MBP_CHICK
ID MBP_CHICK Reviewed; 174 AA.
AC P15720;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Myelin basic protein;
DE Short=MBP;
GN Name=MBP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=White leghorn; TISSUE=Optic lobe;
RX PubMed=2475444; DOI=10.1002/glia.440020405;
RA Zopf D., Sonntag H., Betz H., Gundelfinger E.D.;
RT "Developmental accumulation and heterogeneity of myelin basic protein
RT transcripts in the chick visual system.";
RL Glia 2:241-249(1989).
RN [2]
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT
RP SER-8; SER-19; SER-34; SER-65; SER-74; THR-97; SER-114; SER-142; SER-165
RP AND SER-169, METHYLATION AT ARG-106, DEAMIDATION AT GLN-4; GLN-72; ASN-91;
RP GLN-102 AND GLN-147, CITRULLINATION AT ARG-25; ARG-42 AND ARG-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18618245; DOI=10.1007/s11064-008-9788-4;
RA Kim J., Zhang R., Strittmatter E.F., Smith R.D., Zand R.;
RT "Post-translational modifications of chicken myelin basic protein charge
RT components.";
RL Neurochem. Res. 34:360-372(2009).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P15720-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15720-2; Sequence=VSP_003323;
CC -!- DEVELOPMENTAL STAGE: In the optic lobe, first detected at embryonic day
CC 14. Expression strongly increases between embryonic days 16 and 18,
CC reaches a maximum at postnatal day 1, and then declines again to the
CC adult level.
CC -!- PTM: Several charge isomers are produced as a result of optional post-
CC translational modifications, such as phosphorylation of serine or
CC threonine residues, deamidation of glutamine or asparagine residues,
CC citrullination and methylation of arginine residues. Chicken MBP
CC contains 4 charge components denoted as C1, C2, C3 and C8. C1 lacks any
CC phosphorylation sites, whereas C2 and C3 contain respectively 10 and 8
CC phosphorylation sites and arginine residues modified to citrulline. All
CC three charge components contain deamidated glutamines and asparagine,
CC and a methylated arginine. {ECO:0000269|PubMed:18618245}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
CC -!- SIMILARITY: Belongs to the myelin basic protein family. {ECO:0000305}.
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DR EMBL; X17103; CAA34959.1; -; mRNA.
DR PIR; S08535; S08535.
DR RefSeq; NP_990611.1; NM_205280.1. [P15720-1]
DR AlphaFoldDB; P15720; -.
DR SMR; P15720; -.
DR STRING; 9031.ENSGALP00000022148; -.
DR iPTMnet; P15720; -.
DR PaxDb; P15720; -.
DR Ensembl; ENSGALT00000022187; ENSGALP00000022148; ENSGALG00000013640. [P15720-2]
DR Ensembl; ENSGALT00000098258; ENSGALP00000072483; ENSGALG00000013640. [P15720-1]
DR Ensembl; ENSGALT00000098875; ENSGALP00000070250; ENSGALG00000013640. [P15720-1]
DR Ensembl; ENSGALT00000101982; ENSGALP00000067863; ENSGALG00000013640. [P15720-1]
DR GeneID; 396217; -.
DR KEGG; gga:396217; -.
DR CTD; 4155; -.
DR VEuPathDB; HostDB:geneid_396217; -.
DR eggNOG; ENOG502S4SJ; Eukaryota.
DR GeneTree; ENSGT00390000014772; -.
DR HOGENOM; CLU_102586_0_0_1; -.
DR InParanoid; P15720; -.
DR OrthoDB; 872191at2759; -.
DR PhylomeDB; P15720; -.
DR PRO; PR:P15720; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000013640; Expressed in cerebellum and 11 other tissues.
DR ExpressionAtlas; P15720; baseline and differential.
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:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0042552; P:myelination; IBA:GO_Central.
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; Alternative splicing; Cell membrane; Citrullination; Membrane;
KW Methylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18618245"
FT CHAIN 2..174
FT /note="Myelin basic protein"
FT /id="PRO_0000158996"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine; in forms C1, C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 4
FT /note="Deamidated glutamine; in forms C1 and C2; partial"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 8
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 19
FT /note="Phosphoserine; in form C2"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 25
FT /note="Citrulline; in forms C1, C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 34
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 42
FT /note="Citrulline; in form C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 65
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 72
FT /note="Deamidated glutamine; in forms C1, C2 and C3;
FT partial"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 74
FT /note="Phosphoserine; in form C2"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 91
FT /note="Deamidated asparagine; in forms C1, C2 and C3;
FT partial"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 97
FT /note="Phosphothreonine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 102
FT /note="Deamidated glutamine; in form C1"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 102
FT /note="Deamidated glutamine; in forms C1, C2 and C3;
FT partial"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 106
FT /note="Omega-N-methylarginine; in forms C1, C2 and C3;
FT alternate"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 106
FT /note="Symmetric dimethylarginine; in forms C1, C2 and C3;
FT alternate"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 114
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 142
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 147
FT /note="Deamidated glutamine; in forms C1, C2 and C3;
FT partial"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 165
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 166
FT /note="Citrulline; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT MOD_RES 169
FT /note="Phosphoserine; in forms C2 and C3"
FT /evidence="ECO:0000269|PubMed:18618245"
FT VAR_SEQ 105..115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2475444"
FT /id="VSP_003323"
SQ SEQUENCE 174 AA; 18808 MW; 1935D29D945A317D CRC64;
MASQKRSSFR HGSKMASAST TDHARHGSPR HRDSGLLDSL GRFFGGDRHV PRRGFGKDIH
AARASHVGSI PQRSQHGRPG DDNPVVHFFK NIVSPRTPPP MQAKGRGLSL TRFSWGGEGH
KPGYGSGKFY EHKSAHKGHK GSYHEGQGTL SKIFKLGGSG SRPGSRSGSP VARR
