MYPR_MOUSE
ID MYPR_MOUSE Reviewed; 277 AA.
AC P60202; P04400; P06905; Q9WUS9;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=Plp1; Synonyms=Plp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND DM-20).
RX PubMed=3469678; DOI=10.1073/pnas.84.5.1454;
RA Hudson L.D., Berndt J.A., Puckett C., Kozak C.A., Lazzarini R.A.;
RT "Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy
RT mutant mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1454-1458(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2451027; DOI=10.1016/0022-2836(88)90303-8;
RA Ikenaka K., Furuichi T., Iwasaki Y., Moriguchi A., Okano H., Mikoshiba K.;
RT "Myelin proteolipid protein gene structure and its regulation of expression
RT in normal and jimpy mutant mice.";
RL J. Mol. Biol. 199:587-596(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC STRAIN=BALB/cByJ;
RX PubMed=2449535; DOI=10.1002/jnr.490180302;
RA Macklin W.B., Campagnoni C.W., Deininger P.L., Gardinier M.V.;
RT "Structure and expression of the mouse myelin proteolipid protein gene.";
RL J. Neurosci. Res. 18:383-394(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3466187; DOI=10.1073/pnas.83.23.9264;
RA Nave K.-A., Lai C., Bloom F.E., Milner R.J.;
RT "Jimpy mutant mouse: a 74-base deletion in the mRNA for myelin proteolipid
RT protein and evidence for a primary defect in RNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9264-9268(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DM-20).
RX PubMed=2441390; DOI=10.1073/pnas.84.16.5665;
RA Nave K.-A., Lai C., Bloom F.E., Milner R.J.;
RT "Splice site selection in the proteolipid protein (PLP) gene transcript and
RT primary structure of the DM-20 protein of central nervous system myelin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5665-5669(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina;
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 [7]
RP PROTEIN SEQUENCE OF 2-9; 46-53; 99-122; 145-151 AND 193-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE OF 50-277.
RX PubMed=2442307; DOI=10.1111/j.1471-4159.1987.tb10005.x;
RA Sorg B.A., Smith M.M., Campagnoni A.T.;
RT "Developmental expression of the myelin proteolipid protein and basic
RT protein mRNAs in normal and dysmyelinating mutant mice.";
RL J. Neurochem. 49:1146-1154(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE OF 176-270.
RX PubMed=2432393; DOI=10.1128/mcb.6.11.3755-3762.1986;
RA Gardinier M.V., Macklin W.B., Diniak A.J., Deininger P.L.;
RT "Characterization of myelin proteolipid mRNAs in normal and jimpy mice.";
RL Mol. Cell. Biol. 6:3755-3762(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 209-232, AND ALTERNATIVE SPLICING.
RX PubMed=2444462; DOI=10.1016/0014-5793(87)80331-9;
RA Macklin W.B., Gardinier M.V., King K.D., Kampf K.;
RT "An AG to a GG transition at a splice site in the myelin proteolipid
RT protein gene in jimpy mice results in the removal of an exon.";
RL FEBS Lett. 223:417-421(1987).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=17634366; DOI=10.1523/jneurosci.1254-07.2007;
RA Werner H.B., Kuhlmann K., Shen S., Uecker M., Schardt A., Dimova K.,
RA Orfaniotou F., Dhaunchak A., Brinkmann B.G., Mobius W., Guarente L.,
RA Casaccia-Bonnefil P., Jahn O., Nave K.A.;
RT "Proteolipid protein is required for transport of sirtuin 2 into CNS
RT myelin.";
RL J. Neurosci. 27:7717-7730(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP VARIANT JIMPY MSD VAL-243.
RX PubMed=1688931; DOI=10.1523/jneurosci.10-01-00117.1990;
RA Gencic S., Hudson L.D.;
RT "Conservative amino acid substitution in the myelin proteolipid protein of
RT jimpymsd mice.";
RL J. Neurosci. 10:117-124(1990).
RN [14]
RP VARIANT RUMPSHAKER THR-187.
RX PubMed=1380672; DOI=10.1038/358758a0;
RA Schneider A., Montague P., Griffiths I., Fanarraga M., Kennedy P.,
RA Brophy P., Nave K.-A.;
RT "Uncoupling of hypomyelination and glial cell death by a mutation in the
RT proteolipid protein gene.";
RL Nature 358:758-761(1992).
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 {ECO:0000269|PubMed:17634366};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17634366}. Myelin
CC membrane {ECO:0000269|PubMed:17634366}. Note=Colocalizes with SIRT2 in
CC internodal regions, at paranodal axoglial junction and Schmidt-
CC Lanterman incisures of myelin sheat.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60202-1; Sequence=Displayed;
CC Name=DM-20;
CC IsoId=P60202-2; Sequence=VSP_009194;
CC -!- DISEASE: Note=Defects in Plp1 are the cause of the dysmyelinating
CC diseases Jimpy and Rumpshaker (rsh).
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
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DR EMBL; M15442; AAA39951.1; -; mRNA.
DR EMBL; M15442; AAA39952.1; ALT_SEQ; mRNA.
DR EMBL; M15442; AAA39953.1; -; mRNA.
DR EMBL; X07215; CAA30184.1; -; Genomic_DNA.
DR EMBL; X07216; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; X07217; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; X07218; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; X07219; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; X07220; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; X07221; CAA30184.1; JOINED; Genomic_DNA.
DR EMBL; M37335; AAA39954.1; -; Genomic_DNA.
DR EMBL; M37329; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M37330; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M37331; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M37332; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M37333; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M37334; AAA39954.1; JOINED; Genomic_DNA.
DR EMBL; M14674; AAA39955.1; -; mRNA.
DR EMBL; M16472; AAA39950.1; -; mRNA.
DR EMBL; BC027010; AAH27010.1; -; mRNA.
DR EMBL; X06375; CAB40821.1; -; Genomic_DNA.
DR CCDS; CCDS30424.1; -. [P60202-1]
DR CCDS; CCDS72436.1; -. [P60202-2]
DR PIR; S34792; S34792.
DR RefSeq; NP_001277490.1; NM_001290561.1. [P60202-2]
DR RefSeq; NP_001277491.1; NM_001290562.1.
DR RefSeq; NP_035253.1; NM_011123.3. [P60202-1]
DR RefSeq; XP_017173919.1; XM_017318430.1.
DR RefSeq; XP_017173920.1; XM_017318431.1.
DR RefSeq; XP_017173921.1; XM_017318432.1.
DR AlphaFoldDB; P60202; -.
DR SMR; P60202; -.
DR BioGRID; 202254; 28.
DR CORUM; P60202; -.
DR DIP; DIP-46200N; -.
DR IntAct; P60202; 3.
DR STRING; 10090.ENSMUSP00000033800; -.
DR iPTMnet; P60202; -.
DR PhosphoSitePlus; P60202; -.
DR SwissPalm; P60202; -.
DR MaxQB; P60202; -.
DR PaxDb; P60202; -.
DR PeptideAtlas; P60202; -.
DR PRIDE; P60202; -.
DR ProteomicsDB; 287341; -. [P60202-1]
DR ProteomicsDB; 287342; -. [P60202-2]
DR Antibodypedia; 582; 314 antibodies from 30 providers.
DR DNASU; 18823; -.
DR Ensembl; ENSMUST00000033800; ENSMUSP00000033800; ENSMUSG00000031425. [P60202-1]
DR Ensembl; ENSMUST00000113085; ENSMUSP00000108708; ENSMUSG00000031425. [P60202-2]
DR GeneID; 18823; -.
DR KEGG; mmu:18823; -.
DR UCSC; uc009ujc.2; mouse. [P60202-1]
DR UCSC; uc009ujd.2; mouse. [P60202-2]
DR CTD; 5354; -.
DR MGI; MGI:97623; Plp1.
DR VEuPathDB; HostDB:ENSMUSG00000031425; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; P60202; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 914457at2759; -.
DR PhylomeDB; P60202; -.
DR TreeFam; TF315162; -.
DR BioGRID-ORCS; 18823; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Plp1; mouse.
DR PRO; PR:P60202; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P60202; protein.
DR Bgee; ENSMUSG00000031425; Expressed in globus pallidus and 262 other tissues.
DR ExpressionAtlas; P60202; baseline and differential.
DR Genevisible; P60202; MM.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0019911; F:structural constituent of myelin sheath; ISO:MGI.
DR GO; GO:0098990; P:AMPA selective glutamate receptor signaling pathway; ISO:MGI.
DR GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR GO; GO:0061564; P:axon development; IGI:MGI.
DR GO; GO:0008366; P:axon ensheathment; IMP:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR GO; GO:0010001; P:glial cell differentiation; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
DR GO; GO:0042552; P:myelination; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disease variant; Disulfide bond; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; 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_0000159007"
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:0000250|UniProtKB:P60203"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60203"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60203"
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:0000250"
FT DISULFID 184..228
FT /evidence="ECO:0000250"
FT DISULFID 201..220
FT /evidence="ECO:0000250"
FT VAR_SEQ 117..151
FT /note="Missing (in isoform DM-20)"
FT /evidence="ECO:0000303|PubMed:2441390,
FT ECO:0000303|PubMed:3469678"
FT /id="VSP_009194"
FT VARIANT 187
FT /note="I -> T (in Rumpshaker)"
FT /evidence="ECO:0000269|PubMed:1380672"
FT VARIANT 243
FT /note="A -> V (in Jimpy MSD)"
FT /evidence="ECO:0000269|PubMed:1688931"
FT CONFLICT 70
FT /note="Y -> C (in Ref. 4 and 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="S -> Y (in Ref. 4; AAA39955)"
FT /evidence="ECO:0000305"
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
