Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Myelin proteolipid protein (PLP) (Lipophilin)

 MYPR_HUMAN              Reviewed;         277 AA.
P60201; P04400; P06905; Q502Y1; Q6FHZ6;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 145.
RecName: Full=Myelin proteolipid protein;
Short=PLP;
AltName: Full=Lipophilin;
Name=PLP1; Synonyms=PLP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3467339; DOI=10.1073/pnas.83.24.9807;
Diehl H.-J., Schaich M., Budzinski R.-M., Stoffel W.;
"Individual exons encode the integral membrane domains of human myelin
proteolipid protein.";
Proc. Natl. Acad. Sci. U.S.A. 83:9807-9811(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DM-20).
PubMed=2441695; DOI=10.1016/0006-291X(87)90580-8;
Simons R., Alon N., Riordan J.R.;
"Human myelin DM-20 proteolipid protein deletion defined by cDNA
sequence.";
Biochem. Biophys. Res. Commun. 146:666-671(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT HLD1 ARG-163.
PubMed=2479017; DOI=10.1073/pnas.86.20.8128;
Hudson L.D., Puckett C., Berndt J., Chan J., Gencic S.;
"Mutation of the proteolipid protein gene PLP in a human X chromosome-
linked myelin disorder.";
Proc. Natl. Acad. Sci. U.S.A. 86:8128-8131(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DM-20).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND DM-20).
TISSUE=Spinal cord, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-277.
PubMed=4041237;
Stoffel W., Giersiefen H., Hillen H., Schroeder W., Tunggal B.;
"Amino-acid sequence of human and bovine brain myelin proteolipid
protein (lipophilin) is completely conserved.";
Biol. Chem. Hoppe-Seyler 366:627-635(1985).
[9]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spinal cord;
PubMed=2449536; DOI=10.1002/jnr.490180303;
Kronquist K.E., Crandall B.F., Macklin W.B., Campagnoni A.T.;
"Expression of myelin proteins in the developing human spinal cord:
cloning and sequencing of human proteolipid protein cDNA.";
J. Neurosci. Res. 18:395-401(1987).
[10]
TOPOLOGY.
PubMed=1711121; DOI=10.1007/BF01868534;
Popot J.-L., Pham-Dinh D., Dautigny A.;
"Major myelin proteolipid: the 4-alpha-helix topology.";
J. Membr. Biol. 120:233-246(1991).
[11]
VARIANT HLD1 SER-217.
PubMed=2773936;
Gencic S., Abuelo D., Ambler M., Hudson L.D.;
"Pelizaeus-Merzbacher disease: an X-linked neurologic disorder of
myelin metabolism with a novel mutation in the gene encoding
proteolipid protein.";
Am. J. Hum. Genet. 45:435-442(1989).
[12]
VARIANT HLD1 LEU-15.
PubMed=2480601; DOI=10.1073/pnas.86.23.9427;
Trofatter J., Dlouhy S.R., Demyer W., Conneally P.M., Hodes M.E.;
"Pelizaeus-Merzbacher disease: tight linkage to proteolipid protein
gene exon variant.";
Proc. Natl. Acad. Sci. U.S.A. 86:9427-9430(1989).
[13]
VARIANT HLD1 ILE-156.
PubMed=1708672;
Weimbs T., Dick T., Stoffel W., Boltshauser E.;
"A point mutation at the X-chromosomal proteolipid protein locus in
Pelizaeus-Merzbacher disease leads to disruption of myelinogenesis.";
Biol. Chem. Hoppe-Seyler 371:1175-1183(1990).
[14]
VARIANT HLD1 ILE-156.
PubMed=1707231; DOI=10.1002/ajmg.1320380129;
Pratt V.M., Trofatter J.A., Schinzel A., Dlouhy S.R., Conneally P.M.,
Hodes M.E.;
"A new mutation in the proteolipid protein (PLP) gene in a German
family with Pelizaeus-Merzbacher disease.";
Am. J. Med. Genet. 38:136-139(1991).
[15]
VARIANT HLD1 PHE-219.
PubMed=1715570; DOI=10.1073/pnas.88.17.7562;
Pham-Dinh D., Popot J.-L., Bosepflug-Tanguy O., Landrieu P.,
Deleuze P., Boue J., Jolles P., Dautigny A.;
"Pelizaeus-Merzbacher disease: a valine to phenylalanine point
mutation in a putative extracellular loop of myelin proteolipid.";
Proc. Natl. Acad. Sci. U.S.A. 88:7562-7566(1991).
[16]
VARIANTS HLD1 ARG-74 AND HIS-203.
PubMed=1376966;
Doll R., Natowicz M.R., Schiffmann R., Smith F.I.;
"Molecular diagnostics for myelin proteolipid protein gene mutations
in Pelizaeus-Merzbacher disease.";
Am. J. Hum. Genet. 51:161-169(1992).
[17]
VARIANTS HLD1 PRO-182 AND PRO-224.
PubMed=1384324;
Strautnieks S., Rutland P., Winter R.M., Baraitser M., Malcolm S.;
"Pelizaeus-Merzbacher disease: detection of mutations Thr181-->Pro and
Leu223-->Pro in the proteolipid protein gene, and prenatal
diagnosis.";
Am. J. Hum. Genet. 51:871-878(1992).
[18]
VARIANT HLD1 GLU-166.
PubMed=7684886;
Pratt V.M., Kiefer J.R., Lahdetie J., Schleutker J., Hodes M.E.,
Dlouhy S.R.;
"Linkage of a new mutation in the proteolipid protein (PLP) gene to
Pelizaeus-Merzbacher disease (PMD) in a large Finnish kindred.";
Am. J. Hum. Genet. 52:1053-1056(1993).
[19]
VARIANT HLD1 SER-217.
PubMed=7679906;
Otterbach B., Stoffel W., Ramaekers V.;
"A novel mutation in the proteolipid protein gene leading to
Pelizaeus-Merzbacher disease.";
Biol. Chem. Hoppe-Seyler 374:75-83(1993).
[20]
VARIANT HLD1 CYS-221.
PubMed=7683951; DOI=10.1093/hmg/2.1.19;
Iwaki A., Muramoto T., Iwaki I., Furumi H., Dario-Deleon M.L.,
Tateishi J., Fukumaki Y.;
"A missense mutation in the proteolipid protein gene responsible for
Pelizaeus-Merzbacher disease in a Japanese family.";
Hum. Mol. Genet. 2:19-22(1993).
[21]
VARIANT HLD1 SER-216.
PubMed=8037216;
Pratt V.M., Boyadjiev S., Dlouhy S.R., Silver K., der Kaloustian V.M.,
Hodes M.E.;
"Comparison of statistics for candidate-gene association studies using
cases and parents.";
Am. J. Hum. Genet. 55:402-409(1994).
[22]
VARIANT SPG2 TYR-140.
PubMed=8012387; DOI=10.1038/ng0394-257;
Saugier-Veber P., Munnich A., Bonneau D., Rozet J.-M., le Merrer M.,
Gil R., Boespflug-Tanguy O.;
"X-linked spastic paraplegia and Pelizaeus-Merzbacher disease are
allelic disorders at the proteolipid protein locus.";
Nat. Genet. 6:257-262(1994).
[23]
VARIANT SPG2 THR-187.
PubMed=7522741; DOI=10.1038/ng0794-351;
Kobayashi H., Hoffman E.P., Marks H.G.;
"The rumpshaker mutation in spastic paraplegia.";
Nat. Genet. 7:351-352(1994).
[24]
VARIANT HLD1 116-VAL--LEU-165 DEL.
PubMed=7539213; DOI=10.1002/ajmg.1320550404;
Kleindorfer D.O., Dlouhy S.R., Pratt V.M., Jones M.C., Trofatter J.A.,
Hodes M.E.;
"In-frame deletion in the proteolipid protein gene of a family with
Pelizaeus-Merzbacher disease.";
Am. J. Med. Genet. 55:405-407(1995).
[25]
VARIANT HLD1 ILE-43.
PubMed=7573159; DOI=10.1002/ajmg.1320580114;
Pratt V.M., Boyadjiev S., Green K., Hodes M.E., Dlouhy S.R.;
"Pelizaeus-Merzbacher disease caused by a de novo mutation that
originated in exon 2 of the maternal great-grandfather of the
propositus.";
Am. J. Med. Genet. 58:70-73(1995).
[26]
VARIANT HLD1 PRO-249.
PubMed=7541731;
Pratt V.M., Dlouhy S.R., Hodes M.E.;
"Pelizaeus-Merzbacher disease: a point mutation in exon 6 of the
proteolipid protein (PLP) gene.";
Clin. Genet. 47:99-100(1995).
[27]
VARIANT HLD1 ASN-151.
PubMed=7531827; DOI=10.1212/WNL.45.2.394;
Pratt V.M., Naidu S., Dlouhy S.R., Marks H.G., Hodes M.E.;
"A novel mutation in exon 3 of the proteolipid protein gene in
Pelizaeus-Merzbacher disease.";
Neurology 45:394-395(1995).
[28]
VARIANT SPG2 SER-237.
PubMed=8956049;
DOI=10.1002/(SICI)1098-1004(1996)8:4<384::AID-HUMU17>3.0.CO;2-Z;
Donnelly A., Colley A., Crimmins D., Mulley J.;
"A novel mutation in exon 6 (F236S) of the proteolipid protein gene is
associated with spastic paraplegia.";
Hum. Mutat. 8:384-385(1996).
[29]
VARIANT SPG2 PRO-226.
PubMed=8780101; DOI=10.1212/WNL.46.4.1112;
Cambi F., Tang X.M., Cordray P., Fain P.R., Keppen L.D., Barker D.F.;
"Refined genetic mapping and proteolipid protein mutation analysis in
X-linked pure hereditary spastic paraplegia.";
Neurology 46:1112-1117(1996).
[30]
VARIANT HLD1 LYS-116.
PubMed=8909455; DOI=10.1212/WNL.47.5.1333;
Nance M.A., Boyadjiev S., Pratt V.M., Taylor S., Hodes M.E.,
Dlouhy S.R.;
"Adult-onset neurodegenerative disorder due to proteolipid protein
gene mutation in the mother of a man with Pelizaeus-Merzbacher
disease.";
Neurology 47:1333-1335(1996).
[31]
VARIANT HLD1 PRO-242.
PubMed=9143933;
DOI=10.1002/(SICI)1098-1004(1997)9:5<475::AID-HUMU19>3.0.CO;2-#;
Kawanishi C., Osaka H., Owa K., Inoue K., Miyakawa T., Onishi H.,
Yamada Y., Suzuki K., Kimura S., Kosaka K.;
"A new missense mutation in exon 6 of the proteolipid protein gene in
a patient with Pelizaeus-Merzbacher disease.";
Hum. Mutat. 9:475-476(1997).
[32]
VARIANTS HLD1 ASP-209 AND LEU-211.
PubMed=9008538; DOI=10.1212/WNL.48.1.283;
Inoue K., Osaka H., Kawanishi C., Sugiyama N., Ishii M., Sugita K.,
Yamada Y., Kosaka K.;
"Mutations in the proteolipid protein gene in Japanese families with
Pelizaeus-Merzbacher disease.";
Neurology 48:283-285(1997).
[33]
VARIANT HLD1 VAL-243.
PubMed=9482656;
DOI=10.1002/(SICI)1096-8628(19980203)75:4<439::AID-AJMG19>3.3.CO;2-5;
Yamamoto T., Nanba E., Zhang H., Sasaki M., Komaki H., Takeshita K.;
"Jimpy(msd) mouse mutation and connatal Pelizaeus-Merzbacher
disease.";
Am. J. Med. Genet. 75:439-440(1998).
[34]
VARIANT SPG2 PHE-170.
PubMed=9489796;
DOI=10.1002/(SICI)1096-8628(19980217)75:5<516::AID-AJMG11>3.0.CO;2-N;
Hodes M.E., Hadjisavvas A., Butler I.J., Aydanian A., Dlouhy S.R.;
"X-linked spastic paraplegia due to a mutation (C506T; Ser169Phe) in
exon 4 of the proteolipid protein gene (PLP).";
Am. J. Med. Genet. 75:516-517(1998).
[35]
VARIANT HLD1 PHE-253.
PubMed=9788732;
Hodes M.E., Aydanian A., Dlouhy S.R., Whelan D.T., Heshka T.,
Ronen G.;
"A de novo mutation (C755T; Ser252Phe) in exon 6 of the proteolipid
protein gene responsible for Pelizaeus-Merzbacher disease.";
Clin. Genet. 54:248-249(1998).
[36]
VARIANT HLD1 VAL-203.
PubMed=9747038; DOI=10.1007/s100380050072;
Nagao M., Kadowaki J.;
"Connatal Pelizaeus-Merzbacher disease: a missense mutation in exon 4
of the proteolipid protein 'PLP' gene.";
J. Hum. Genet. 43:206-208(1998).
[37]
VARIANTS HLD1 VAL-32; ALA-172; GLY-205 AND CYS-207.
PubMed=9633722; DOI=10.1212/WNL.50.6.1749;
Sistermans E.A., de Coo R.F.M., De Wijs I.J., Van Oost B.A.;
"Duplication of the proteolipid protein gene is the major cause of
Pelizaeus-Merzbacher disease.";
Neurology 50:1749-1754(1998).
[38]
VARIANTS HLD1 TYR-35; THR-39; CYS-60; ARG-74; ARG-169; CYS-175;
CYS-181; ASN-183; ASN-203; GLU-203; GLY-203; HIS-210; ARG-212;
SER-216; TYR-228; PRO-234; GLU-246 AND GLU-248.
PubMed=10417279; DOI=10.1086/302483;
Mimault C., Giraud G., Courtois V., Cailloux F., Boire J.Y.,
Dastugue B., Boespflug-Tanguy O., Baethmann M., Bertini E.,
Cuisset J.M., Gaertner J., Hanefeld F., Kohlschutter A., Landrieu P.,
Mayer M., Peudenier S., Rodriguez D., Rating D., Surtees R., Uziel G.,
Vallee L., Voit T.;
"Proteolipoprotein gene analysis in 82 patients with sporadic
Pelizaeus-Merzbacher Disease: duplications, the major cause of the
disease, originate more frequently in male germ cells, but point
mutations do not.";
Am. J. Hum. Genet. 65:360-369(1999).
[39]
VARIANT HLD1 PRO-46, AND VARIANTS GLY-166 AND ILE-224.
PubMed=9934976;
DOI=10.1002/(SICI)1096-8628(19990115)82:2<132::AID-AJMG6>3.0.CO;2-4;
Hodes M.E., Zimmerman A.W., Aydanian A., Naidu S., Miller N.R.,
Garcia Oller J.L., Barker B., Aleck K.A., Hurley T.D., Dlouhy S.R.;
"Different mutations in the same codon of the proteolipid protein
gene, PLP, may help in correlating genotype with phenotype in
Pelizaeus-Merzbacher disease/X-linked spastic paraplegia (PMD/SPG2).";
Am. J. Med. Genet. 82:132-139(1999).
[40]
VARIANTS HLD1 ARG-46; ASP-209; LEU-211; TYR-220 AND PRO-242.
PubMed=9894878;
DOI=10.1002/1531-8249(199901)45:1<59::AID-ART11>3.0.CO;2-3;
Osaka H., Kawanishi C., Inoue K., Onishi H., Kobayashi T.,
Sugiyama N., Kosaka K., Nezu A., Fujii K., Sugita K., Kodama K.,
Murayama K., Murayama S., Kanazawa I., Kimura S.;
"Pelizaeus-Merzbacher disease: three novel mutations and implication
for locus heterogeneity.";
Ann. Neurol. 45:59-64(1999).
[41]
VARIANT SPG2 TYR-148.
PubMed=10319897;
DOI=10.1002/1531-8249(199905)45:5<680::AID-ANA23>3.3.CO;2-8;
Sivakumar K., Sambuughin N., Selenge B., Nagle J.W., Baasanjav D.,
Hudson L.D., Goldfarb L.G.;
"Novel exon 3B proteolipid protein gene mutation causing late-onset
spastic paraplegia type 2 with variable penetrance in female family
members.";
Ann. Neurol. 45:680-683(1999).
[42]
VARIANT HLD1 THR-247.
PubMed=10425042;
DOI=10.1002/(SICI)1098-1004(1999)14:2<182::AID-HUMU12>3.0.CO;2-Y;
Yamamoto T., Nanba E.;
"A novel mutation (A246T) in exon 6 of the proteolipid protein gene
associated with connatal Pelizaeus-Merzbacher disease.";
Hum. Mutat. 14:182-182(1999).
[43]
VARIANTS HLD1 PRO-31; LEU-32; SER-51; ARG-74; CYS-181; GLU-203;
ARG-212 AND ALA-216, AND VARIANT SPG2 TYR-130.
PubMed=11093273; DOI=10.1038/sj.ejhg.5200537;
Cailloux F., Gauthier-Barichard F., Mimault C., Isabelle V.,
Courtois V., Giraud G., Dastugue B., Boespflug-Tanguy O.,
Baethmann M., Bertini E., Cuisset J.M., Gaertner J., Hanefeld F.,
Kohlschutter A., Landrieu P., Mayer M., Peudenier S., Rodriguez D.,
Rating D., Surtees R., Uziel G., Vallee L., Voit T.;
"Genotype-phenotype correlation in inherited brain myelination defects
due to proteolipid protein gene mutations.";
Eur. J. Hum. Genet. 8:837-845(2000).
[44]
VARIANT HLD1 GLU-243.
PubMed=11786921;
Seeman P., Paderova K., Benes V. Jr., Sistermans E.A.;
"A severe connatal form of Pelizaeus Merzbacher disease in a Czech boy
caused by a novel mutation (725C>A, Ala242Glu) at the 'jimpy(msd)
codon' in the PLP gene.";
Int. J. Mol. Med. 9:125-129(2002).
[45]
VARIANT SPG2 LEU-216.
PubMed=15450775; DOI=10.1016/j.jns.2004.05.015;
Lee E.S., Moon H.K., Park Y.H., Garbern J., Hobson G.M.;
"A case of complicated spastic paraplegia 2 due to a point mutation in
the proteolipid protein 1 gene.";
J. Neurol. Sci. 224:83-87(2004).
[46]
VARIANTS HLD1 TYR-33; ARG-35; THR-39; PRO-46; CYS-50; PRO-76; TYR-148;
GLU-162; PRO-170; SER-173; PRO-225; PRO-239 AND ALA-246.
PubMed=15712223; DOI=10.1002/humu.9314;
Huebner C.A., Orth U., Senning A., Steglich C., Kohlschuetter A.,
Korinthenberg R., Gal A.;
"Seventeen novel PLP1 mutations in patients with Pelizaeus-Merzbacher
disease.";
Hum. Mutat. 25:321-322(2005).
[47]
VARIANT SPG2 TRP-137.
PubMed=17438221; DOI=10.1212/01.wnl.0000259522.49388.53;
Gorman M.P., Golomb M.R., Walsh L.E., Hobson G.M., Garbern J.Y.,
Kinkel R.P., Darras B.T., Urion D.K., Eksioglu Y.Z.;
"Steroid-responsive neurologic relapses in a child with a proteolipid
protein-1 mutation.";
Neurology 68:1305-1307(2007).
[48]
VARIANT SPG2 PRO-30, CHARACTERIZATION OF VARIANT SPG2 PRO-30, AND
SUBCELLULAR LOCATION.
PubMed=24103481; DOI=10.1016/j.gene.2013.09.076;
Noetzli L., Sanz P.G., Brodsky G.L., Hinckley J.D., Giugni J.C.,
Giannaula R.J., Gonzalez-Alegre P., Di Paola J.;
"A novel mutation in PLP1 causes severe hereditary spastic paraplegia
type 2.";
Gene 533:447-450(2014).
-!- FUNCTION: This is the major myelin protein from the central
nervous system. It plays an important role in the formation or
maintenance of the multilamellar structure of myelin.
-!- INTERACTION:
O43889-2:CREB3; NbExp=3; IntAct=EBI-12188331, EBI-625022;
Q96BA8:CREB3L1; NbExp=5; IntAct=EBI-12188331, EBI-6942903;
Q16849-3:PTPRN; NbExp=5; IntAct=EBI-12188331, EBI-10200782;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24103481};
Multi-pass membrane protein {ECO:0000269|PubMed:24103481}. Myelin
membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in internodal
regions, at paranodal axoglial junction and Schmidt-Lanterman
incisures of myelin sheat. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P60201-1; Sequence=Displayed;
Name=DM-20;
IsoId=P60201-2; Sequence=VSP_003325;
-!- DISEASE: Leukodystrophy, hypomyelinating, 1 (HLD1) [MIM:312080]: A
X-linked recessive disorder of the central nervous system in which
myelin is not formed properly. Clinically characterized by
nystagmus, spastic quadriplegia, ataxia, and developmental delay.
{ECO:0000269|PubMed:10417279, ECO:0000269|PubMed:10425042,
ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:11786921,
ECO:0000269|PubMed:1376966, ECO:0000269|PubMed:1384324,
ECO:0000269|PubMed:15712223, ECO:0000269|PubMed:1707231,
ECO:0000269|PubMed:1708672, ECO:0000269|PubMed:1715570,
ECO:0000269|PubMed:2479017, ECO:0000269|PubMed:2480601,
ECO:0000269|PubMed:2773936, ECO:0000269|PubMed:7531827,
ECO:0000269|PubMed:7539213, ECO:0000269|PubMed:7541731,
ECO:0000269|PubMed:7573159, ECO:0000269|PubMed:7679906,
ECO:0000269|PubMed:7683951, ECO:0000269|PubMed:7684886,
ECO:0000269|PubMed:8037216, ECO:0000269|PubMed:8909455,
ECO:0000269|PubMed:9008538, ECO:0000269|PubMed:9143933,
ECO:0000269|PubMed:9482656, ECO:0000269|PubMed:9633722,
ECO:0000269|PubMed:9747038, ECO:0000269|PubMed:9788732,
ECO:0000269|PubMed:9894878, ECO:0000269|PubMed:9934976}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Spastic paraplegia 2, X-linked (SPG2) [MIM:312920]: A
form of spastic paraplegia, a neurodegenerative disorder
characterized by a slow, gradual, progressive weakness and
spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG2 is characterized by spastic gait and hyperreflexia.
In some patients, complicating features include nystagmus,
dysarthria, sensory disturbance, mental retardation, optic
atrophy. {ECO:0000269|PubMed:10319897,
ECO:0000269|PubMed:11093273, ECO:0000269|PubMed:15450775,
ECO:0000269|PubMed:17438221, ECO:0000269|PubMed:24103481,
ECO:0000269|PubMed:7522741, ECO:0000269|PubMed:8012387,
ECO:0000269|PubMed:8780101, ECO:0000269|PubMed:8956049,
ECO:0000269|PubMed:9489796}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the myelin proteolipid protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
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};
Sequence=AAD13880.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M15032; AAA60350.1; ALT_SEQ; Genomic_DNA.
EMBL; M15026; AAA60350.1; JOINED; Genomic_DNA.
EMBL; M15027; AAA60350.1; JOINED; Genomic_DNA.
EMBL; M15028; AAA60350.1; JOINED; Genomic_DNA.
EMBL; M15029; AAA60350.1; JOINED; Genomic_DNA.
EMBL; M15031; AAA60350.1; JOINED; Genomic_DNA.
EMBL; AJ006976; CAA07364.1; -; Genomic_DNA.
EMBL; M54927; AAA59565.1; -; mRNA.
EMBL; M17085; AAA60118.1; -; mRNA.
EMBL; M27110; AAA60117.1; -; mRNA.
EMBL; CR536542; CAG38779.1; -; mRNA.
EMBL; Z73964; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471190; EAW54690.1; -; Genomic_DNA.
EMBL; BC002665; AAH02665.1; -; mRNA.
EMBL; BC095452; AAH95452.1; -; mRNA.
EMBL; D13320; BAA02577.1; -; Genomic_DNA.
EMBL; S55837; AAD13880.1; ALT_SEQ; Genomic_DNA.
CCDS; CCDS14513.1; -. [P60201-1]
CCDS; CCDS14514.1; -. [P60201-2]
PIR; A26665; MPHUPL.
RefSeq; NP_000524.3; NM_000533.4. [P60201-1]
RefSeq; NP_001122306.1; NM_001128834.2. [P60201-1]
RefSeq; NP_001291933.1; NM_001305004.1.
RefSeq; NP_955772.1; NM_199478.2. [P60201-2]
UniGene; Hs.1787; -.
PDB; 2XPG; X-ray; 2.60 A; C=45-53.
PDBsum; 2XPG; -.
ProteinModelPortal; P60201; -.
SMR; P60201; -.
BioGrid; 111368; 21.
IntAct; P60201; 27.
STRING; 9606.ENSP00000305152; -.
iPTMnet; P60201; -.
PhosphoSitePlus; P60201; -.
SwissPalm; P60201; -.
BioMuta; PLP1; -.
DMDM; 41393531; -.
UCD-2DPAGE; P60201; -.
EPD; P60201; -.
PaxDb; P60201; -.
PeptideAtlas; P60201; -.
PRIDE; P60201; -.
DNASU; 5354; -.
Ensembl; ENST00000612423; ENSP00000481006; ENSG00000123560. [P60201-1]
Ensembl; ENST00000619236; ENSP00000477619; ENSG00000123560. [P60201-2]
Ensembl; ENST00000621218; ENSP00000484450; ENSG00000123560. [P60201-1]
GeneID; 5354; -.
KEGG; hsa:5354; -.
UCSC; uc033epn.2; human. [P60201-1]
CTD; 5354; -.
DisGeNET; 5354; -.
EuPathDB; HostDB:ENSG00000123560.13; -.
GeneCards; PLP1; -.
GeneReviews; PLP1; -.
HGNC; HGNC:9086; PLP1.
HPA; HPA004128; -.
MalaCards; PLP1; -.
MIM; 300401; gene.
MIM; 312080; phenotype.
MIM; 312920; phenotype.
neXtProt; NX_P60201; -.
OpenTargets; ENSG00000123560; -.
Orphanet; 280234; Null syndrome.
Orphanet; 280229; Pelizaeus-Merzbacher disease in female carriers.
Orphanet; 280219; Pelizaeus-Merzbacher disease, classic form.
Orphanet; 280210; Pelizaeus-Merzbacher disease, connatal form.
Orphanet; 280224; Pelizaeus-Merzbacher disease, transitional form.
Orphanet; 99015; Spastic paraplegia type 2.
PharmGKB; PA33414; -.
eggNOG; KOG4800; Eukaryota.
eggNOG; ENOG4110EPW; LUCA.
GeneTree; ENSGT00390000006915; -.
HOGENOM; HOG000231338; -.
HOVERGEN; HBG000096; -.
InParanoid; P60201; -.
KO; K17271; -.
OMA; YCIVLLA; -.
OrthoDB; EOG091G0IM5; -.
PhylomeDB; P60201; -.
TreeFam; TF315162; -.
ChiTaRS; PLP1; human.
GeneWiki; Proteolipid_protein_1; -.
GenomeRNAi; 5354; -.
PRO; PR:P60201; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000123560; -.
CleanEx; HS_PLP1; -.
ExpressionAtlas; P60201; baseline and differential.
Genevisible; P60201; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043209; C:myelin sheath; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019911; F:structural constituent of myelin sheath; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0061564; P:axon development; IEA:Ensembl.
GO; GO:0008366; P:axon ensheathment; TAS:ProtInc.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
InterPro; IPR001614; Myelin_PLP.
InterPro; IPR018237; Myelin_PLP_CS.
PANTHER; PTHR11683; PTHR11683; 1.
Pfam; PF01275; Myelin_PLP; 1.
PRINTS; PR00214; MYELINPLP.
SMART; SM00002; PLP; 1.
PROSITE; PS00575; MYELIN_PLP_1; 1.
PROSITE; PS01004; MYELIN_PLP_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Hereditary spastic paraplegia; Leukodystrophy; Lipoprotein; Membrane;
Neurodegeneration; Palmitate; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:4041237}.
CHAIN 2 277 Myelin proteolipid protein.
/FTId=PRO_0000159005.
TOPO_DOM 2 9 Cytoplasmic.
{ECO:0000305|PubMed:1711121}.
TRANSMEM 10 36 Helical; Name=1. {ECO:0000305}.
TOPO_DOM 37 63 Extracellular.
{ECO:0000305|PubMed:1711121}.
TRANSMEM 64 88 Helical; Name=2. {ECO:0000305}.
TOPO_DOM 89 151 Cytoplasmic.
{ECO:0000305|PubMed:1711121}.
TRANSMEM 152 177 Helical; Name=3. {ECO:0000305}.
TOPO_DOM 178 233 Extracellular.
{ECO:0000305|PubMed:1711121}.
TRANSMEM 234 260 Helical; Name=4. {ECO:0000305}.
TOPO_DOM 261 277 Cytoplasmic.
{ECO:0000305|PubMed:1711121}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000250|UniProtKB:P60203}.
MOD_RES 116 116 Phosphothreonine.
{ECO:0000250|UniProtKB:P60203}.
MOD_RES 118 118 Phosphothreonine.
{ECO:0000250|UniProtKB:P60203}.
LIPID 6 6 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 7 7 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 10 10 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 109 109 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 139 139 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 141 141 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 199 199 O-palmitoyl serine. {ECO:0000250}.
DISULFID 184 228 {ECO:0000250}.
DISULFID 201 220 {ECO:0000250}.
VAR_SEQ 117 151 Missing (in isoform DM-20).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2441695,
ECO:0000303|Ref.4}.
/FTId=VSP_003325.
VARIANT 15 15 P -> L (in HLD1; dbSNP:rs11543022).
{ECO:0000269|PubMed:2480601}.
/FTId=VAR_004546.
VARIANT 30 30 A -> P (in SPG2; partially retained in
the endoplasmic reticulum; does not
induce unfolded protein response).
{ECO:0000269|PubMed:24103481}.
/FTId=VAR_070667.
VARIANT 31 31 L -> P (in HLD1).
{ECO:0000269|PubMed:11093273}.
/FTId=VAR_015014.
VARIANT 32 32 F -> L (in HLD1).
{ECO:0000269|PubMed:11093273}.
/FTId=VAR_015015.
VARIANT 32 32 F -> V (in HLD1).
{ECO:0000269|PubMed:9633722}.
/FTId=VAR_015016.
VARIANT 33 33 C -> Y (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046906.
VARIANT 35 35 C -> R (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046907.
VARIANT 35 35 C -> Y (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015017.
VARIANT 39 39 A -> T (in HLD1).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:15712223}.
/FTId=VAR_015018.
VARIANT 43 43 T -> I (in HLD1; dbSNP:rs132630289).
{ECO:0000269|PubMed:7573159}.
/FTId=VAR_004547.
VARIANT 46 46 L -> P (in HLD1).
{ECO:0000269|PubMed:15712223,
ECO:0000269|PubMed:9934976}.
/FTId=VAR_015019.
VARIANT 46 46 L -> R (in HLD1).
{ECO:0000269|PubMed:9894878}.
/FTId=VAR_015020.
VARIANT 50 50 Y -> C (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046908.
VARIANT 51 51 F -> S (in HLD1).
{ECO:0000269|PubMed:11093273}.
/FTId=VAR_015021.
VARIANT 60 60 Y -> C (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015022.
VARIANT 74 74 G -> R (in HLD1; dbSNP:rs132630285).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:11093273,
ECO:0000269|PubMed:1376966}.
/FTId=VAR_004548.
VARIANT 76 76 A -> P (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046909.
VARIANT 116 116 T -> K (in HLD1).
{ECO:0000269|PubMed:8909455}.
/FTId=VAR_015023.
VARIANT 117 165 Missing (in HLD1).
/FTId=VAR_004550.
VARIANT 130 130 H -> Y (in SPG2; dbSNP:rs878853076).
{ECO:0000269|PubMed:11093273}.
/FTId=VAR_015024.
VARIANT 137 137 R -> W (in SPG2; dbSNP:rs132630295).
{ECO:0000269|PubMed:17438221}.
/FTId=VAR_046910.
VARIANT 140 140 H -> Y (in SPG2; dbSNP:rs132630287).
{ECO:0000269|PubMed:8012387}.
/FTId=VAR_004551.
VARIANT 148 148 H -> Y (in HLD1 and SPG2).
{ECO:0000269|PubMed:10319897,
ECO:0000269|PubMed:15712223}.
/FTId=VAR_015025.
VARIANT 151 151 K -> N (in HLD1).
{ECO:0000269|PubMed:7531827}.
/FTId=VAR_015026.
VARIANT 156 156 T -> I (in HLD1; dbSNP:rs132630280).
{ECO:0000269|PubMed:1707231,
ECO:0000269|PubMed:1708672}.
/FTId=VAR_004552.
VARIANT 162 162 V -> E (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046911.
VARIANT 163 163 W -> R (in HLD1; dbSNP:rs132630279).
{ECO:0000269|PubMed:2479017}.
/FTId=VAR_004553.
VARIANT 166 166 V -> E (in HLD1).
{ECO:0000269|PubMed:7684886}.
/FTId=VAR_004554.
VARIANT 166 166 V -> G (probable disease-associated
mutation found in Pelizaeus-Merzbacher
disease/X-linked spastic paraplegia).
{ECO:0000269|PubMed:9934976}.
/FTId=VAR_015027.
VARIANT 169 169 C -> R (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015028.
VARIANT 170 170 S -> F (in SPG2; dbSNP:rs132630294).
{ECO:0000269|PubMed:9489796}.
/FTId=VAR_015029.
VARIANT 170 170 S -> P (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046912.
VARIANT 172 172 V -> A (in HLD1).
{ECO:0000269|PubMed:9633722}.
/FTId=VAR_015030.
VARIANT 173 173 P -> S (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046913.
VARIANT 175 175 Y -> C (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015031.
VARIANT 181 181 W -> C (in HLD1).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:11093273}.
/FTId=VAR_015032.
VARIANT 182 182 T -> P (in HLD1; dbSNP:rs132630282).
{ECO:0000269|PubMed:1384324}.
/FTId=VAR_004555.
VARIANT 183 183 T -> N (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015033.
VARIANT 187 187 I -> T (in SPG2; dbSNP:rs132630288).
{ECO:0000269|PubMed:7522741}.
/FTId=VAR_004556.
VARIANT 203 203 D -> E (in HLD1).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:11093273}.
/FTId=VAR_015034.
VARIANT 203 203 D -> G (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015035.
VARIANT 203 203 D -> H (in HLD1; dbSNP:rs132630284).
{ECO:0000269|PubMed:1376966}.
/FTId=VAR_004557.
VARIANT 203 203 D -> N (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015036.
VARIANT 203 203 D -> V (in HLD1).
{ECO:0000269|PubMed:9747038}.
/FTId=VAR_007956.
VARIANT 205 205 R -> G (in HLD1).
{ECO:0000269|PubMed:9633722}.
/FTId=VAR_015037.
VARIANT 207 207 Y -> C (in HLD1).
{ECO:0000269|PubMed:9633722}.
/FTId=VAR_015038.
VARIANT 209 209 V -> D (in HLD1).
{ECO:0000269|PubMed:9008538,
ECO:0000269|PubMed:9894878}.
/FTId=VAR_015039.
VARIANT 210 210 L -> H (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015040.
VARIANT 211 211 P -> L (in HLD1).
{ECO:0000269|PubMed:9008538,
ECO:0000269|PubMed:9894878}.
/FTId=VAR_015041.
VARIANT 212 212 W -> R (in HLD1).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:11093273}.
/FTId=VAR_015042.
VARIANT 216 216 P -> A (in HLD1).
{ECO:0000269|PubMed:11093273}.
/FTId=VAR_015043.
VARIANT 216 216 P -> L (in SPG2).
{ECO:0000269|PubMed:15450775}.
/FTId=VAR_046914.
VARIANT 216 216 P -> S (in HLD1; dbSNP:rs132630278).
{ECO:0000269|PubMed:10417279,
ECO:0000269|PubMed:8037216}.
/FTId=VAR_004558.
VARIANT 217 217 G -> S (in HLD1).
{ECO:0000269|PubMed:2773936,
ECO:0000269|PubMed:7679906}.
/FTId=VAR_004559.
VARIANT 219 219 V -> F (in HLD1; dbSNP:rs132630281).
{ECO:0000269|PubMed:1715570}.
/FTId=VAR_004560.
VARIANT 220 220 C -> Y (in HLD1).
{ECO:0000269|PubMed:9894878}.
/FTId=VAR_015044.
VARIANT 221 221 G -> C (in HLD1; dbSNP:rs132630286).
{ECO:0000269|PubMed:7683951}.
/FTId=VAR_004561.
VARIANT 224 224 L -> I (probable disease-associated
mutation found in Pelizaeus-Merzbacher
disease/X-linked spastic paraplegia).
{ECO:0000269|PubMed:9934976}.
/FTId=VAR_015045.
VARIANT 224 224 L -> P (in HLD1; dbSNP:rs132630283).
{ECO:0000269|PubMed:1384324}.
/FTId=VAR_004562.
VARIANT 225 225 L -> P (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046915.
VARIANT 226 226 S -> P (in SPG2).
{ECO:0000269|PubMed:8780101}.
/FTId=VAR_015046.
VARIANT 228 228 C -> Y (in HLD1; dbSNP:rs398123466).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015047.
VARIANT 234 234 Q -> P (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015048.
VARIANT 237 237 F -> S (in SPG2; dbSNP:rs132630291).
{ECO:0000269|PubMed:8956049}.
/FTId=VAR_004563.
VARIANT 239 239 L -> P (in HLD1).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046916.
VARIANT 242 242 A -> P (in HLD1).
{ECO:0000269|PubMed:9143933,
ECO:0000269|PubMed:9894878}.
/FTId=VAR_015049.
VARIANT 243 243 A -> E (in HLD1).
{ECO:0000269|PubMed:11786921}.
/FTId=VAR_046917.
VARIANT 243 243 A -> V (in HLD1).
{ECO:0000269|PubMed:9482656}.
/FTId=VAR_046918.
VARIANT 246 246 G -> A (in HLD1; dbSNP:rs398123467).
{ECO:0000269|PubMed:15712223}.
/FTId=VAR_046919.
VARIANT 246 246 G -> E (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015050.
VARIANT 247 247 A -> T (in HLD1).
{ECO:0000269|PubMed:10425042}.
/FTId=VAR_046920.
VARIANT 248 248 A -> E (in HLD1).
{ECO:0000269|PubMed:10417279}.
/FTId=VAR_015051.
VARIANT 249 249 A -> P (in HLD1).
{ECO:0000269|PubMed:7541731}.
/FTId=VAR_004565.
VARIANT 253 253 S -> F (in HLD1).
{ECO:0000269|PubMed:9788732}.
/FTId=VAR_015052.
CONFLICT 140 140 H -> T (in Ref. 7; AAA60117).
{ECO:0000305}.
CONFLICT 185 185 Q -> D (in Ref. 3; AAA59565).
{ECO:0000305}.
CONFLICT 213 213 N -> I (in Ref. 3; AAA59565).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
E0417p ELISA kit Lipophilin,Myelin proteolipid protein,Pig,PLP,PLP,PLP1,Sus scrofa 96T
E0417p ELISA Lipophilin,Myelin proteolipid protein,Pig,PLP,PLP,PLP1,Sus scrofa 96T
U0417p CLIA Lipophilin,Myelin proteolipid protein,Pig,PLP,PLP,PLP1,Sus scrofa 96T
E0417r ELISA kit Lipophilin,Myelin proteolipid protein,PLP,Plp,Plp1,Rat,Rattus norvegicus 96T
18-783-77953 RABBIT ANTI HUMAN MYELIN PROTEOLIPID PROTEIN - PLP; PLP; Lipophilin Polyclonal 1 ml
E0417r ELISA Lipophilin,Myelin proteolipid protein,PLP,Plp,Plp1,Rat,Rattus norvegicus 96T
E0417m ELISA Lipophilin,Mouse,Mus musculus,Myelin proteolipid protein,PLP,Plp,Plp1 96T
E0417b ELISA Bos taurus,Bovine,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
U0417m CLIA Lipophilin,Mouse,Mus musculus,Myelin proteolipid protein,PLP,Plp,Plp1 96T
U0417b CLIA Bos taurus,Bovine,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
U0417r CLIA Lipophilin,Myelin proteolipid protein,PLP,Plp,Plp1,Rat,Rattus norvegicus 96T
E0417b ELISA kit Bos taurus,Bovine,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
E0417m ELISA kit Lipophilin,Mouse,Mus musculus,Myelin proteolipid protein,PLP,Plp,Plp1 96T
E0417Rb ELISA kit Lipophilin,Myelin proteolipid protein,Oryctolagus cuniculus,PLP,PLP,PLP1,Rabbit 96T
E0417Rb ELISA Lipophilin,Myelin proteolipid protein,Oryctolagus cuniculus,PLP,PLP,PLP1,Rabbit 96T
E0417h ELISA kit Homo sapiens,Human,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
E0417h ELISA Homo sapiens,Human,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
U0417Rb CLIA Lipophilin,Myelin proteolipid protein,Oryctolagus cuniculus,PLP,PLP,PLP1,Rabbit 96T
06-271-83001 [Ser140] Myelin Proteolipid Protein (Depalmitoylated) (139-151) Human Bovine Dog Mouse Rat - PLP; Lipophilin 0.5 mg
06-271-83001 [Ser140] Myelin Proteolipid Protein (Depalmitoylated) (139-151) Human Bovine Dog Mouse Rat - PLP; Lipophilin 1 mg
U0417h CLIA Homo sapiens,Human,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
U0417c CLIA Chicken,Gallus gallus,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
E0417c ELISA kit Chicken,Gallus gallus,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
E0417c ELISA Chicken,Gallus gallus,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T
E0417c ELISA kit Canis familiaris,Canis lupus familiaris,Dog,Lipophilin,Myelin proteolipid protein,PLP,PLP,PLP1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur