MYPR_HUMAN
ID MYPR_HUMAN Reviewed; 277 AA.
AC P60201; P04400; P06905; Q502Y1; Q6FHZ6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Myelin proteolipid protein;
DE Short=PLP;
DE AltName: Full=Lipophilin;
GN Name=PLP1; Synonyms=PLP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3467339; DOI=10.1073/pnas.83.24.9807;
RA Diehl H.-J., Schaich M., Budzinski R.-M., Stoffel W.;
RT "Individual exons encode the integral membrane domains of human myelin
RT proteolipid protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9807-9811(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DM-20).
RX PubMed=2441695; DOI=10.1016/0006-291x(87)90580-8;
RA Simons R., Alon N., Riordan J.R.;
RT "Human myelin DM-20 proteolipid protein deletion defined by cDNA
RT sequence.";
RL Biochem. Biophys. Res. Commun. 146:666-671(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HLD1 ARG-163.
RX PubMed=2479017; DOI=10.1073/pnas.86.20.8128;
RA Hudson L.D., Puckett C., Berndt J., Chan J., Gencic S.;
RT "Mutation of the proteolipid protein gene PLP in a human X chromosome-
RT linked myelin disorder.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8128-8131(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DM-20).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DM-20).
RC TISSUE=Spinal cord, and Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-277.
RX PubMed=4041237; DOI=10.1515/bchm3.1985.366.2.627;
RA Stoffel W., Giersiefen H., Hillen H., Schroeder W., Tunggal B.;
RT "Amino-acid sequence of human and bovine brain myelin proteolipid protein
RT (lipophilin) is completely conserved.";
RL Biol. Chem. Hoppe-Seyler 366:627-635(1985).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spinal cord;
RX PubMed=2449536; DOI=10.1002/jnr.490180303;
RA Kronquist K.E., Crandall B.F., Macklin W.B., Campagnoni A.T.;
RT "Expression of myelin proteins in the developing human spinal cord: cloning
RT and sequencing of human proteolipid protein cDNA.";
RL J. Neurosci. Res. 18:395-401(1987).
RN [10]
RP TOPOLOGY.
RX PubMed=1711121; DOI=10.1007/bf01868534;
RA Popot J.-L., Pham-Dinh D., Dautigny A.;
RT "Major myelin proteolipid: the 4-alpha-helix topology.";
RL J. Membr. Biol. 120:233-246(1991).
RN [11]
RP VARIANT HLD1 SER-217.
RX PubMed=2773936;
RA Gencic S., Abuelo D., Ambler M., Hudson L.D.;
RT "Pelizaeus-Merzbacher disease: an X-linked neurologic disorder of myelin
RT metabolism with a novel mutation in the gene encoding proteolipid
RT protein.";
RL Am. J. Hum. Genet. 45:435-442(1989).
RN [12]
RP VARIANT HLD1 LEU-15.
RX PubMed=2480601; DOI=10.1073/pnas.86.23.9427;
RA Trofatter J., Dlouhy S.R., Demyer W., Conneally P.M., Hodes M.E.;
RT "Pelizaeus-Merzbacher disease: tight linkage to proteolipid protein gene
RT exon variant.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9427-9430(1989).
RN [13]
RP VARIANT HLD1 ILE-156.
RX PubMed=1708672; DOI=10.1515/bchm3.1990.371.2.1175;
RA Weimbs T., Dick T., Stoffel W., Boltshauser E.;
RT "A point mutation at the X-chromosomal proteolipid protein locus in
RT Pelizaeus-Merzbacher disease leads to disruption of myelinogenesis.";
RL Biol. Chem. Hoppe-Seyler 371:1175-1183(1990).
RN [14]
RP VARIANT HLD1 ILE-156.
RX PubMed=1707231; DOI=10.1002/ajmg.1320380129;
RA Pratt V.M., Trofatter J.A., Schinzel A., Dlouhy S.R., Conneally P.M.,
RA Hodes M.E.;
RT "A new mutation in the proteolipid protein (PLP) gene in a German family
RT with Pelizaeus-Merzbacher disease.";
RL Am. J. Med. Genet. 38:136-139(1991).
RN [15]
RP VARIANT HLD1 PHE-219.
RX PubMed=1715570; DOI=10.1073/pnas.88.17.7562;
RA Pham-Dinh D., Popot J.-L., Bosepflug-Tanguy O., Landrieu P., Deleuze P.,
RA Boue J., Jolles P., Dautigny A.;
RT "Pelizaeus-Merzbacher disease: a valine to phenylalanine point mutation in
RT a putative extracellular loop of myelin proteolipid.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7562-7566(1991).
RN [16]
RP VARIANTS HLD1 ARG-74 AND HIS-203.
RX PubMed=1376966;
RA Doll R., Natowicz M.R., Schiffmann R., Smith F.I.;
RT "Molecular diagnostics for myelin proteolipid protein gene mutations in
RT Pelizaeus-Merzbacher disease.";
RL Am. J. Hum. Genet. 51:161-169(1992).
RN [17]
RP VARIANTS HLD1 PRO-182 AND PRO-224.
RX PubMed=1384324;
RA Strautnieks S., Rutland P., Winter R.M., Baraitser M., Malcolm S.;
RT "Pelizaeus-Merzbacher disease: detection of mutations Thr181-->Pro and
RT Leu223-->Pro in the proteolipid protein gene, and prenatal diagnosis.";
RL Am. J. Hum. Genet. 51:871-878(1992).
RN [18]
RP VARIANT HLD1 GLU-166.
RX PubMed=7684886;
RA Pratt V.M., Kiefer J.R., Lahdetie J., Schleutker J., Hodes M.E.,
RA Dlouhy S.R.;
RT "Linkage of a new mutation in the proteolipid protein (PLP) gene to
RT Pelizaeus-Merzbacher disease (PMD) in a large Finnish kindred.";
RL Am. J. Hum. Genet. 52:1053-1056(1993).
RN [19]
RP VARIANT HLD1 SER-217.
RX PubMed=7679906; DOI=10.1515/bchm3.1993.374.1-6.75;
RA Otterbach B., Stoffel W., Ramaekers V.;
RT "A novel mutation in the proteolipid protein gene leading to Pelizaeus-
RT Merzbacher disease.";
RL Biol. Chem. Hoppe-Seyler 374:75-83(1993).
RN [20]
RP VARIANT HLD1 CYS-221.
RX PubMed=7683951; DOI=10.1093/hmg/2.1.19;
RA Iwaki A., Muramoto T., Iwaki I., Furumi H., Dario-Deleon M.L., Tateishi J.,
RA Fukumaki Y.;
RT "A missense mutation in the proteolipid protein gene responsible for
RT Pelizaeus-Merzbacher disease in a Japanese family.";
RL Hum. Mol. Genet. 2:19-22(1993).
RN [21]
RP VARIANT HLD1 SER-216.
RX PubMed=8037216;
RA Pratt V.M., Boyadjiev S., Dlouhy S.R., Silver K., der Kaloustian V.M.,
RA Hodes M.E.;
RT "Comparison of statistics for candidate-gene association studies using
RT cases and parents.";
RL Am. J. Hum. Genet. 55:402-409(1994).
RN [22]
RP VARIANT SPG2 TYR-140.
RX PubMed=8012387; DOI=10.1038/ng0394-257;
RA Saugier-Veber P., Munnich A., Bonneau D., Rozet J.-M., le Merrer M.,
RA Gil R., Boespflug-Tanguy O.;
RT "X-linked spastic paraplegia and Pelizaeus-Merzbacher disease are allelic
RT disorders at the proteolipid protein locus.";
RL Nat. Genet. 6:257-262(1994).
RN [23]
RP VARIANT SPG2 THR-187.
RX PubMed=7522741; DOI=10.1038/ng0794-351;
RA Kobayashi H., Hoffman E.P., Marks H.G.;
RT "The rumpshaker mutation in spastic paraplegia.";
RL Nat. Genet. 7:351-352(1994).
RN [24]
RP VARIANT HLD1 116-VAL--LEU-165 DEL.
RX PubMed=7539213; DOI=10.1002/ajmg.1320550404;
RA Kleindorfer D.O., Dlouhy S.R., Pratt V.M., Jones M.C., Trofatter J.A.,
RA Hodes M.E.;
RT "In-frame deletion in the proteolipid protein gene of a family with
RT Pelizaeus-Merzbacher disease.";
RL Am. J. Med. Genet. 55:405-407(1995).
RN [25]
RP VARIANT HLD1 ILE-43.
RX PubMed=7573159; DOI=10.1002/ajmg.1320580114;
RA Pratt V.M., Boyadjiev S., Green K., Hodes M.E., Dlouhy S.R.;
RT "Pelizaeus-Merzbacher disease caused by a de novo mutation that originated
RT in exon 2 of the maternal great-grandfather of the propositus.";
RL Am. J. Med. Genet. 58:70-73(1995).
RN [26]
RP VARIANT HLD1 PRO-249.
RX PubMed=7541731; DOI=10.1111/j.1399-0004.1995.tb03932.x;
RA Pratt V.M., Dlouhy S.R., Hodes M.E.;
RT "Pelizaeus-Merzbacher disease: a point mutation in exon 6 of the
RT proteolipid protein (PLP) gene.";
RL Clin. Genet. 47:99-100(1995).
RN [27]
RP VARIANT HLD1 ASN-151.
RX PubMed=7531827; DOI=10.1212/wnl.45.2.394;
RA Pratt V.M., Naidu S., Dlouhy S.R., Marks H.G., Hodes M.E.;
RT "A novel mutation in exon 3 of the proteolipid protein gene in Pelizaeus-
RT Merzbacher disease.";
RL Neurology 45:394-395(1995).
RN [28]
RP VARIANT SPG2 SER-237.
RX PubMed=8956049;
RX DOI=10.1002/(sici)1098-1004(1996)8:4<384::aid-humu17>3.0.co;2-z;
RA Donnelly A., Colley A., Crimmins D., Mulley J.;
RT "A novel mutation in exon 6 (F236S) of the proteolipid protein gene is
RT associated with spastic paraplegia.";
RL Hum. Mutat. 8:384-385(1996).
RN [29]
RP VARIANT SPG2 PRO-226.
RX PubMed=8780101; DOI=10.1212/wnl.46.4.1112;
RA Cambi F., Tang X.M., Cordray P., Fain P.R., Keppen L.D., Barker D.F.;
RT "Refined genetic mapping and proteolipid protein mutation analysis in X-
RT linked pure hereditary spastic paraplegia.";
RL Neurology 46:1112-1117(1996).
RN [30]
RP VARIANT HLD1 LYS-116.
RX PubMed=8909455; DOI=10.1212/wnl.47.5.1333;
RA Nance M.A., Boyadjiev S., Pratt V.M., Taylor S., Hodes M.E., Dlouhy S.R.;
RT "Adult-onset neurodegenerative disorder due to proteolipid protein gene
RT mutation in the mother of a man with Pelizaeus-Merzbacher disease.";
RL Neurology 47:1333-1335(1996).
RN [31]
RP VARIANT HLD1 PRO-242.
RX PubMed=9143933;
RX DOI=10.1002/(sici)1098-1004(1997)9:5<475::aid-humu19>3.0.co;2-#;
RA Kawanishi C., Osaka H., Owa K., Inoue K., Miyakawa T., Onishi H.,
RA Yamada Y., Suzuki K., Kimura S., Kosaka K.;
RT "A new missense mutation in exon 6 of the proteolipid protein gene in a
RT patient with Pelizaeus-Merzbacher disease.";
RL Hum. Mutat. 9:475-476(1997).
RN [32]
RP VARIANTS HLD1 ASP-209 AND LEU-211.
RX PubMed=9008538; DOI=10.1212/wnl.48.1.283;
RA Inoue K., Osaka H., Kawanishi C., Sugiyama N., Ishii M., Sugita K.,
RA Yamada Y., Kosaka K.;
RT "Mutations in the proteolipid protein gene in Japanese families with
RT Pelizaeus-Merzbacher disease.";
RL Neurology 48:283-285(1997).
RN [33]
RP VARIANT HLD1 VAL-243.
RX PubMed=9482656;
RX DOI=10.1002/(sici)1096-8628(19980203)75:4<439::aid-ajmg19>3.0.co;2-p;
RA Yamamoto T., Nanba E., Zhang H., Sasaki M., Komaki H., Takeshita K.;
RT "Jimpy(msd) mouse mutation and connatal Pelizaeus-Merzbacher disease.";
RL Am. J. Med. Genet. 75:439-440(1998).
RN [34]
RP VARIANT SPG2 PHE-170.
RX PubMed=9489796;
RX DOI=10.1002/(sici)1096-8628(19980217)75:5<516::aid-ajmg11>3.0.co;2-n;
RA Hodes M.E., Hadjisavvas A., Butler I.J., Aydanian A., Dlouhy S.R.;
RT "X-linked spastic paraplegia due to a mutation (C506T; Ser169Phe) in exon 4
RT of the proteolipid protein gene (PLP).";
RL Am. J. Med. Genet. 75:516-517(1998).
RN [35]
RP VARIANT HLD1 PHE-253.
RX PubMed=9788732; DOI=10.1111/j.1399-0004.1998.tb04295.x;
RA Hodes M.E., Aydanian A., Dlouhy S.R., Whelan D.T., Heshka T., Ronen G.;
RT "A de novo mutation (C755T; Ser252Phe) in exon 6 of the proteolipid protein
RT gene responsible for Pelizaeus-Merzbacher disease.";
RL Clin. Genet. 54:248-249(1998).
RN [36]
RP VARIANT HLD1 VAL-203.
RX PubMed=9747038; DOI=10.1007/s100380050072;
RA Nagao M., Kadowaki J.;
RT "Connatal Pelizaeus-Merzbacher disease: a missense mutation in exon 4 of
RT the proteolipid protein 'PLP' gene.";
RL J. Hum. Genet. 43:206-208(1998).
RN [37]
RP VARIANTS HLD1 VAL-32; ALA-172; GLY-205 AND CYS-207.
RX PubMed=9633722; DOI=10.1212/wnl.50.6.1749;
RA Sistermans E.A., de Coo R.F.M., De Wijs I.J., Van Oost B.A.;
RT "Duplication of the proteolipid protein gene is the major cause of
RT Pelizaeus-Merzbacher disease.";
RL Neurology 50:1749-1754(1998).
RN [38]
RP VARIANTS HLD1 TYR-35; THR-39; CYS-60; ARG-74; ARG-169; CYS-175; CYS-181;
RP ASN-183; ASN-203; GLU-203; GLY-203; HIS-210; ARG-212; SER-216; TYR-228;
RP PRO-234; GLU-246 AND GLU-248.
RX PubMed=10417279; DOI=10.1086/302483;
RA Mimault C., Giraud G., Courtois V., Cailloux F., Boire J.Y., Dastugue B.,
RA Boespflug-Tanguy O., Baethmann M., Bertini E., Cuisset J.M., Gaertner J.,
RA Hanefeld F., Kohlschutter A., Landrieu P., Mayer M., Peudenier S.,
RA Rodriguez D., Rating D., Surtees R., Uziel G., Vallee L., Voit T.;
RT "Proteolipoprotein gene analysis in 82 patients with sporadic Pelizaeus-
RT Merzbacher Disease: duplications, the major cause of the disease, originate
RT more frequently in male germ cells, but point mutations do not.";
RL Am. J. Hum. Genet. 65:360-369(1999).
RN [39]
RP VARIANT HLD1 PRO-46, AND VARIANTS GLY-166 AND ILE-224.
RX PubMed=9934976;
RX DOI=10.1002/(sici)1096-8628(19990115)82:2<132::aid-ajmg6>3.0.co;2-4;
RA Hodes M.E., Zimmerman A.W., Aydanian A., Naidu S., Miller N.R.,
RA Garcia Oller J.L., Barker B., Aleck K.A., Hurley T.D., Dlouhy S.R.;
RT "Different mutations in the same codon of the proteolipid protein gene,
RT PLP, may help in correlating genotype with phenotype in Pelizaeus-
RT Merzbacher disease/X-linked spastic paraplegia (PMD/SPG2).";
RL Am. J. Med. Genet. 82:132-139(1999).
RN [40]
RP VARIANTS HLD1 ARG-46; ASP-209; LEU-211; TYR-220 AND PRO-242.
RX PubMed=9894878; DOI=10.1002/1531-8249(199901)45:1<59::aid-art11>3.0.co;2-3;
RA Osaka H., Kawanishi C., Inoue K., Onishi H., Kobayashi T., Sugiyama N.,
RA Kosaka K., Nezu A., Fujii K., Sugita K., Kodama K., Murayama K.,
RA Murayama S., Kanazawa I., Kimura S.;
RT "Pelizaeus-Merzbacher disease: three novel mutations and implication for
RT locus heterogeneity.";
RL Ann. Neurol. 45:59-64(1999).
RN [41]
RP VARIANT SPG2 TYR-148.
RX PubMed=10319897;
RX DOI=10.1002/1531-8249(199905)45:5<680::aid-ana23>3.0.co;2-h;
RA Sivakumar K., Sambuughin N., Selenge B., Nagle J.W., Baasanjav D.,
RA Hudson L.D., Goldfarb L.G.;
RT "Novel exon 3B proteolipid protein gene mutation causing late-onset spastic
RT paraplegia type 2 with variable penetrance in female family members.";
RL Ann. Neurol. 45:680-683(1999).
RN [42]
RP VARIANT HLD1 THR-247.
RX PubMed=10425042;
RX DOI=10.1002/(sici)1098-1004(1999)14:2<182::aid-humu12>3.0.co;2-y;
RA Yamamoto T., Nanba E.;
RT "A novel mutation (A246T) in exon 6 of the proteolipid protein gene
RT associated with connatal Pelizaeus-Merzbacher disease.";
RL Hum. Mutat. 14:182-182(1999).
RN [43]
RP VARIANTS HLD1 PRO-31; LEU-32; SER-51; ARG-74; CYS-181; GLU-203; ARG-212 AND
RP ALA-216, AND VARIANT SPG2 TYR-130.
RX PubMed=11093273; DOI=10.1038/sj.ejhg.5200537;
RA Cailloux F., Gauthier-Barichard F., Mimault C., Isabelle V., Courtois V.,
RA Giraud G., Dastugue B., Boespflug-Tanguy O., Baethmann M., Bertini E.,
RA Cuisset J.M., Gaertner J., Hanefeld F., Kohlschutter A., Landrieu P.,
RA Mayer M., Peudenier S., Rodriguez D., Rating D., Surtees R., Uziel G.,
RA Vallee L., Voit T.;
RT "Genotype-phenotype correlation in inherited brain myelination defects due
RT to proteolipid protein gene mutations.";
RL Eur. J. Hum. Genet. 8:837-845(2000).
RN [44]
RP VARIANT HLD1 GLU-243.
RX PubMed=11786921;
RA Seeman P., Paderova K., Benes V. Jr., Sistermans E.A.;
RT "A severe connatal form of Pelizaeus Merzbacher disease in a Czech boy
RT caused by a novel mutation (725C>A, Ala242Glu) at the 'jimpy(msd) codon' in
RT the PLP gene.";
RL Int. J. Mol. Med. 9:125-129(2002).
RN [45]
RP VARIANT SPG2 LEU-216.
RX PubMed=15450775; DOI=10.1016/j.jns.2004.05.015;
RA Lee E.S., Moon H.K., Park Y.H., Garbern J., Hobson G.M.;
RT "A case of complicated spastic paraplegia 2 due to a point mutation in the
RT proteolipid protein 1 gene.";
RL J. Neurol. Sci. 224:83-87(2004).
RN [46]
RP VARIANTS HLD1 TYR-33; ARG-35; THR-39; PRO-46; CYS-50; PRO-76; TYR-148;
RP GLU-162; PRO-170; SER-173; PRO-225; PRO-239 AND ALA-246.
RX PubMed=15712223; DOI=10.1002/humu.9314;
RA Huebner C.A., Orth U., Senning A., Steglich C., Kohlschuetter A.,
RA Korinthenberg R., Gal A.;
RT "Seventeen novel PLP1 mutations in patients with Pelizaeus-Merzbacher
RT disease.";
RL Hum. Mutat. 25:321-322(2005).
RN [47]
RP VARIANT SPG2 TRP-137.
RX PubMed=17438221; DOI=10.1212/01.wnl.0000259522.49388.53;
RA Gorman M.P., Golomb M.R., Walsh L.E., Hobson G.M., Garbern J.Y.,
RA Kinkel R.P., Darras B.T., Urion D.K., Eksioglu Y.Z.;
RT "Steroid-responsive neurologic relapses in a child with a proteolipid
RT protein-1 mutation.";
RL Neurology 68:1305-1307(2007).
RN [48]
RP VARIANT SPG2 PRO-30, CHARACTERIZATION OF VARIANT SPG2 PRO-30, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24103481; DOI=10.1016/j.gene.2013.09.076;
RA Noetzli L., Sanz P.G., Brodsky G.L., Hinckley J.D., Giugni J.C.,
RA Giannaula R.J., Gonzalez-Alegre P., Di Paola J.;
RT "A novel mutation in PLP1 causes severe hereditary spastic paraplegia type
RT 2.";
RL Gene 533:447-450(2014).
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 -!- INTERACTION:
CC P60201; P05067-4: APP; NbExp=5; IntAct=EBI-8653150, EBI-302641;
CC P60201; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-8653150, EBI-747430;
CC P60201; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-8653150, EBI-6942903;
CC P60201; Q16849-3: PTPRN; NbExp=3; IntAct=EBI-8653150, EBI-10200782;
CC P60201-1; P60201-1: PLP1; NbExp=2; IntAct=EBI-15668477, EBI-15668477;
CC P60201-2; Q86Y34: ADGRG3; NbExp=3; IntAct=EBI-12188331, EBI-17979264;
CC P60201-2; Q96PS8: AQP10; NbExp=3; IntAct=EBI-12188331, EBI-12820279;
CC P60201-2; Q13520: AQP6; NbExp=3; IntAct=EBI-12188331, EBI-13059134;
CC P60201-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12188331, EBI-11343438;
CC P60201-2; Q96RK4: BBS4; NbExp=3; IntAct=EBI-12188331, EBI-1805814;
CC P60201-2; Q9BXK5: BCL2L13; NbExp=6; IntAct=EBI-12188331, EBI-747430;
CC P60201-2; Q13323: BIK; NbExp=3; IntAct=EBI-12188331, EBI-700794;
CC P60201-2; Q9BXU9: CALN1; NbExp=3; IntAct=EBI-12188331, EBI-12187137;
CC P60201-2; P17655: CAPN2; NbExp=3; IntAct=EBI-12188331, EBI-1028956;
CC P60201-2; P25942: CD40; NbExp=3; IntAct=EBI-12188331, EBI-525714;
CC P60201-2; P04233-2: CD74; NbExp=3; IntAct=EBI-12188331, EBI-12222807;
CC P60201-2; O14735: CDIPT; NbExp=3; IntAct=EBI-12188331, EBI-358858;
CC P60201-2; P57739: CLDN2; NbExp=3; IntAct=EBI-12188331, EBI-751440;
CC P60201-2; P56880: CLDN20; NbExp=3; IntAct=EBI-12188331, EBI-23801559;
CC P60201-2; Q9UHP7-3: CLEC2D; NbExp=3; IntAct=EBI-12188331, EBI-11749983;
CC P60201-2; O43889-2: CREB3; NbExp=3; IntAct=EBI-12188331, EBI-625022;
CC P60201-2; Q96BA8: CREB3L1; NbExp=16; IntAct=EBI-12188331, EBI-6942903;
CC P60201-2; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-12188331, EBI-2680384;
CC P60201-2; P40126: DCT; NbExp=3; IntAct=EBI-12188331, EBI-18640065;
CC P60201-2; O75923-13: DYSF; NbExp=3; IntAct=EBI-12188331, EBI-19949386;
CC P60201-2; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-12188331, EBI-526033;
CC P60201-2; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-12188331, EBI-18535450;
CC P60201-2; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12188331, EBI-781551;
CC P60201-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12188331, EBI-18304435;
CC P60201-2; Q96LA5-2: FCRL2; NbExp=3; IntAct=EBI-12188331, EBI-17263163;
CC P60201-2; O15552: FFAR2; NbExp=3; IntAct=EBI-12188331, EBI-2833872;
CC P60201-2; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-12188331, EBI-12142257;
CC P60201-2; P01350: GAST; NbExp=3; IntAct=EBI-12188331, EBI-3436637;
CC P60201-2; O15529: GPR42; NbExp=3; IntAct=EBI-12188331, EBI-18076404;
CC P60201-2; Q9BZJ8: GPR61; NbExp=3; IntAct=EBI-12188331, EBI-12808020;
CC P60201-2; O00219-2: HAS3; NbExp=3; IntAct=EBI-12188331, EBI-17186025;
CC P60201-2; Q9Y5U9: IER3IP1; NbExp=3; IntAct=EBI-12188331, EBI-725665;
CC P60201-2; Q01628: IFITM3; NbExp=3; IntAct=EBI-12188331, EBI-7932862;
CC P60201-2; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-12188331, EBI-10266796;
CC P60201-2; Q9HDC5: JPH1; NbExp=3; IntAct=EBI-12188331, EBI-465137;
CC P60201-2; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-12188331, EBI-10973851;
CC P60201-2; P26715: KLRC1; NbExp=3; IntAct=EBI-12188331, EBI-9018187;
CC P60201-2; O95214: LEPROTL1; NbExp=3; IntAct=EBI-12188331, EBI-750776;
CC P60201-2; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-12188331, EBI-17490413;
CC P60201-2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12188331, EBI-2820517;
CC P60201-2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-12188331, EBI-11956541;
CC P60201-2; O14880: MGST3; NbExp=3; IntAct=EBI-12188331, EBI-724754;
CC P60201-2; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-12188331, EBI-12806656;
CC P60201-2; Q96JQ5: MS4A4A; NbExp=5; IntAct=EBI-12188331, EBI-12820341;
CC P60201-2; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12188331, EBI-3923617;
CC P60201-2; P15941-11: MUC1; NbExp=3; IntAct=EBI-12188331, EBI-17263240;
CC P60201-2; Q96S97: MYADM; NbExp=3; IntAct=EBI-12188331, EBI-13301517;
CC P60201-2; Q02297-10: NRG1; NbExp=3; IntAct=EBI-12188331, EBI-12842334;
CC P60201-2; O15534: PER1; NbExp=3; IntAct=EBI-12188331, EBI-2557276;
CC P60201-2; Q6UXB8: PI16; NbExp=3; IntAct=EBI-12188331, EBI-12810028;
CC P60201-2; P57054: PIGP; NbExp=3; IntAct=EBI-12188331, EBI-17630288;
CC P60201-2; Q16849-3: PTPRN; NbExp=9; IntAct=EBI-12188331, EBI-10200782;
CC P60201-2; Q09028: RBBP4; NbExp=3; IntAct=EBI-12188331, EBI-620823;
CC P60201-2; Q8NC24: RELL2; NbExp=3; IntAct=EBI-12188331, EBI-10269209;
CC P60201-2; Q96TC7: RMDN3; NbExp=3; IntAct=EBI-12188331, EBI-1056589;
CC P60201-2; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-12188331, EBI-13044680;
CC P60201-2; Q86WV1-2: SKAP1; NbExp=3; IntAct=EBI-12188331, EBI-11995314;
CC P60201-2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12188331, EBI-18159983;
CC P60201-2; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-12188331, EBI-17595455;
CC P60201-2; Q15758: SLC1A5; NbExp=3; IntAct=EBI-12188331, EBI-356576;
CC P60201-2; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-12188331, EBI-12814225;
CC P60201-2; P0CK97: SLC35E2A; NbExp=3; IntAct=EBI-12188331, EBI-18054851;
CC P60201-2; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-12188331, EBI-13389236;
CC P60201-2; Q96GZ6: SLC41A3; NbExp=3; IntAct=EBI-12188331, EBI-7225508;
CC P60201-2; Q9BZL3: SMIM3; NbExp=4; IntAct=EBI-12188331, EBI-741850;
CC P60201-2; Q6ZMD2-2: SPNS3; NbExp=3; IntAct=EBI-12188331, EBI-17848320;
CC P60201-2; Q16623: STX1A; NbExp=3; IntAct=EBI-12188331, EBI-712466;
CC P60201-2; Q12846: STX4; NbExp=3; IntAct=EBI-12188331, EBI-744942;
CC P60201-2; Q96L08: SUSD3; NbExp=3; IntAct=EBI-12188331, EBI-18194029;
CC P60201-2; Q5T0J7-2: TEX35; NbExp=3; IntAct=EBI-12188331, EBI-12833746;
CC P60201-2; Q9BVX2: TMEM106C; NbExp=3; IntAct=EBI-12188331, EBI-2821497;
CC P60201-2; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-12188331, EBI-8638294;
CC P60201-2; Q6ZP80: TMEM182; NbExp=3; IntAct=EBI-12188331, EBI-10255122;
CC P60201-2; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-12188331, EBI-10315004;
CC P60201-2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-12188331, EBI-12887458;
CC P60201-2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-12188331, EBI-11956809;
CC P60201-2; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-12188331, EBI-3923061;
CC P60201-2; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12188331, EBI-18178701;
CC P60201-2; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-12188331, EBI-12111910;
CC P60201-2; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-12188331, EBI-12345267;
CC P60201-2; O00526: UPK2; NbExp=3; IntAct=EBI-12188331, EBI-10179682;
CC P60201-2; Q99536: VAT1; NbExp=3; IntAct=EBI-12188331, EBI-2514883;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24103481};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24103481}. Myelin
CC membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in internodal
CC regions, at paranodal axoglial junction and Schmidt-Lanterman incisures
CC of myelin sheat. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60201-1; Sequence=Displayed;
CC Name=DM-20;
CC IsoId=P60201-2; Sequence=VSP_003325;
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 1 (HLD1) [MIM:312080]: An X-
CC linked recessive disorder of the central nervous system in which myelin
CC is not formed properly. Clinically characterized by nystagmus, spastic
CC quadriplegia, ataxia, and developmental delay.
CC {ECO:0000269|PubMed:10417279, ECO:0000269|PubMed:10425042,
CC ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:11786921,
CC ECO:0000269|PubMed:1376966, ECO:0000269|PubMed:1384324,
CC ECO:0000269|PubMed:15712223, ECO:0000269|PubMed:1707231,
CC ECO:0000269|PubMed:1708672, ECO:0000269|PubMed:1715570,
CC ECO:0000269|PubMed:2479017, ECO:0000269|PubMed:2480601,
CC ECO:0000269|PubMed:2773936, ECO:0000269|PubMed:7531827,
CC ECO:0000269|PubMed:7539213, ECO:0000269|PubMed:7541731,
CC ECO:0000269|PubMed:7573159, ECO:0000269|PubMed:7679906,
CC ECO:0000269|PubMed:7683951, ECO:0000269|PubMed:7684886,
CC ECO:0000269|PubMed:8037216, ECO:0000269|PubMed:8909455,
CC ECO:0000269|PubMed:9008538, ECO:0000269|PubMed:9143933,
CC ECO:0000269|PubMed:9482656, ECO:0000269|PubMed:9633722,
CC ECO:0000269|PubMed:9747038, ECO:0000269|PubMed:9788732,
CC ECO:0000269|PubMed:9894878, ECO:0000269|PubMed:9934976}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Spastic paraplegia 2, X-linked (SPG2) [MIM:312920]: A form of
CC spastic paraplegia, a neurodegenerative disorder characterized by a
CC slow, gradual, progressive weakness and spasticity of the lower limbs.
CC Rate of progression and the severity of symptoms are quite variable.
CC Initial symptoms may include difficulty with balance, weakness and
CC stiffness in the legs, muscle spasms, and dragging the toes when
CC walking. In some forms of the disorder, bladder symptoms (such as
CC incontinence) may appear, or the weakness and stiffness may spread to
CC other parts of the body. SPG2 is characterized by spastic gait and
CC hyperreflexia. In some patients, complicating features include
CC nystagmus, dysarthria, sensory disturbance, intellectual disability,
CC optic atrophy. {ECO:0000269|PubMed:10319897,
CC ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:15450775,
CC ECO:0000269|PubMed:17438221, ECO:0000269|PubMed:24103481,
CC ECO:0000269|PubMed:7522741, ECO:0000269|PubMed:8012387,
CC ECO:0000269|PubMed:8780101, ECO:0000269|PubMed:8956049,
CC ECO:0000269|PubMed:9489796}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60350.1; Type=Miscellaneous discrepancy; Note=The submitted sequence only contains the last exon but the authors annotated a CDS including all exons of that gene.; Evidence={ECO:0000305};
CC Sequence=AAD13880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M15032; AAA60350.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M15026; AAA60350.1; JOINED; Genomic_DNA.
DR EMBL; M15027; AAA60350.1; JOINED; Genomic_DNA.
DR EMBL; M15028; AAA60350.1; JOINED; Genomic_DNA.
DR EMBL; M15029; AAA60350.1; JOINED; Genomic_DNA.
DR EMBL; M15031; AAA60350.1; JOINED; Genomic_DNA.
DR EMBL; AJ006976; CAA07364.1; -; Genomic_DNA.
DR EMBL; M54927; AAA59565.1; -; mRNA.
DR EMBL; M17085; AAA60118.1; -; mRNA.
DR EMBL; M27110; AAA60117.1; -; mRNA.
DR EMBL; CR536542; CAG38779.1; -; mRNA.
DR EMBL; Z73964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471190; EAW54690.1; -; Genomic_DNA.
DR EMBL; BC002665; AAH02665.1; -; mRNA.
DR EMBL; BC095452; AAH95452.1; -; mRNA.
DR EMBL; D13320; BAA02577.1; -; Genomic_DNA.
DR EMBL; S55837; AAD13880.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS14513.1; -. [P60201-1]
DR CCDS; CCDS14514.1; -. [P60201-2]
DR PIR; A26665; MPHUPL.
DR RefSeq; NP_000524.3; NM_000533.4. [P60201-1]
DR RefSeq; NP_001122306.1; NM_001128834.2. [P60201-1]
DR RefSeq; NP_001291933.1; NM_001305004.1.
DR RefSeq; NP_955772.1; NM_199478.2. [P60201-2]
DR PDB; 2XPG; X-ray; 2.60 A; C=45-53.
DR PDBsum; 2XPG; -.
DR AlphaFoldDB; P60201; -.
DR SMR; P60201; -.
DR BioGRID; 111368; 110.
DR IntAct; P60201; 103.
DR MINT; P60201; -.
DR STRING; 9606.ENSP00000481006; -.
DR GlyGen; P60201; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P60201; -.
DR PhosphoSitePlus; P60201; -.
DR SwissPalm; P60201; -.
DR BioMuta; PLP1; -.
DR DMDM; 41393531; -.
DR UCD-2DPAGE; P60201; -.
DR EPD; P60201; -.
DR jPOST; P60201; -.
DR MassIVE; P60201; -.
DR PaxDb; P60201; -.
DR PeptideAtlas; P60201; -.
DR PRIDE; P60201; -.
DR ProteomicsDB; 57188; -. [P60201-1]
DR ProteomicsDB; 57189; -. [P60201-2]
DR Antibodypedia; 582; 314 antibodies from 30 providers.
DR DNASU; 5354; -.
DR Ensembl; ENST00000612423.4; ENSP00000481006.1; ENSG00000123560.14. [P60201-1]
DR Ensembl; ENST00000619236.1; ENSP00000477619.1; ENSG00000123560.14. [P60201-2]
DR Ensembl; ENST00000621218.5; ENSP00000484450.1; ENSG00000123560.14. [P60201-1]
DR GeneID; 5354; -.
DR KEGG; hsa:5354; -.
DR MANE-Select; ENST00000621218.5; ENSP00000484450.1; NM_000533.5; NP_000524.3.
DR UCSC; uc033epn.2; human. [P60201-1]
DR CTD; 5354; -.
DR DisGeNET; 5354; -.
DR GeneCards; PLP1; -.
DR GeneReviews; PLP1; -.
DR HGNC; HGNC:9086; PLP1.
DR HPA; ENSG00000123560; Tissue enriched (brain).
DR MalaCards; PLP1; -.
DR MIM; 300401; gene.
DR MIM; 312080; phenotype.
DR MIM; 312920; phenotype.
DR neXtProt; NX_P60201; -.
DR OpenTargets; ENSG00000123560; -.
DR Orphanet; 599376; Hypomyelination of early myelinating structures.
DR Orphanet; 280234; Null syndrome.
DR Orphanet; 280229; Pelizaeus-Merzbacher disease in female carriers.
DR Orphanet; 280219; Pelizaeus-Merzbacher disease, classic form.
DR Orphanet; 280210; Pelizaeus-Merzbacher disease, connatal form.
DR Orphanet; 280224; Pelizaeus-Merzbacher disease, transitional form.
DR Orphanet; 99015; Spastic paraplegia type 2.
DR PharmGKB; PA33414; -.
DR VEuPathDB; HostDB:ENSG00000123560; -.
DR eggNOG; KOG4800; Eukaryota.
DR GeneTree; ENSGT00390000006915; -.
DR HOGENOM; CLU_064167_2_1_1; -.
DR InParanoid; P60201; -.
DR OMA; ENYFARN; -.
DR OrthoDB; 712239at2759; -.
DR PhylomeDB; P60201; -.
DR TreeFam; TF315162; -.
DR PathwayCommons; P60201; -.
DR SignaLink; P60201; -.
DR BioGRID-ORCS; 5354; 18 hits in 697 CRISPR screens.
DR ChiTaRS; PLP1; human.
DR GeneWiki; Proteolipid_protein_1; -.
DR GenomeRNAi; 5354; -.
DR Pharos; P60201; Tbio.
DR PRO; PR:P60201; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P60201; protein.
DR Bgee; ENSG00000123560; Expressed in middle frontal gyrus and 175 other tissues.
DR ExpressionAtlas; P60201; baseline and differential.
DR Genevisible; P60201; HS.
DR GO; GO:0034683; C:integrin alphav-beta3 complex; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0019911; F:structural constituent of myelin sheath; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0098990; P:AMPA selective glutamate receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IBA:GO_Central.
DR GO; GO:0008366; P:axon ensheathment; TAS:ProtInc.
DR GO; GO:0022010; P:central nervous system myelination; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1904427; P:positive regulation of calcium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0021762; P:substantia nigra development; HEP: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 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disease variant; Disulfide bond;
KW Hereditary spastic paraplegia; Leukodystrophy; Lipoprotein; Membrane;
KW Neurodegeneration; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4041237"
FT CHAIN 2..277
FT /note="Myelin proteolipid protein"
FT /id="PRO_0000159005"
FT TOPO_DOM 2..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:1711121"
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|PubMed:1711121"
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|PubMed:1711121"
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|PubMed:1711121"
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|PubMed:1711121"
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:15489334,
FT ECO:0000303|PubMed:2441695, ECO:0000303|Ref.4"
FT /id="VSP_003325"
FT VARIANT 15
FT /note="P -> L (in HLD1; dbSNP:rs11543022)"
FT /evidence="ECO:0000269|PubMed:2480601"
FT /id="VAR_004546"
FT VARIANT 30
FT /note="A -> P (in SPG2; partially retained in the
FT endoplasmic reticulum; does not induce unfolded protein
FT response)"
FT /evidence="ECO:0000269|PubMed:24103481"
FT /id="VAR_070667"
FT VARIANT 31
FT /note="L -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:11093273"
FT /id="VAR_015014"
FT VARIANT 32
FT /note="F -> L (in HLD1)"
FT /evidence="ECO:0000269|PubMed:11093273"
FT /id="VAR_015015"
FT VARIANT 32
FT /note="F -> V (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9633722"
FT /id="VAR_015016"
FT VARIANT 33
FT /note="C -> Y (in HLD1; dbSNP:rs1064794255)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046906"
FT VARIANT 35
FT /note="C -> R (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046907"
FT VARIANT 35
FT /note="C -> Y (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015017"
FT VARIANT 39
FT /note="A -> T (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:15712223"
FT /id="VAR_015018"
FT VARIANT 43
FT /note="T -> I (in HLD1; dbSNP:rs132630289)"
FT /evidence="ECO:0000269|PubMed:7573159"
FT /id="VAR_004547"
FT VARIANT 46
FT /note="L -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223,
FT ECO:0000269|PubMed:9934976"
FT /id="VAR_015019"
FT VARIANT 46
FT /note="L -> R (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9894878"
FT /id="VAR_015020"
FT VARIANT 50
FT /note="Y -> C (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046908"
FT VARIANT 51
FT /note="F -> S (in HLD1)"
FT /evidence="ECO:0000269|PubMed:11093273"
FT /id="VAR_015021"
FT VARIANT 60
FT /note="Y -> C (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015022"
FT VARIANT 74
FT /note="G -> R (in HLD1; dbSNP:rs132630285)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:1376966"
FT /id="VAR_004548"
FT VARIANT 76
FT /note="A -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046909"
FT VARIANT 116
FT /note="T -> K (in HLD1)"
FT /evidence="ECO:0000269|PubMed:8909455"
FT /id="VAR_015023"
FT VARIANT 117..165
FT /note="Missing (in HLD1)"
FT /id="VAR_004550"
FT VARIANT 130
FT /note="H -> Y (in SPG2; dbSNP:rs878853076)"
FT /evidence="ECO:0000269|PubMed:11093273"
FT /id="VAR_015024"
FT VARIANT 137
FT /note="R -> W (in SPG2; dbSNP:rs132630295)"
FT /evidence="ECO:0000269|PubMed:17438221"
FT /id="VAR_046910"
FT VARIANT 140
FT /note="H -> Y (in SPG2; dbSNP:rs132630287)"
FT /evidence="ECO:0000269|PubMed:8012387"
FT /id="VAR_004551"
FT VARIANT 148
FT /note="H -> Y (in HLD1 and SPG2)"
FT /evidence="ECO:0000269|PubMed:10319897,
FT ECO:0000269|PubMed:15712223"
FT /id="VAR_015025"
FT VARIANT 151
FT /note="K -> N (in HLD1)"
FT /evidence="ECO:0000269|PubMed:7531827"
FT /id="VAR_015026"
FT VARIANT 156
FT /note="T -> I (in HLD1; dbSNP:rs132630280)"
FT /evidence="ECO:0000269|PubMed:1707231,
FT ECO:0000269|PubMed:1708672"
FT /id="VAR_004552"
FT VARIANT 162
FT /note="V -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046911"
FT VARIANT 163
FT /note="W -> R (in HLD1; dbSNP:rs132630279)"
FT /evidence="ECO:0000269|PubMed:2479017"
FT /id="VAR_004553"
FT VARIANT 166
FT /note="V -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:7684886"
FT /id="VAR_004554"
FT VARIANT 166
FT /note="V -> G (probable disease-associated variant found in
FT Pelizaeus-Merzbacher disease/X-linked spastic paraplegia)"
FT /evidence="ECO:0000269|PubMed:9934976"
FT /id="VAR_015027"
FT VARIANT 169
FT /note="C -> R (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015028"
FT VARIANT 170
FT /note="S -> F (in SPG2; dbSNP:rs132630294)"
FT /evidence="ECO:0000269|PubMed:9489796"
FT /id="VAR_015029"
FT VARIANT 170
FT /note="S -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046912"
FT VARIANT 172
FT /note="V -> A (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9633722"
FT /id="VAR_015030"
FT VARIANT 173
FT /note="P -> S (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046913"
FT VARIANT 175
FT /note="Y -> C (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015031"
FT VARIANT 181
FT /note="W -> C (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:11093273"
FT /id="VAR_015032"
FT VARIANT 182
FT /note="T -> P (in HLD1; dbSNP:rs132630282)"
FT /evidence="ECO:0000269|PubMed:1384324"
FT /id="VAR_004555"
FT VARIANT 183
FT /note="T -> N (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015033"
FT VARIANT 187
FT /note="I -> T (in SPG2; dbSNP:rs132630288)"
FT /evidence="ECO:0000269|PubMed:7522741"
FT /id="VAR_004556"
FT VARIANT 203
FT /note="D -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:11093273"
FT /id="VAR_015034"
FT VARIANT 203
FT /note="D -> G (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015035"
FT VARIANT 203
FT /note="D -> H (in HLD1; dbSNP:rs132630284)"
FT /evidence="ECO:0000269|PubMed:1376966"
FT /id="VAR_004557"
FT VARIANT 203
FT /note="D -> N (in HLD1; dbSNP:rs132630284)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015036"
FT VARIANT 203
FT /note="D -> V (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9747038"
FT /id="VAR_007956"
FT VARIANT 205
FT /note="R -> G (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9633722"
FT /id="VAR_015037"
FT VARIANT 207
FT /note="Y -> C (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9633722"
FT /id="VAR_015038"
FT VARIANT 209
FT /note="V -> D (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9008538,
FT ECO:0000269|PubMed:9894878"
FT /id="VAR_015039"
FT VARIANT 210
FT /note="L -> H (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015040"
FT VARIANT 211
FT /note="P -> L (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9008538,
FT ECO:0000269|PubMed:9894878"
FT /id="VAR_015041"
FT VARIANT 212
FT /note="W -> R (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:11093273"
FT /id="VAR_015042"
FT VARIANT 216
FT /note="P -> A (in HLD1)"
FT /evidence="ECO:0000269|PubMed:11093273"
FT /id="VAR_015043"
FT VARIANT 216
FT /note="P -> L (in SPG2)"
FT /evidence="ECO:0000269|PubMed:15450775"
FT /id="VAR_046914"
FT VARIANT 216
FT /note="P -> S (in HLD1; dbSNP:rs132630278)"
FT /evidence="ECO:0000269|PubMed:10417279,
FT ECO:0000269|PubMed:8037216"
FT /id="VAR_004558"
FT VARIANT 217
FT /note="G -> S (in HLD1)"
FT /evidence="ECO:0000269|PubMed:2773936,
FT ECO:0000269|PubMed:7679906"
FT /id="VAR_004559"
FT VARIANT 219
FT /note="V -> F (in HLD1; dbSNP:rs132630281)"
FT /evidence="ECO:0000269|PubMed:1715570"
FT /id="VAR_004560"
FT VARIANT 220
FT /note="C -> Y (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9894878"
FT /id="VAR_015044"
FT VARIANT 221
FT /note="G -> C (in HLD1; dbSNP:rs132630286)"
FT /evidence="ECO:0000269|PubMed:7683951"
FT /id="VAR_004561"
FT VARIANT 224
FT /note="L -> I (probable disease-associated variant found in
FT Pelizaeus-Merzbacher disease/X-linked spastic paraplegia)"
FT /evidence="ECO:0000269|PubMed:9934976"
FT /id="VAR_015045"
FT VARIANT 224
FT /note="L -> P (in HLD1; dbSNP:rs132630283)"
FT /evidence="ECO:0000269|PubMed:1384324"
FT /id="VAR_004562"
FT VARIANT 225
FT /note="L -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046915"
FT VARIANT 226
FT /note="S -> P (in SPG2)"
FT /evidence="ECO:0000269|PubMed:8780101"
FT /id="VAR_015046"
FT VARIANT 228
FT /note="C -> Y (in HLD1; dbSNP:rs398123466)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015047"
FT VARIANT 234
FT /note="Q -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015048"
FT VARIANT 237
FT /note="F -> S (in SPG2; dbSNP:rs132630291)"
FT /evidence="ECO:0000269|PubMed:8956049"
FT /id="VAR_004563"
FT VARIANT 239
FT /note="L -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046916"
FT VARIANT 242
FT /note="A -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9143933,
FT ECO:0000269|PubMed:9894878"
FT /id="VAR_015049"
FT VARIANT 243
FT /note="A -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:11786921"
FT /id="VAR_046917"
FT VARIANT 243
FT /note="A -> V (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9482656"
FT /id="VAR_046918"
FT VARIANT 246
FT /note="G -> A (in HLD1; dbSNP:rs398123467)"
FT /evidence="ECO:0000269|PubMed:15712223"
FT /id="VAR_046919"
FT VARIANT 246
FT /note="G -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015050"
FT VARIANT 247
FT /note="A -> T (in HLD1; dbSNP:rs886043504)"
FT /evidence="ECO:0000269|PubMed:10425042"
FT /id="VAR_046920"
FT VARIANT 248
FT /note="A -> E (in HLD1)"
FT /evidence="ECO:0000269|PubMed:10417279"
FT /id="VAR_015051"
FT VARIANT 249
FT /note="A -> P (in HLD1)"
FT /evidence="ECO:0000269|PubMed:7541731"
FT /id="VAR_004565"
FT VARIANT 253
FT /note="S -> F (in HLD1)"
FT /evidence="ECO:0000269|PubMed:9788732"
FT /id="VAR_015052"
FT CONFLICT 140
FT /note="H -> T (in Ref. 7; AAA60117)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="Q -> D (in Ref. 3; AAA59565)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> I (in Ref. 3; AAA59565)"
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
