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   02-SEP-2026, entry version 173.
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   -!- SUBUNIT: Interacts with MAL. {ECO:0000250|UniProtKB:P60201}.
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_001290561.2. [P60202-2]
DR   RefSeq; NP_001346046.1; NM_001359117.1. [P60202-1]
DR   RefSeq; NP_001346047.1; NM_001359118.1. [P60202-2]
DR   RefSeq; NP_001346048.1; NM_001359119.1. [P60202-1]
DR   RefSeq; NP_001346049.1; NM_001359120.1. [P60202-1]
DR   RefSeq; NP_035253.1; NM_011123.4. [P60202-1]
DR   AlphaFoldDB; P60202; -.
DR   SMR; P60202; -.
DR   BioGRID; 202254; 29.
DR   CORUM; P60202; -.
DR   DIP; DIP-46200N; -.
DR   FunCoup; P60202; 104.
DR   IntAct; P60202; 3.
DR   STRING; 10090.ENSMUSP00000033800; -.
DR   GlyGen; P60202; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P60202; -.
DR   PhosphoSitePlus; P60202; -.
DR   SwissPalm; P60202; -.
DR   PaxDb; 10090-ENSMUSP00000033800; -.
DR   PeptideAtlas; P60202; -.
DR   ProteomicsDB; 287341; -. [P60202-1]
DR   ProteomicsDB; 287342; -. [P60202-2]
DR   Antibodypedia; 582; 322 antibodies from 31 providers.
DR   DNASU; 18823; -.
DR   Ensembl; ENSMUST00000033800.13; ENSMUSP00000033800.7; ENSMUSG00000031425.16. [P60202-1]
DR   Ensembl; ENSMUST00000113085.2; ENSMUSP00000108708.2; ENSMUSG00000031425.16. [P60202-2]
DR   GeneID; 18823; -.
DR   KEGG; mmu:18823; -.
DR   UCSC; uc009ujc.2; mouse. [P60202-1]
DR   UCSC; uc009ujd.2; mouse. [P60202-2]
DR   AGR; MGI:97623; -.
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; AVCKTRE; -.
DR   OrthoDB; 9993736at2759; -.
DR   PhylomeDB; P60202; -.
DR   BioGRID-ORCS; 18823; 1 hit in 79 CRISPR screens.
DR   CD-CODE; CE726F99; Postsynaptic density.
DR   PRO; PR:P60202; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P60202; protein.
DR   Bgee; ENSMUSG00000031425; Expressed in globus pallidus and 264 other cell types or tissues.
DR   ExpressionAtlas; P60202; baseline and differential.
DR   GO; GO:0034683; C:integrin alphav-beta3 complex; ISO:GO_Central.
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:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central.
DR   GO; GO:0019911; F:structural constituent of myelin sheath; ISO:GO_Central.
DR   GO; GO:0098990; P:AMPA selective glutamate receptor signaling pathway; ISO:GO_Central.
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:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; ISO:GO_Central.
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:1904427; P:positive regulation of calcium ion transmembrane transport; ISO:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:GO_Central.
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; MYELIN PROTEOLIPID; 1.
DR   PANTHER; PTHR11683:SF11; MYELIN PROTEOLIPID PROTEIN; 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
//