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   27-MAR-2024, entry version 131.
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 cause 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; 10116-ENSRNOP00000003283; -.
DR   Ensembl; ENSRNOT00000003283.7; ENSRNOP00000003283.4; ENSRNOG00000002419.7.
DR   Ensembl; ENSRNOT00055043728; ENSRNOP00055035715; ENSRNOG00055025336.
DR   Ensembl; ENSRNOT00060030251; ENSRNOP00060024414; ENSRNOG00060017626.
DR   Ensembl; ENSRNOT00065045449; ENSRNOP00065037260; ENSRNOG00065026297.
DR   GeneID; 24943; -.
DR   KEGG; rno:24943; -.
DR   UCSC; RGD:3354; rat.
DR   AGR; RGD:3354; -.
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; NTWTTCN; -.
DR   OrthoDB; 3091734at2759; -.
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 cell types or tissues.
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: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; 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.
DR   Genevisible; P60203; RN.
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
//