRGSGKDH
AARTTHYGSL PQKSGHRPQD ENPVVHFFKN IVTPRTPPPS QGKGRGTVLS RFSWGAEGQK
PGFGYGGRAA DYKSAHKGLK GADAQGTLSR LFKLGGRDSR SGSPMARR
