MYPR_RAT
ID MYPR_RAT Reviewed; 277 AA.
AC P60203; P04400; P06905; Q561K5;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=Plp1; Synonyms=Plp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2410294; DOI=10.1016/0014-5793(85)80869-3;
RA Dautigny A., Alliel P.M., D'Auriol L., Pham Dinh D., Nussbaum J.-L.,
RA Galibert F., Jolles P.;
RT "Molecular cloning and nucleotide sequence of a cDNA clone coding for rat
RT brain myelin proteolipid.";
RL FEBS Lett. 188:33-36(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2414013; DOI=10.1016/0092-8674(85)90289-2;
RA Milner R.J., Lai C., Nave K.-A., Lenoir D., Ogata J., Sutcliffe J.G.;
RT "Nucleotide sequences of two mRNAs for rat brain myelin proteolipid
RT protein.";
RL Cell 42:931-939(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-9; 46-53; 99-105; 112-122; 145-151 AND 193-229,
RP PALMITOYLATION AT SER-199, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; THR-116 AND THR-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP VARIANT MD PRO-75.
RX PubMed=2479544; DOI=10.1002/j.1460-2075.1989.tb08490.x;
RA Boison D., Stoffel W.;
RT "Myelin-deficient rat: a point mutation in exon III (A-->C, Thr75-->Pro) of
RT the myelin proteolipid protein causes dysmyelination and oligodendrocyte
RT death.";
RL EMBO J. 8:3295-3302(1989).
RN [7]
RP VARIANT MD PRO-75.
RX PubMed=1702593; DOI=10.1111/j.1749-6632.1990.tb42389.x;
RA Simons R., Riordan J.R.;
RT "Single base substitution in codon 74 of the MD rat myelin proteolipid
RT protein gene.";
RL Ann. N. Y. Acad. Sci. 605:146-154(1990).
RN [8]
RP VARIANT MD PRO-75.
RX PubMed=1689377; DOI=10.1111/j.1471-4159.1990.tb02360.x;
RA Simons R., Riordan J.R.;
RT "The myelin-deficient rat has a single base substitution in the third exon
RT of the myelin proteolipid protein gene.";
RL J. Neurochem. 54:1079-1081(1990).
CC -!- FUNCTION: This is the major myelin protein from the central nervous
CC system. It plays an important role in the formation or maintenance of
CC the multilamellar structure of myelin.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Myelin membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in
CC internodal regions, at paranodal axoglial junction and Schmidt-
CC Lanterman incisures of myelin sheat. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Plp1 are the causee of the dysmyelinating
CC disease MD.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; X02809; CAA26577.1; -; mRNA.
DR EMBL; M11185; AAA41898.1; -; mRNA.
DR EMBL; BC093596; AAH93596.1; -; mRNA.
DR PIR; I52775; MPRTPL.
DR RefSeq; NP_112252.1; NM_030990.2.
DR RefSeq; XP_017457402.1; XM_017601913.1.
DR AlphaFoldDB; P60203; -.
DR SMR; P60203; -.
DR BioGRID; 247046; 3.
DR CORUM; P60203; -.
DR IntAct; P60203; 3.
DR MINT; P60203; -.
DR STRING; 10116.ENSRNOP00000003283; -.
DR iPTMnet; P60203; -.
DR PhosphoSitePlus; P60203; -.
DR SwissPalm; P60203; -.
DR PaxDb; P60203; -.
DR PRIDE; P60203; -.
DR Ensembl; ENSRNOT00000003283; ENSRNOP00000003283; ENSRNOG00000002419.
DR GeneID; 24943; -.
DR KEGG; rno:24943; -.
DR UCSC; RGD:3354; rat.
DR CTD; 5354; -.
DR RGD; 3354; Plp1.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; P60203; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 914457at2759; -.
DR PhylomeDB; P60203; -.
DR TreeFam; TF315162; -.
DR PRO; PR:P60203; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000002419; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; P60203; RN.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IMP:RGD.
DR GO; GO:0098990; P:AMPA selective glutamate receptor signaling pathway; IMP:RGD.
DR GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR GO; GO:0061564; P:axon development; ISO:RGD.
DR GO; GO:0008366; P:axon ensheathment; ISO:RGD.
DR GO; GO:0022010; P:central nervous system myelination; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; IMP:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0042552; P:myelination; IMP:RGD.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; IMP:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR InterPro; IPR001614; Myelin_PLP.
DR InterPro; IPR018237; Myelin_PLP_CS.
DR PANTHER; PTHR11683; PTHR11683; 1.
DR Pfam; PF01275; Myelin_PLP; 1.
DR PRINTS; PR00214; MYELINPLP.
DR SMART; SM00002; PLP; 1.
DR PROSITE; PS00575; MYELIN_PLP_1; 1.
DR PROSITE; PS01004; MYELIN_PLP_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disease variant; Disulfide bond;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P04116"
FT CHAIN 2..277
FT /note="Myelin proteolipid protein"
FT /id="PRO_0000159008"
FT TOPO_DOM 2..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 37..63
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..88
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 89..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 178..233
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..260
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 261..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 6
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 7
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 109
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 139
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 141
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="O-palmitoyl serine"
FT /evidence="ECO:0000305|Ref.4"
FT DISULFID 184..228
FT /evidence="ECO:0000250"
FT DISULFID 201..220
FT /evidence="ECO:0000250"
FT VARIANT 75
FT /note="T -> P (in MD)"
FT /evidence="ECO:0000269|PubMed:1689377,
FT ECO:0000269|PubMed:1702593, ECO:0000269|PubMed:2479544"
SQ SEQUENCE 277 AA; 30077 MW; 3C2BC973C3061C38 CRC64;
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT
WTTCQSIAFP SKTSASIGSL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF
