ID   MBP_XENLA               Reviewed;         176 AA.
AC   P87346; A2VDD9;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Myelin basic protein;
DE            Short=MBP;
DE   AltName: Full=Myelin A1 protein;
GN   Name=mbp;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=J; TISSUE=Brain;
RA   Nagata S., Ogino K.;
RT   "cDNA for Xenopus laevis myelin basic protein.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tail;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Is, with PLP, the most abundant protein component of the
CC       myelin membrane in the CNS. Plays 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.
CC   -!- SIMILARITY: Belongs to the myelin basic protein family. {ECO:0000305}.
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DR   EMBL; AB000736; BAA19174.1; -; mRNA.
DR   EMBL; BC129777; AAI29778.1; -; mRNA.
DR   RefSeq; NP_001083760.1; NM_001090291.1.
DR   AlphaFoldDB; P87346; -.
DR   SMR; P87346; -.
DR   BioGRID; 100427; 3.
DR   DNASU; 399102; -.
DR   GeneID; 399102; -.
DR   KEGG; xla:399102; -.
DR   CTD; 399102; -.
DR   Xenbase; XB-GENE-17333093; mbp.S.
DR   Proteomes; UP000186698; Chromosome 6S.
DR   Bgee; 399102; Expressed in brain and 18 other tissues.
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.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Citrullination; Membrane; Methylation;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..176
FT                   /note="Myelin basic protein"
FT                   /id="PRO_0000158997"
FT   REGION          1..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         25
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         33
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         97
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         103
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         108
FT                   /note="Deamidated glutamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         111
FT                   /note="Symmetric dimethylarginine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         167
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         171
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         176
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   176 AA;  19720 MW;  D30B13DA3EB29F3C CRC64;
     MASQKHSRGH GSKQMATAST YDHSRHGYGA HGRHRDSGLL DSLGRFFGGE RSVPRKGSGK
     EVHMSRSGYL SSSPQRSPYH AHGRHVDDNP VVHFFRNIVS PRTPPPSQPK RGFSRFSWGA
     ENHKPYYGGY GSRSLEHHKS SYKGYKDPHR EGHGSLSRIF KLGGQRSRSS SPMARR