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 27-MAR-2024, entry version 186. 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>3.3.co;2-5; 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>3.3.co;2-8; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 111. DR IntAct; P60201; 104. DR MINT; P60201; -. DR STRING; 9606.ENSP00000481006; -. DR TCDB; 9.B.38.1.4; the myelin proteolipid protein (mplp) family. DR GlyCosmos; P60201; 1 site, 1 glycan. 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 EPD; P60201; -. DR jPOST; P60201; -. DR MassIVE; P60201; -. DR PaxDb; 9606-ENSP00000481006; -. DR PeptideAtlas; P60201; -. DR ProteomicsDB; 57188; -. [P60201-1] DR ProteomicsDB; 57189; -. [P60201-2] DR Antibodypedia; 582; 356 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 AGR; HGNC:9086; -. 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; NTWTTCN; -. DR OrthoDB; 3091734at2759; -. DR PhylomeDB; P60201; -. DR TreeFam; TF315162; -. DR PathwayCommons; P60201; -. DR SignaLink; P60201; -. DR SIGNOR; P60201; -. DR BioGRID-ORCS; 5354; 18 hits in 771 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 177 other cell types or tissues. DR ExpressionAtlas; P60201; baseline and differential. 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: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; 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 UCD-2DPAGE; P60201; -. DR Genevisible; P60201; HS. 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 (found in Pelizaeus-Merzbacher FT disease/X-linked spastic paraplegia; likely pathogenic)" 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 (found in Pelizaeus-Merzbacher FT disease/X-linked spastic paraplegia; likely pathogenic)" 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 //