MBP_BOVIN
ID MBP_BOVIN Reviewed; 169 AA.
AC P02687; Q9BGM8; Q9TS63; Q9TSA6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
DE AltName: Full=20 kDa microtubule-stabilizing protein;
DE AltName: Full=Myelin A1 protein;
GN Name=MBP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=5096093; DOI=10.1016/s0021-9258(18)61872-1;
RA Eylar E.H., Brostoff S.W., Hashim G., Caccam J., Burnett P.;
RT "Basic A1 protein of the myelin membrane. The complete amino acid
RT sequence.";
RL J. Biol. Chem. 246:5770-5784(1971).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=4129204; DOI=10.1016/s0021-9258(19)43066-4;
RA Brostoff S.W., Reuter W., Hichens M., Eylar E.H.;
RT "Specific cleavage of the A1 protein from myelin with cathepsin D.";
RL J. Biol. Chem. 249:559-567(1974).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-56.
RA Pietrowski D., Medugorac I., Foerster M.;
RT "A new MBP allele in Bos taurus is characterized by BseNI PCR-RFLP.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 43-87.
RA Shapira R., McKneally S.S., Chou F.C.-H., 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 [5]
RP PROTEIN SEQUENCE OF 38-58 AND 119-141.
RC TISSUE=Brain;
RX PubMed=1382581; DOI=10.1021/bi00152a022;
RA Pirollet F., Derancourt J., Haiech J., Job D., Margolis R.L.;
RT "Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine
RT brain.";
RL Biochemistry 31:8849-8855(1992).
RN [6]
RP PROTEIN SEQUENCE OF 30-42; 74-89 AND 114-129.
RX PubMed=8530487; DOI=10.1074/jbc.270.51.30551;
RA Prasad K., Barouch W., Martin B.M., Greene L.E., Eisenberg E.;
RT "Purification of a new clathrin assembly protein from bovine brain coated
RT vesicles and its identification as myelin basic protein.";
RL J. Biol. Chem. 270:30551-30556(1995).
RN [7]
RP SYNTHESIS OF ALLERGIC ENCEPHALOMYELITIS INDUCING REGION.
RX PubMed=5442707; DOI=10.1126/science.168.3936.1220;
RA Eylar E.H., Caccam J., Jackson J.J., Westall F.C., Robinson A.B.;
RT "Experimental allergic encephalomyelitis: synthesis of disease-inducing
RT site of the basic protein.";
RL Science 168:1220-1223(1970).
RN [8]
RP METHYLATION AT ARG-106.
RX PubMed=4994464; DOI=10.1073/pnas.68.4.765;
RA Brostoff S.W., Eylar E.H.;
RT "Localization of methylated arginine in the A1 protein from myelin.";
RL Proc. Natl. Acad. Sci. U.S.A. 68:765-769(1971).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=57115; DOI=10.1016/s0021-9258(17)33540-8;
RA Chou F.C.-H., Chou C.-H.J., Shapira R., Kibler R.F.;
RT "Basis of microheterogeneity of myelin basic protein.";
RL J. Biol. Chem. 251:2671-2679(1976).
RN [10]
RP PROTEIN SEQUENCE OF 97-104, AND PHOSPHORYLATION AT THR-97.
RX PubMed=1700979; DOI=10.1016/s0021-9258(17)45433-0;
RA Erickson A.K., Payne D.M., Martino P.A., Rossomando A.J., Shabanowitz J.,
RA Weber M.J., Hunt D.F., Sturgill T.W.;
RT "Identification by mass spectrometry of threonine 97 in bovine myelin basic
RT protein as a specific phosphorylation site for mitogen-activated protein
RT kinase.";
RL J. Biol. Chem. 265:19728-19735(1990).
RN [11]
RP DEAMIDATION AT GLN-146, AND PHOSPHORYLATION AT SER-7; SER-54; THR-97;
RP SER-160 AND SER-164.
RX PubMed=9485392; DOI=10.1021/bi972347t;
RA Zand R., Li M.X., Jin X., Lubman D.;
RT "Determination of the sites of posttranslational modifications in the
RT charge isomers of bovine myelin basic protein by capillary electrophoresis-
RT mass spectroscopy.";
RL Biochemistry 37:2441-2449(1998).
RN [12]
RP DIMERIZATION.
RX PubMed=6155143; DOI=10.1021/bi00550a015;
RA Smith R.;
RT "Sedimentation analysis of the self-association of bovine myelin basic
RT protein.";
RL Biochemistry 19:1826-1831(1980).
RN [13]
RP ACETYLATION AT ALA-1 AND LYS-121, METHYLATION AT ARG-106, DEAMIDATION AT
RP GLN-102 AND GLN-120, CITRULLINATION AT ARG-23; ARG-47; ARG-96 AND ARG-161,
RP AND PHOSPHORYLATION AT THR-97.
RX PubMed=22420465; DOI=10.1021/pr201196e;
RA Zhang C., Walker A.K., Zand R., Moscarello M.A., Yan J.M., Andrews P.C.;
RT "Myelin basic protein undergoes a broader range of modifications in mammals
RT than in lower vertebrates.";
RL J. Proteome Res. 11:4791-4802(2012).
RN [14]
RP CITRULLINATION AT ARG-41; ARG-63; ARG-96; ARG-106; ARG-112; ARG-129;
RP ARG-158; ARG-161; ARG-168 AND ARG-169, AND METHYLATION AT ARG-106.
RX PubMed=23828821; DOI=10.1002/pmic.201300064;
RA Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
RT "Identification and Characterization of citrulline-modified brain proteins
RT by combining HCD and CID fragmentation.";
RL Proteomics 13:2682-2691(2013).
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; self-associates in the presence of lysolipid.
CC -!- INTERACTION:
CC P02687; A2A121: dclk2a; Xeno; NbExp=4; IntAct=EBI-908215, EBI-9006039;
CC P02687; Q5S007: LRRK2; Xeno; NbExp=3; IntAct=EBI-908215, EBI-5323863;
CC P02687; P28482: MAPK1; Xeno; NbExp=2; IntAct=EBI-908215, EBI-959949;
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: At least 6 charge isomers; C1 (the most cationic and least
CC modified form), C2, C3, C4, C5 and C6 (the least cationic form); are
CC produced as a result of optional post-translational modifications, such
CC as phosphorylation of serine or threonine residues, deamidation of
CC glutamine or asparagine residues, citrullination and methylation of
CC arginine residues. {ECO:0000269|PubMed:1700979,
CC ECO:0000269|PubMed:22420465, ECO:0000269|PubMed:23828821,
CC ECO:0000269|PubMed:4994464}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF226693; AAK00645.1; -; mRNA.
DR PIR; A92089; MBBOB.
DR AlphaFoldDB; P02687; -.
DR BMRB; P02687; -.
DR SASBDB; P02687; -.
DR SMR; P02687; -.
DR DIP; DIP-29967N; -.
DR IntAct; P02687; 37.
DR MINT; P02687; -.
DR STRING; 9913.ENSBTAP00000002984; -.
DR iPTMnet; P02687; -.
DR CPTAC; CPTAC-1475; -.
DR PaxDb; P02687; -.
DR PRIDE; P02687; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR InParanoid; P02687; -.
DR OrthoDB; 872191at2759; -.
DR Proteomes; UP000009136; 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:0043209; C:myelin sheath; IDA:CAFA.
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:0005543; F:phospholipid binding; IDA: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; DP00047; -.
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..169
FT /note="Myelin basic protein"
FT /id="PRO_0000158987"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..87
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 1"
FT REGION 114..122
FT /note="Induces experimental autoimmune encephalomyelitis
FT (EAE) 2"
FT REGION 133..169
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 89..90
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT SITE 113..114
FT /note="Cleavage; by CTSG"
FT /evidence="ECO:0000250|UniProtKB:P02686"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 7
FT /note="Phosphoserine; in C5 and C6"
FT /evidence="ECO:0000269|PubMed:9485392"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 23
FT /note="Citrulline; in form C8b"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 29
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 41
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 41
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 47
FT /note="Citrulline; in form C8b"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 47
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P04370"
FT MOD_RES 54
FT /note="Phosphoserine; in C4, C5 and C6"
FT /evidence="ECO:0000269|PubMed:9485392"
FT MOD_RES 63
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
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 94
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02688"
FT MOD_RES 96
FT /note="Citrulline; in form C2, C3, C8a and C8b"
FT /evidence="ECO:0000269|PubMed:22420465,
FT ECO:0000269|PubMed:23828821"
FT MOD_RES 97
FT /note="Phosphothreonine; by MAPK; in C3, C4, C5 and C6"
FT /evidence="ECO:0000269|PubMed:1700979,
FT ECO:0000269|PubMed:22420465, ECO:0000269|PubMed:9485392"
FT MOD_RES 102
FT /note="Deamidated glutamine; in form C5"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 106
FT /note="Citrulline; alternate"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 106
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:22420465,
FT ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:4994464"
FT MOD_RES 106
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:22420465,
FT ECO:0000269|PubMed:23828821, ECO:0000269|PubMed:4994464"
FT MOD_RES 112
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25274"
FT MOD_RES 120
FT /note="Deamidated glutamine; in form C3"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22420465"
FT MOD_RES 129
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 146
FT /note="Deamidated glutamine; in form C2"
FT /evidence="ECO:0000269|PubMed:9485392"
FT MOD_RES 158
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 160
FT /note="Phosphoserine; in C4 and C6"
FT /evidence="ECO:0000269|PubMed:9485392"
FT MOD_RES 161
FT /note="Citrulline; in form C3"
FT /evidence="ECO:0000269|PubMed:22420465,
FT ECO:0000269|PubMed:23828821"
FT MOD_RES 164
FT /note="Phosphoserine; in form C3, C5 and C6"
FT /evidence="ECO:0000269|PubMed:9485392"
FT MOD_RES 168
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 169
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:23828821"
SQ SEQUENCE 169 AA; 18323 MW; 8E1157B7A1978484 CRC64;
AAQKRPSQRS KYLASASTMD HARHGFLPRH RDTGILDSLG RFFGSDRGAP KRGSGKDGHH
AARTTHYGSL PQKAQGHRPQ DENPVVHFFK NIVTPRTPPP SQGKGRGLSL SRFSWGAEGQ
KPGFGYGGRA SDYKSAHKGL KGHDAQGTLS KIFKLGGRDS RSGSPMARR
