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Niemann-Pick C1 protein

 NPC1_HUMAN              Reviewed;        1278 AA.
O15118; B4DET3; Q9P130;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
27-SEP-2017, entry version 173.
RecName: Full=Niemann-Pick C1 protein;
Flags: Precursor;
Name=NPC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ILE-642, AND VARIANTS
NPC1.
PubMed=9211849; DOI=10.1126/science.277.5323.228;
Carstea E.D., Morris J.A., Coleman K.G., Loftus S.K., Zhang D.,
Cummings C., Gu J., Rosenfeld M.A., Pavan W.J., Krizman D.B.,
Nagle J., Polymeropoulos M.H., Sturley S.L., Ioannou Y.A.,
Higgins M.E., Comly M., Cooney A., Brown A., Kaneski C.R.,
Blanchette-Mackie E.J., Dwyer N.K., Neufeld E.B., Chang T.-Y.,
Liscum L., Strauss J.F. III, Ohno K., Zeigler M., Carmi R., Sokol J.,
Markie D., O'Neill R.R., van Diggelen O.P., Elleder M.,
Patterson M.C., Brady R.O., Vanier M.T., Pentchev P.G., Tagle D.A.;
"Niemann-Pick C1 disease gene: homology to mediators of cholesterol
homeostasis.";
Science 277:228-231(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS.
PubMed=10425213; DOI=10.1006/bbrc.1999.1070;
Morris J.A., Zhang D., Coleman K.G., Nagle J., Pentchev P.G.,
Carstea E.D.;
"The genomic organization and polymorphism analysis of the human
Niemann-Pick C1 gene.";
Biochem. Biophys. Res. Commun. 261:493-498(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS NPC1 ARG-512; TRP-670;
CYS-825; ILE-849; VAL-874; TYR-948; LEU-954; LEU-958; ALA-1007 AND
THR-1061, AND VARIANTS ARG-215; ILE-642; VAL-858; GLY-971 AND
VAL-1049.
PubMed=11754101; DOI=10.1002/humu.10016;
Bauer P., Knoblich R., Bauer C., Finckh U., Hufen A., Kropp J.,
Braun S., Kustermann-Kuhn B., Schmidt D., Harzer K., Rolfs A.;
"NPC1: complete genomic sequence, mutation analysis, and
characterization of haplotypes.";
Hum. Mutat. 19:30-38(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
GLY-151 AND ILE-642.
TISSUE=Placenta;
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).
[7]
CHARACTERIZATION, AND MUTAGENESIS OF CYS-63 AND CYS-97.
PubMed=9927649; DOI=10.1073/pnas.96.3.805;
Watari H., Blanchette-Mackie E.J., Dwyer N.K., Glick J.M., Patel S.,
Neufeld E.B., Brady R.O., Pentchev P.G., Strauss J.F. III;
"Niemann-Pick C1 protein: obligatory roles for N-terminal domains and
lysosomal targeting in cholesterol mobilization.";
Proc. Natl. Acad. Sci. U.S.A. 96:805-810(1999).
[8]
TOPOLOGY, AND GLYCOSYLATION.
PubMed=10821832; DOI=10.1074/jbc.M002184200;
Davies J.P., Ioannou Y.A.;
"Topological analysis of Niemann-Pick C1 protein reveals that the
membrane orientation of the putative sterol-sensing domain is
identical to those of 3-hydroxy-3-methylglutaryl-CoA reductase and
sterol regulatory element binding protein cleavage-activating
protein.";
J. Biol. Chem. 275:24367-24374(2000).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Placenta;
PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B.,
Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.;
"Integral and associated lysosomal membrane proteins.";
Traffic 8:1676-1686(2007).
[10]
FUNCTION.
PubMed=18772377; DOI=10.1073/pnas.0807328105;
Infante R.E., Wang M.L., Radhakrishnan A., Kwon H.J., Brown M.S.,
Goldstein J.L.;
"NPC2 facilitates bidirectional transfer of cholesterol between NPC1
and lipid bilayers, a step in cholesterol egress from lysosomes.";
Proc. Natl. Acad. Sci. U.S.A. 105:15287-15292(2008).
[11]
INTERACTION WITH TMEM97.
PubMed=19583955; DOI=10.1016/j.cmet.2009.05.009;
Bartz F., Kern L., Erz D., Zhu M., Gilbert D., Meinhof T., Wirkner U.,
Erfle H., Muckenthaler M., Pepperkok R., Runz H.;
"Identification of cholesterol-regulating genes by targeted RNAi
screening.";
Cell Metab. 10:63-75(2009).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135 AND ASN-524.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
REVIEW ON FUNCTION.
PubMed=18832164; DOI=10.1073/pnas.0808256105;
Subramanian K., Balch W.E.;
"NPC1/NPC2 function as a tag team duo to mobilize cholesterol.";
Proc. Natl. Acad. Sci. U.S.A. 105:15223-15224(2008).
[14]
REVIEW ON FUNCTION.
PubMed=20674853; DOI=10.1016/j.cmet.2010.07.004;
Vance J.E.;
"Transfer of cholesterol by the NPC team.";
Cell Metab. 12:105-106(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
REVIEW ON FUNCTION.
PubMed=21412152; DOI=10.1097/MOL.0b013e3283453e69;
Vance J.E., Peake K.B.;
"Function of the Niemann-Pick type C proteins and their bypass by
cyclodextrin.";
Curr. Opin. Lipidol. 22:204-209(2011).
[17]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EBOLAVIRUS
GLYCOPROTEIN.
PubMed=21866103; DOI=10.1038/nature10348;
Carette J.E., Raaben M., Wong A.C., Herbert A.S., Obernosterer G.,
Mulherkar N., Kuehne A.I., Kranzusch P.J., Griffin A.M., Ruthel G.,
Dal Cin P., Dye J.M., Whelan S.P., Chandran K., Brummelkamp T.R.;
"Ebola virus entry requires the cholesterol transporter Niemann-Pick
C1.";
Nature 477:340-343(2011).
[18]
INTERACTION WITH TIM1, AND FUNCTION (MICROBIAL INFECTION).
PubMed=25855742; DOI=10.1128/JVI.03156-14;
Kuroda M., Fujikura D., Nanbo A., Marzi A., Noyori O., Kajihara M.,
Maruyama J., Matsuno K., Miyamoto H., Yoshida R., Feldmann H.,
Takada A.;
"Interaction between TIM-1 and NPC1 Is Important for Cellular Entry of
Ebola Virus.";
J. Virol. 89:6481-6493(2015).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 23-252 OF MUTANT GLN-70;
GLN-122 AND GLN-185 IN COMPLEX WITH CHOLESTEROL, FUNCTION, DISULFIDE
BONDS, GLYCOSYLATION AT ASN-158 AND ASN-222, AND MUTAGENESIS OF
26-VAL-TRP-27; 39-ARG--ASN-41; ASN-41; ASN-70; 82-THR-LEU-83;
101-PHE-TYR-102; 106-ASN--PHE-108; 110-GLU--THR-112; ASN-122;
144-LEU-GLN-145; 146-TYR-TYR-147; 175-LEU-LEU-176; 180-ASP--ASP-182;
ASN-185; 187-TYR-ASN-188; 191-GLU-TYR-192; 195-ASN-LYS-196;
197-ASP-ASN-198; 199-GLY-GLN-200; 202-PRO-PHE-203; 204-THR-ILE-205 AND
GLY-660.
PubMed=19563754; DOI=10.1016/j.cell.2009.03.049;
Kwon H.J., Abi-Mosleh L., Wang M.L., Deisenhofer J., Goldstein J.L.,
Brown M.S., Infante R.E.;
"Structure of N-terminal domain of NPC1 reveals distinct subdomains
for binding and transfer of cholesterol.";
Cell 137:1213-1224(2009).
[21]
VARIANT NPC1 TRP-992.
PubMed=9634529; DOI=10.1086/301931;
Greer W.L., Riddell D.C., Gillan T.L., Girouard G.S., Sparrow S.M.,
Byers D.M., Dobson M.J., Neumann P.E.;
"The Nova Scotia (type D) form of Niemann-Pick disease is caused by a
G3097-->T transversion in NPC1.";
Am. J. Hum. Genet. 63:52-54(1998).
[22]
VARIANTS NPC1 GLN-934; LEU-940; ASN-948; LEU-954; TRP-992; ALA-1007;
THR-1061 AND VAL-1213.
PubMed=10521290; DOI=10.1086/302620;
Greer W.L., Dobson M.J., Girouard G.S., Byers D.M., Riddell D.C.,
Neumann P.E.;
"Mutations in NPC1 highlight a conserved NPC1-specific cysteine-rich
domain.";
Am. J. Hum. Genet. 65:1252-1260(1999).
[23]
VARIANT NPC1 THR-1061.
PubMed=10521297; DOI=10.1086/302626;
Millat G., Marcais C., Rafi M.A., Yamamoto T., Morris J.A.,
Pentchev P.G., Ohno K., Wenger D.A., Vanier M.T.;
"Niemann-Pick C1 disease: the I1061T substitution is a frequent mutant
allele in patients of Western European descent and correlates with a
classic juvenile phenotype.";
Am. J. Hum. Genet. 65:1321-1329(1999).
[24]
VARIANTS NPC1, AND VARIANTS ARG-215; VAL-858 AND GLN-1266.
PubMed=10480349; DOI=10.1007/s004399900059;
Yamamoto T., Nanba E., Ninomiya H., Higaki K., Taniguchi M., Zhang H.,
Akaboshi S., Watanabe Y., Takeshima T., Inui K., Okada S., Tanaka A.,
Sakuragawa N., Millat G., Vanier M.T., Morris J.A., Pentchev P.G.,
Ohno K.;
"NPC1 gene mutations in Japanese patients with Niemann-Pick disease
type C.";
Hum. Genet. 105:10-16(1999).
[25]
VARIANTS NPC1 GLY-177; SER-237; PRO-473; PRO-510; GLN-518; SER-703;
MET-889; LEU-954; TYR-956; ARG-996; THR-1061; CYS-1088; ARG-1205;
PHE-1213 AND GLU-1236, AND VARIANT ALA-873.
PubMed=11182931; DOI=10.1136/jmg.37.9.707;
Yamamoto T., Ninomiya H., Matsumoto M., Ohta Y., Nanba E.,
Tsutsumi Y., Yamakawa K., Millat G., Vanier M.T., Pentchev P.G.,
Ohno K.;
"Genotype-phenotype relationship of Niemann-Pick disease type C: a
possible correlation between clinical onset and levels of NPC1 protein
in isolated skin fibroblasts.";
J. Med. Genet. 37:707-712(2000).
[26]
VARIANTS NPC1 ARG-92; MET-137; SER-237; ASN-242; VAL-248; THR-401;
GLN-404; ASP-612; TRP-652; CYS-789; CYS-825; VAL-874; SER-888;
PRO-929; LEU-940; ASN-944; ASN-948; GLN-958; ARG-976; CYS-978;
LEU-1004; ALA-1007; GLY-1023; THR-1061; LYS-1089; THR-1142; LYS-1150;
SER-1156; MET-1165; HIS-1186 AND GLY-1189.
PubMed=11349231; DOI=10.1086/320599;
Sun X., Marks D.L., Park W.D., Wheatley C.L., Puri V., O'Brien J.F.,
Kraft D.L., Lundquist P.A., Patterson M.C., Pagano R.E., Snow K.;
"Niemann-Pick C variant detection by altered sphingolipid trafficking
and correlation with mutations within a specific domain of NPC1.";
Am. J. Hum. Genet. 68:1361-1372(2001).
[27]
VARIANTS NPC1 SER-237; HIS-242; ARG-272; ALA-378; GLN-404; GLN-518;
VAL-605; ARG-631; PRO-724; PRO-775; CYS-825; VAL-874; GLN-934;
MET-943; ASN-944; MET-950; SER-986; ARG-992; ALA-1007; THR-1054;
THR-1061; THR-1142; TYR-1168 AND HIS-1186.
PubMed=11333381; DOI=10.1086/320606;
Millat G., Marcais C., Tomasetto C., Chikh K., Fensom A.H., Harzer K.,
Wenger D.A., Ohno K., Vanier M.T.;
"Niemann-Pick C1 disease: correlations between NPC1 mutations, levels
of NPC1 protein, and phenotypes emphasize the functional significance
of the putative sterol-sensing domain and of the cysteine-rich luminal
loop.";
Am. J. Hum. Genet. 68:1373-1385(2001).
[28]
VARIANTS NPC1 ARG-63; GLN-404; VAL-927; TRP-992; ASP-1012 AND
SER-1156.
PubMed=11545687; DOI=10.1097/00125817-200109000-00003;
Meiner V., Shpitzen S., Mandel H., Klar A., Ben-Neriah Z.,
Zlotogora J., Sagi M., Lossos A., Bargal R., Sury V., Carmi R.,
Leitersdorf E., Zeigler M.;
"Clinical-biochemical correlation in molecularly characterized
patients with Niemann-Pick type C.";
Genet. Med. 3:343-348(2001).
[29]
VARIANTS NPC1 ARG-92; TYR-177; TRP-518; CYS-942; CYS-978; ALA-1007
VAL-1035 AND THR-1061, AND VARIANTS ARG-215; ILE-642 AND VAL-858.
PubMed=11479732; DOI=10.1007/s004390100531;
Ribeiro I., Marcao A., Amaral O., Sa Miranda M.C., Vanier M.T.,
Millat G.;
"Niemann-Pick type C disease: NPC1 mutations associated with severe
and mild cellular cholesterol trafficking alterations.";
Hum. Genet. 109:24-32(2001).
[30]
VARIANTS NPC1 GLY-231; SER-237; VAL-874 ASN-948 AND THR-1094, AND
VARIANTS CYS-381 AND ILE-642.
PubMed=12408188; DOI=10.1023/A:1020151801060;
Kaminski W.E., Kluenemann H.H., Ibach B., Aslanidis C., Klein H.E.,
Schmitz G.;
"Identification of novel mutations in the NPC1 gene in German patients
with Niemann-Pick C disease.";
J. Inherit. Metab. Dis. 25:385-389(2002).
[31]
VARIANTS NPC1 LYS-451; LEU-474; CYS-890; ASP-899; SER-910; TRP-992;
ALA-1007; THR-1061 AND SER-1156, AND VARIANTS ARG-215; ILE-642 AND
VAL-858.
PubMed=12401890; DOI=10.1194/jlr.M200203-JLR200;
Tarugi P., Ballarini G., Bembi B., Battisti C., Palmeri S.,
Panzani F., Di Leo E., Martini C., Federico A., Calandra S.;
"Niemann-Pick type C disease: mutations of NPC1 gene and evidence of
abnormal expression of some mutant alleles in fibroblasts.";
J. Lipid Res. 43:1908-1919(2002).
[32]
VARIANT NPC1 ARG-113, VARIANT SER-273, CHARACTERIZATION OF VARIANT
NPC1 ARG-113, AND CHARACTERIZATION OF VARIANT SER-273.
PubMed=12554680; DOI=10.1093/hmg/ddg025;
Blom T.S., Linder M.D., Snow K., Pihko H., Hess M.W., Jokitalo E.,
Veckman V., Syvaenen A.-C., Ikonen E.;
"Defective endocytic trafficking of NPC1 and NPC2 underlying infantile
Niemann-Pick type C disease.";
Hum. Mol. Genet. 12:257-272(2003).
[33]
VARIANTS NPC1 TYR-74; SER-166; SER-222; TYR-247; PHE-380; PRO-388;
CYS-389; TRP-404; LEU-433; SER-509; SER-521; LEU-543; CYS-615;
ARG-640; SER-660; MET-664; VAL-673; PHE-684; LEU-691; VAL-695;
ASN-700; ILE-734; LYS-742; GLU-745; VAL-767; GLY-789; ASN-945;
ARG-1016; GLN-1059; LEU-1087; ILE-1137; VAL-1140; LYS-1205 AND
GLY-1249, AND VARIANTS ARG-215; SER-237; SER-434 AND GLN-1266.
PubMed=12955717; DOI=10.1002/humu.10255;
Park W.D., O'Brien J.F., Lundquist P.A., Kraft D.L., Vockley C.W.,
Karnes P.S., Patterson M.C., Snow K.;
"Identification of 58 novel mutations in Niemann-Pick disease type C:
correlation with biochemical phenotype and importance of PTC1-like
domains in NPC1.";
Hum. Mutat. 22:313-325(2003).
[34]
VARIANTS NPC1 MET-137; TYR-177; TRP-372; LEU-434; LEU-474; TYR-479;
ARG-576; MET-664; PHE-727; LYS-754; PRO-775; LEU-865; THR-926;
CYS-942; ASN-944; HIS-948; GLU-959; 961-ASN--PHE-966 DELINS SER;
ALA-1007; VAL-1035; LYS-1036; THR-1061; ASN-1066; ILE-1156; SER-1156
AND LEU-1224, AND VARIANTS ARG-215; ILE-642; VAL-858 AND GLN-1266.
PubMed=16098014; DOI=10.1111/j.1399-0004.2005.00490.x;
Fernandez-Valero E.M., Ballart A., Iturriaga C., Lluch M., Macias J.,
Vanier M.T., Pineda M., Coll M.J.;
"Identification of 25 new mutations in 40 unrelated Spanish Niemann-
Pick type C patients: genotype-phenotype correlations.";
Clin. Genet. 68:245-254(2005).
[35]
VARIANTS NPC1 SER-968; VAL-1015; ARG-1034 AND LEU-1212, AND VARIANTS
ARG-215; ILE-642; VAL-858 AND GLN-1266.
PubMed=15774455; DOI=10.1136/jnnp.2004.046045;
Yang C.-C., Su Y.-N., Chiou P.-C., Fietz M.J., Yu C.-L., Hwu W.-L.,
Lee M.-J.;
"Six novel NPC1 mutations in Chinese patients with Niemann-Pick
disease type C.";
J. Neurol. Neurosurg. Psych. 76:592-595(2005).
[36]
VARIANTS NPC1 SER-166; TYR-177; PRO-404; LEU-537; LEU-543; LEU-615;
ARG-631; LEU-763; CYS-825; LEU-862; LEU-865; CYS-871; TYR-917;
GLN-934; LEU-940; MET-950; SER-968; ALA-992; ARG-992; TRP-992;
ALA-1007; MET-1036; THR-1061; VAL-1062; ASN-1097; VAL-1174; HIS-1186;
VAL-1216 AND ARG-1240, AND VARIANT MET-511.
PubMed=16126423; DOI=10.1016/j.ymgme.2005.07.007;
Millat G., Baielo N., Molinero S., Rodriguez C., Chikh K.,
Vanier M.T.;
"Niemann-Pick C disease: use of denaturing high performance liquid
chromatography for the detection of NPC1 and NPC2 genetic variations
and impact on management of patients and families.";
Mol. Genet. Metab. 86:220-232(2005).
[37]
VARIANTS NPC1 ASN-666 AND SER-961.
PubMed=16802107; DOI=10.1007/s10545-006-0330-z;
Dvorakova L., Sikora J., Hrebicek M., Hulkova H., Bouckova M.,
Stolnaja L., Elleder M.;
"Subclinical course of adult visceral Niemann-Pick type C1 disease. A
rare or underdiagnosed disorder?";
J. Inherit. Metab. Dis. 29:591-591(2006).
[38]
VARIANT NCP1 MET-137.
PubMed=23453666; DOI=10.1016/j.ajhg.2013.02.004;
Akizu N., Shembesh N.M., Ben-Omran T., Bastaki L., Al-Tawari A.,
Zaki M.S., Koul R., Spencer E., Rosti R.O., Scott E., Nickerson E.,
Gabriel S., da Gente G., Li J., Deardorff M.A., Conlin L.K.,
Horton M.A., Zackai E.H., Sherr E.H., Gleeson J.G.;
"Whole-exome sequencing identifies mutated c12orf57 in recessive
corpus callosum hypoplasia.";
Am. J. Hum. Genet. 92:392-400(2013).
-!- FUNCTION: Intracellular cholesterol transporter which acts in
concert with NPC2 and plays an important role in the egress of
cholesterol from the endosomal/lysosomal compartment. Both NPC1
and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze
the mobilization of cholesterol within the multivesicular
environment of the late endosome (LE) to effect egress through the
limiting bilayer of the LE. NPC2 binds unesterified cholesterol
that has been released from LDLs in the lumen of the late
endosomes/lysosomes and transfers it to the cholesterol-binding
pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1
with the hydroxyl group buried in the binding pocket and is
exported from the limiting membrane of late endosomes/ lysosomes
to the ER and plasma membrane by an unknown mechanism. Binds
oxysterol with higher affinity than cholesterol. May play a role
in vesicular trafficking in glia, a process that may be crucial
for maintaining the structural and functional integrity of nerve
terminals. {ECO:0000269|PubMed:18772377,
ECO:0000269|PubMed:19563754}.
-!- FUNCTION: (Microbial infection) Acts as an endosomal entry
receptor for ebolavirus. {ECO:0000269|PubMed:21866103,
ECO:0000269|PubMed:25855742}.
-!- SUBUNIT: Interacts with TMEM97. Interacts (via the second lumenal
domain) with NPC2 in a cholestrol-dependent manner (By
similarity). Interacts with TIM1 (PubMed:25855742). {ECO:0000250,
ECO:0000269|PubMed:25855742}.
-!- SUBUNIT: (Microbial infection) Interacts with ebolavirus
glycoprotein. {ECO:0000269|PubMed:21866103}.
-!- INTERACTION:
Q03135:CAV1; NbExp=3; IntAct=EBI-2368710, EBI-603614;
X5HMX4:GP (xeno); NbExp=3; IntAct=EBI-2368710, EBI-13643336;
-!- SUBCELLULAR LOCATION: Late endosome membrane
{ECO:0000269|PubMed:17897319}; Multi-pass membrane protein
{ECO:0000269|PubMed:17897319}. Lysosome membrane
{ECO:0000269|PubMed:17897319}; Multi-pass membrane protein
{ECO:0000269|PubMed:17897319}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15118-1; Sequence=Displayed;
Name=2;
IsoId=O15118-2; Sequence=VSP_056431, VSP_056432, VSP_056433;
Note=No experimental confirmation available.;
-!- DOMAIN: A cysteine-rich N-terminal domain and a C-terminal domain
containing a di-leucine motif necessary for lysosomal targeting
are critical for mobilization of cholesterol from lysosomes.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:10821832,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19563754}.
-!- DISEASE: Niemann-Pick disease C1 (NPC1) [MIM:257220]: A lysosomal
storage disorder that affects the viscera and the central nervous
system. It is due to defective intracellular processing and
transport of low-density lipoprotein derived cholesterol. It
causes accumulation of cholesterol in lysosomes, with delayed
induction of cholesterol homeostatic reactions. Niemann-Pick
disease type C1 has a highly variable clinical phenotype. Clinical
features include variable hepatosplenomegaly and severe
progressive neurological dysfunction such as ataxia, dystonia and
dementia. The age of onset can vary from infancy to late
adulthood. An allelic variant of Niemann-Pick disease type C1 is
found in people with Nova Scotia ancestry. Patients with the Nova
Scotian clinical variant are less severely affected.
{ECO:0000269|PubMed:10480349, ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:10521297, ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11333381, ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11479732, ECO:0000269|PubMed:11545687,
ECO:0000269|PubMed:11754101, ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:12408188, ECO:0000269|PubMed:12554680,
ECO:0000269|PubMed:12955717, ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16098014, ECO:0000269|PubMed:16126423,
ECO:0000269|PubMed:16802107, ECO:0000269|PubMed:9211849,
ECO:0000269|PubMed:9634529}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF002020; AAB63982.1; -; mRNA.
EMBL; AF157379; AAD48006.1; -; Genomic_DNA.
EMBL; AF157365; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157366; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157367; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157368; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157369; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157370; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157371; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157372; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157373; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157374; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157375; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157376; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157377; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF157378; AAD48006.1; JOINED; Genomic_DNA.
EMBL; AF338230; AAK25791.1; -; Genomic_DNA.
EMBL; AH009108; AAF28875.1; -; Genomic_DNA.
EMBL; AK293779; BAG57194.1; -; mRNA.
EMBL; AC010853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC026634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063302; AAH63302.1; -; mRNA.
CCDS; CCDS11878.1; -. [O15118-1]
RefSeq; NP_000262.2; NM_000271.4. [O15118-1]
UniGene; Hs.464779; -.
UniGene; Hs.715623; -.
PDB; 3GKH; X-ray; 1.81 A; A=23-252.
PDB; 3GKI; X-ray; 1.80 A; A=23-252.
PDB; 3GKJ; X-ray; 1.60 A; A=23-252.
PDB; 3JD8; EM; 4.43 A; A=1-1267.
PDB; 5F18; X-ray; 2.00 A; A=374-620.
PDB; 5F1B; X-ray; 2.30 A; C=374-620.
PDB; 5HNS; X-ray; 2.45 A; A/B=387-618.
PDB; 5I31; X-ray; 3.35 A; A=341-1246.
PDB; 5JNX; EM; 6.56 A; A=1-1278.
PDB; 5KWY; X-ray; 2.40 A; A/B=374-620.
PDBsum; 3GKH; -.
PDBsum; 3GKI; -.
PDBsum; 3GKJ; -.
PDBsum; 3JD8; -.
PDBsum; 5F18; -.
PDBsum; 5F1B; -.
PDBsum; 5HNS; -.
PDBsum; 5I31; -.
PDBsum; 5JNX; -.
PDBsum; 5KWY; -.
ProteinModelPortal; O15118; -.
SMR; O15118; -.
BioGrid; 110925; 18.
DIP; DIP-53217N; -.
ELM; O15118; -.
IntAct; O15118; 8.
STRING; 9606.ENSP00000269228; -.
BindingDB; O15118; -.
ChEMBL; CHEMBL1293277; -.
SwissLipids; SLP:000000478; -.
TCDB; 2.A.6.6.1; the resistance-nodulation-cell division (rnd) superfamily.
iPTMnet; O15118; -.
PhosphoSitePlus; O15118; -.
SwissPalm; O15118; -.
BioMuta; NPC1; -.
EPD; O15118; -.
MaxQB; O15118; -.
PaxDb; O15118; -.
PeptideAtlas; O15118; -.
PRIDE; O15118; -.
Ensembl; ENST00000269228; ENSP00000269228; ENSG00000141458. [O15118-1]
GeneID; 4864; -.
KEGG; hsa:4864; -.
UCSC; uc002kum.5; human. [O15118-1]
CTD; 4864; -.
DisGeNET; 4864; -.
EuPathDB; HostDB:ENSG00000141458.12; -.
GeneCards; NPC1; -.
GeneReviews; NPC1; -.
H-InvDB; HIX0039703; -.
HGNC; HGNC:7897; NPC1.
HPA; CAB070132; -.
HPA; HPA026618; -.
MalaCards; NPC1; -.
MIM; 257220; phenotype.
MIM; 607623; gene.
neXtProt; NX_O15118; -.
OpenTargets; ENSG00000141458; -.
Orphanet; 216986; Niemann-Pick disease type C, adult neurologic onset.
Orphanet; 216981; Niemann-Pick disease type C, juvenile neurologic onset.
Orphanet; 216978; Niemann-Pick disease type C, late infantile neurologic onset.
Orphanet; 216975; Niemann-Pick disease type C, severe early infantile neurologic onset.
Orphanet; 216972; Niemann-Pick disease type C, severe perinatal form.
PharmGKB; PA31698; -.
eggNOG; KOG1933; Eukaryota.
eggNOG; ENOG410XR54; LUCA.
GeneTree; ENSGT00890000139370; -.
HOGENOM; HOG000036674; -.
HOVERGEN; HBG003913; -.
InParanoid; O15118; -.
KO; K12385; -.
OMA; MYNACRD; -.
OrthoDB; EOG091G00JD; -.
PhylomeDB; O15118; -.
TreeFam; TF300416; -.
Reactome; R-HSA-8964038; LDL clearance.
ChiTaRS; NPC1; human.
EvolutionaryTrace; O15118; -.
GeneWiki; NPC1; -.
GenomeRNAi; 4864; -.
PRO; PR:O15118; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141458; -.
CleanEx; HS_NPC1; -.
ExpressionAtlas; O15118; baseline and differential.
Genevisible; O15118; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0015248; F:sterol transporter activity; TAS:ProtInc.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IGI:MGI.
GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEA:Ensembl.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030301; P:cholesterol transport; IDA:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:Ensembl.
GO; GO:0090150; P:establishment of protein localization to membrane; IDA:UniProtKB.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
GO; GO:0031579; P:membrane raft organization; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
GO; GO:0016242; P:negative regulation of macroautophagy; IEA:Ensembl.
GO; GO:2000189; P:positive regulation of cholesterol homeostasis; IMP:CACAO.
GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
InterPro; IPR004765; NP_C_type.
InterPro; IPR032190; NPC1_N.
InterPro; IPR003392; Ptc/Disp.
InterPro; IPR000731; SSD.
PANTHER; PTHR10796:SF176; PTHR10796:SF176; 1.
Pfam; PF16414; NPC1_N; 1.
Pfam; PF02460; Patched; 1.
Pfam; PF12349; Sterol-sensing; 1.
TIGRFAMs; TIGR00917; 2A060601; 1.
PROSITE; PS50156; SSD; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cholesterol metabolism;
Complete proteome; Disease mutation; Disulfide bond; Endosome;
Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Lipid metabolism; Lysosome; Membrane;
Niemann-Pick disease; Polymorphism; Receptor; Reference proteome;
Signal; Steroid metabolism; Sterol metabolism; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1278 Niemann-Pick C1 protein.
/FTId=PRO_0000023261.
TOPO_DOM 23 269 Lumenal. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TOPO_DOM 291 350 Cytoplasmic. {ECO:0000255}.
TRANSMEM 351 371 Helical. {ECO:0000255}.
TOPO_DOM 372 620 Lumenal. {ECO:0000255}.
TRANSMEM 621 641 Helical. {ECO:0000255}.
TOPO_DOM 642 654 Cytoplasmic. {ECO:0000255}.
TRANSMEM 655 675 Helical. {ECO:0000255}.
TOPO_DOM 676 677 Lumenal. {ECO:0000255}.
TRANSMEM 678 698 Helical. {ECO:0000255}.
TOPO_DOM 699 734 Cytoplasmic. {ECO:0000255}.
TRANSMEM 735 755 Helical. {ECO:0000255}.
TOPO_DOM 756 759 Lumenal. {ECO:0000255}.
TRANSMEM 760 780 Helical. {ECO:0000255}.
TOPO_DOM 781 832 Cytoplasmic. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TOPO_DOM 854 1098 Lumenal. {ECO:0000255}.
TRANSMEM 1099 1119 Helical. {ECO:0000255}.
TOPO_DOM 1120 1124 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1125 1145 Helical. {ECO:0000255}.
TOPO_DOM 1146 1146 Lumenal. {ECO:0000255}.
TRANSMEM 1147 1167 Helical. {ECO:0000255}.
TOPO_DOM 1168 1195 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1196 1216 Helical. {ECO:0000255}.
TOPO_DOM 1217 1227 Lumenal. {ECO:0000255}.
TRANSMEM 1228 1248 Helical. {ECO:0000255}.
TOPO_DOM 1249 1278 Cytoplasmic. {ECO:0000255}.
DOMAIN 620 785 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REGION 175 205 Important for cholesterol binding and
cholesterol transfer from NPC1 to
liposomes.
MOTIF 1275 1278 Di-leucine motif.
COMPBIAS 249 259 Poly-Pro.
BINDING 41 41 Cholesterol.
{ECO:0000269|PubMed:19563754}.
BINDING 79 79 Cholesterol.
{ECO:0000269|PubMed:19563754}.
SITE 108 108 Important for cholesterol binding.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10821832}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10821832}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19563754}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10821832}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19563754}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 961 961 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 968 968 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1064 1064 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1072 1072 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 74 {ECO:0000269|PubMed:19563754}.
DISULFID 31 42 {ECO:0000269|PubMed:19563754}.
DISULFID 63 109 {ECO:0000269|PubMed:19563754}.
DISULFID 75 113 {ECO:0000269|PubMed:19563754}.
DISULFID 97 238 {ECO:0000269|PubMed:19563754}.
DISULFID 100 160 {ECO:0000269|PubMed:19563754}.
DISULFID 177 184 {ECO:0000269|PubMed:19563754}.
DISULFID 227 243 {ECO:0000269|PubMed:19563754}.
DISULFID 240 247 {ECO:0000269|PubMed:19563754}.
VAR_SEQ 1 267 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056431.
VAR_SEQ 318 318 K -> KGTAWLLTSTFPSSPVLP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056432.
VAR_SEQ 519 586 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056433.
VARIANT 63 63 C -> R (in NPC1; dbSNP:rs747049347).
{ECO:0000269|PubMed:11545687}.
/FTId=VAR_043172.
VARIANT 74 74 C -> Y (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043173.
VARIANT 92 92 Q -> R (in NPC1).
{ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11479732}.
/FTId=VAR_043174.
VARIANT 113 113 C -> R (in NPC1; partially mislocalized
from late endocytic organelles diffusely
to the cell periphery; localizes to the
endoplasmic reticulum Rab7-negative
endosomes and the cell surface; does not
clears the lysosomal cholesterol
accumulation in NPC1-deficient cells;
dbSNP:rs120074136).
{ECO:0000269|PubMed:12554680}.
/FTId=VAR_043175.
VARIANT 137 137 T -> M (in NPC1; dbSNP:rs372947142).
{ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:23453666}.
/FTId=VAR_043176.
VARIANT 151 151 S -> G (in dbSNP:rs17855819).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_043177.
VARIANT 166 166 P -> S (in NPC1; dbSNP:rs866966704).
{ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043178.
VARIANT 177 177 C -> G (in NPC1; late infantile form).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008815.
VARIANT 177 177 C -> Y (in NPC1; dbSNP:rs80358252).
{ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_015561.
VARIANT 215 215 H -> R (common polymorphism in Japanese;
dbSNP:rs1805081).
{ECO:0000269|PubMed:10480349,
ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_008816.
VARIANT 222 222 N -> S (in NPC1; dbSNP:rs55680026).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043179.
VARIANT 231 231 V -> G (in NPC1).
{ECO:0000269|PubMed:12408188}.
/FTId=VAR_043180.
VARIANT 237 237 P -> S (in NPC1; late infantile form;
dbSNP:rs80358251).
{ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:12408188,
ECO:0000269|PubMed:12955717}.
/FTId=VAR_008817.
VARIANT 242 242 D -> H (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043181.
VARIANT 242 242 D -> N (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043182.
VARIANT 247 247 C -> Y (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043183.
VARIANT 248 248 G -> V (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043184.
VARIANT 272 272 M -> R (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043185.
VARIANT 273 273 W -> S (colocalizes with the wild-type
protein with Rab7-positive late
endosomes; clears the lysosomal
cholesterol accumulation in NPC1-
deficient cells).
{ECO:0000269|PubMed:12554680}.
/FTId=VAR_043186.
VARIANT 333 333 G -> D.
/FTId=VAR_008818.
VARIANT 372 372 R -> W (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043187.
VARIANT 378 378 V -> A (in NPC1; dbSNP:rs120074134).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_015562.
VARIANT 380 380 L -> F (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043188.
VARIANT 381 381 W -> C. {ECO:0000269|PubMed:12408188}.
/FTId=VAR_043189.
VARIANT 388 388 A -> P (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043190.
VARIANT 389 389 R -> C (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043191.
VARIANT 401 401 P -> T (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043192.
VARIANT 404 404 R -> P (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043193.
VARIANT 404 404 R -> Q (in NPC1; dbSNP:rs139751448).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11545687}.
/FTId=VAR_043194.
VARIANT 404 404 R -> W (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043195.
VARIANT 433 433 P -> L (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043196.
VARIANT 434 434 P -> L (in NPC1; dbSNP:rs774333145).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043197.
VARIANT 434 434 P -> S (in dbSNP:rs61731962).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043198.
VARIANT 451 451 E -> K (in NPC1; dbSNP:rs781065429).
{ECO:0000269|PubMed:12401890}.
/FTId=VAR_043199.
VARIANT 472 472 L -> P.
/FTId=VAR_008819.
VARIANT 473 473 S -> P (in NPC1; late infantile form).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008820.
VARIANT 474 474 P -> L (in NPC1; dbSNP:rs372445155).
{ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_043200.
VARIANT 479 479 C -> Y (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043201.
VARIANT 509 509 Y -> S (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043202.
VARIANT 510 510 H -> P (in NPC1; late infantile form).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008821.
VARIANT 511 511 T -> M (in dbSNP:rs13381670).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043203.
VARIANT 512 512 H -> R (in NPC1).
{ECO:0000269|PubMed:11754101}.
/FTId=VAR_043204.
VARIANT 518 518 R -> Q (in NPC1; late infantile form;
Common in Japanese; dbSNP:rs483352886).
{ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11333381}.
/FTId=VAR_008822.
VARIANT 518 518 R -> W (in NPC1; dbSNP:rs377515417).
{ECO:0000269|PubMed:11479732}.
/FTId=VAR_043205.
VARIANT 521 521 A -> S (in NPC1; dbSNP:rs138184115).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043206.
VARIANT 537 537 F -> L (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043207.
VARIANT 543 543 P -> L (in NPC1; dbSNP:rs369368181).
{ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043208.
VARIANT 574 574 T -> K (in NPC1).
/FTId=VAR_043209.
VARIANT 576 576 K -> R (in NPC1; dbSNP:rs761660695).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043210.
VARIANT 605 605 A -> V (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043211.
VARIANT 612 612 E -> D (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043212.
VARIANT 615 615 R -> C (in NPC1; dbSNP:rs745777805).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043213.
VARIANT 615 615 R -> L (in NPC1; dbSNP:rs773351341).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043214.
VARIANT 631 631 M -> R (in NPC1).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043215.
VARIANT 640 640 G -> R (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043216.
VARIANT 642 642 M -> I (in dbSNP:rs1788799).
{ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:12408188,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:9211849}.
/FTId=VAR_008823.
VARIANT 652 652 S -> W (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043217.
VARIANT 660 660 G -> S (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043218.
VARIANT 664 664 V -> M (in NPC1; dbSNP:rs376213990).
{ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_043219.
VARIANT 666 666 S -> N (in NPC1; dbSNP:rs750480579).
{ECO:0000269|PubMed:16802107}.
/FTId=VAR_043220.
VARIANT 670 670 C -> W (in NPC1).
{ECO:0000269|PubMed:11754101}.
/FTId=VAR_043221.
VARIANT 673 673 G -> V (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043222.
VARIANT 684 684 L -> F (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043223.
VARIANT 691 691 P -> L (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043224.
VARIANT 695 695 L -> V (in NPC1; dbSNP:rs370323921).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043225.
VARIANT 700 700 D -> N (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043226.
VARIANT 703 703 F -> S (in NPC1).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_043227.
VARIANT 724 724 L -> P (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043228.
VARIANT 727 727 V -> F (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043229.
VARIANT 734 734 S -> I (in NPC1; dbSNP:rs757475924).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043230.
VARIANT 742 742 E -> K (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043231.
VARIANT 745 745 A -> E (in NPC1; dbSNP:rs752386083).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043232.
VARIANT 754 754 M -> K (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043233.
VARIANT 757 757 V -> A.
/FTId=VAR_008824.
VARIANT 763 763 F -> L (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043234.
VARIANT 767 767 A -> V (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043235.
VARIANT 775 775 Q -> P (in NPC1; dbSNP:rs80358253).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_043236.
VARIANT 789 789 R -> C (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043237.
VARIANT 789 789 R -> G (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043238.
VARIANT 825 825 Y -> C (in NPC1; dbSNP:rs550562774).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043239.
VARIANT 849 849 S -> I (in NPC1).
{ECO:0000269|PubMed:11754101}.
/FTId=VAR_043240.
VARIANT 858 858 I -> V (common polymorphism in Japanese;
dbSNP:rs1805082).
{ECO:0000269|PubMed:10480349,
ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_008825.
VARIANT 862 862 Q -> L (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043241.
VARIANT 865 865 S -> L (in NPC1).
{ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043242.
VARIANT 871 871 Y -> C (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043243.
VARIANT 873 873 V -> A. {ECO:0000269|PubMed:11182931}.
/FTId=VAR_043244.
VARIANT 874 874 D -> V (in NPC1; dbSNP:rs372030650).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11754101}.
/FTId=VAR_043245.
VARIANT 888 888 P -> S (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043246.
VARIANT 889 889 V -> M (in NPC1; adult form;
dbSNP:rs120074130).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008826.
VARIANT 890 890 Y -> C (in NPC1).
{ECO:0000269|PubMed:12401890}.
/FTId=VAR_043247.
VARIANT 899 899 Y -> D (in NPC1).
{ECO:0000269|PubMed:12401890}.
/FTId=VAR_043248.
VARIANT 910 910 G -> S (in NPC1; dbSNP:rs768999208).
{ECO:0000269|PubMed:12401890}.
/FTId=VAR_043249.
VARIANT 917 917 D -> Y (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043250.
VARIANT 926 926 A -> T (in NPC1; dbSNP:rs564631426).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043251.
VARIANT 927 927 A -> V (in NPC1; dbSNP:rs753768576).
{ECO:0000269|PubMed:11545687}.
/FTId=VAR_043252.
VARIANT 928 928 Q -> P (in NPC1; dbSNP:rs28940897).
/FTId=VAR_008827.
VARIANT 929 929 L -> P (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043253.
VARIANT 934 934 R -> Q (in NPC1; dbSNP:rs786204714).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_008828.
VARIANT 940 940 S -> L (in NPC1; dbSNP:rs143124972).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_008829.
VARIANT 942 942 W -> C (in NPC1).
{ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_043254.
VARIANT 943 943 I -> M (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043255.
VARIANT 944 944 D -> N (in NPC1; dbSNP:rs748837410).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_043256.
VARIANT 945 945 D -> N (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043257.
VARIANT 948 948 D -> H (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043258.
VARIANT 948 948 D -> N (in NPC1).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:12408188}.
/FTId=VAR_008830.
VARIANT 948 948 D -> Y (in NPC1).
{ECO:0000269|PubMed:11754101}.
/FTId=VAR_043259.
VARIANT 950 950 V -> M (in NPC1; adult form;
dbSNP:rs120074135).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_015563.
VARIANT 954 954 S -> L (in NPC1; dbSNP:rs543206298).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11754101}.
/FTId=VAR_008831.
VARIANT 956 956 C -> Y (in NPC1; late infantile form).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008832.
VARIANT 958 958 R -> L (in NPC1).
{ECO:0000269|PubMed:11754101}.
/FTId=VAR_043260.
VARIANT 958 958 R -> Q (in NPC1; dbSNP:rs120074132).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_015564.
VARIANT 959 959 V -> E (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043261.
VARIANT 961 966 NITDQF -> S (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043262.
VARIANT 961 961 N -> S (in NPC1; dbSNP:rs34084984).
{ECO:0000269|PubMed:16802107}.
/FTId=VAR_043263.
VARIANT 968 968 N -> S (in NPC1; dbSNP:rs773767253).
{ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_043264.
VARIANT 971 971 V -> G. {ECO:0000269|PubMed:11754101}.
/FTId=VAR_043265.
VARIANT 976 976 C -> R (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043266.
VARIANT 978 978 R -> C (in NPC1; dbSNP:rs28942108).
{ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11479732}.
/FTId=VAR_015565.
VARIANT 986 986 G -> S (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043267.
VARIANT 992 992 G -> A (in NPC1; dbSNP:rs757534240).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043268.
VARIANT 992 992 G -> R (in NPC1; dbSNP:rs80358254).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_015566.
VARIANT 992 992 G -> W (in NPC1; found in the Nova
Scotian clinical variant;
dbSNP:rs80358254).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11545687,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:16126423,
ECO:0000269|PubMed:9634529}.
/FTId=VAR_008833.
VARIANT 996 996 M -> R (in NPC1).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_043269.
VARIANT 1004 1004 S -> L (in NPC1; dbSNP:rs150334966).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043270.
VARIANT 1007 1007 P -> A (in NPC1; dbSNP:rs80358257).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_008834.
VARIANT 1012 1012 G -> D (in NPC1).
{ECO:0000269|PubMed:11545687}.
/FTId=VAR_043271.
VARIANT 1015 1015 G -> V (in NPC1; dbSNP:rs761773567).
{ECO:0000269|PubMed:15774455}.
/FTId=VAR_043272.
VARIANT 1016 1016 H -> R (in NPC1; dbSNP:rs140211089).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043273.
VARIANT 1023 1023 V -> G (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043274.
VARIANT 1034 1034 G -> R (in NPC1).
{ECO:0000269|PubMed:15774455}.
/FTId=VAR_043275.
VARIANT 1035 1035 A -> V (in NPC1; dbSNP:rs28942107).
{ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_015567.
VARIANT 1036 1036 T -> K (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043276.
VARIANT 1036 1036 T -> M (in NPC1; dbSNP:rs28942104).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_008835.
VARIANT 1049 1049 A -> V. {ECO:0000269|PubMed:11754101}.
/FTId=VAR_043277.
VARIANT 1054 1054 A -> T (in NPC1; dbSNP:rs80358258).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043278.
VARIANT 1059 1059 R -> Q (in NPC1; dbSNP:rs771000314).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043279.
VARIANT 1061 1061 I -> T (in NPC1; late infantile form;
dbSNP:rs80358259).
{ECO:0000269|PubMed:10521290,
ECO:0000269|PubMed:10521297,
ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:11754101,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:16098014,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_008836.
VARIANT 1062 1062 A -> V (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043280.
VARIANT 1066 1066 T -> N (in NPC1; dbSNP:rs772622214).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043281.
VARIANT 1087 1087 F -> L (in NPC1; dbSNP:rs746715353).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043282.
VARIANT 1088 1088 Y -> C (in NPC1; juvenile form;
dbSNP:rs28942106).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008837.
VARIANT 1089 1089 E -> K (in NPC1; dbSNP:rs374526072).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043283.
VARIANT 1094 1094 I -> T (in NPC1).
{ECO:0000269|PubMed:12408188}.
/FTId=VAR_043284.
VARIANT 1097 1097 D -> N (in NPC1; dbSNP:rs758829443).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043285.
VARIANT 1137 1137 N -> I (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043286.
VARIANT 1140 1140 G -> V (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043287.
VARIANT 1142 1142 M -> T (in NPC1; dbSNP:rs778878523).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231}.
/FTId=VAR_043288.
VARIANT 1150 1150 N -> K (in NPC1).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043289.
VARIANT 1156 1156 N -> I (in NPC1; dbSNP:rs28942105).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043290.
VARIANT 1156 1156 N -> S (in NPC1; dbSNP:rs28942105).
{ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:11545687,
ECO:0000269|PubMed:12401890,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_008838.
VARIANT 1165 1165 V -> M (in NPC1; dbSNP:rs748862167).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043291.
VARIANT 1167 1167 F -> L (in NPC1).
/FTId=VAR_008839.
VARIANT 1168 1168 C -> Y (in NPC1).
{ECO:0000269|PubMed:11333381}.
/FTId=VAR_043292.
VARIANT 1174 1174 A -> V (in NPC1; dbSNP:rs780175800).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043293.
VARIANT 1186 1186 R -> H (in NPC1; dbSNP:rs200444084).
{ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:16126423}.
/FTId=VAR_008840.
VARIANT 1189 1189 E -> G (in NPC1; dbSNP:rs369098773).
{ECO:0000269|PubMed:11349231}.
/FTId=VAR_043294.
VARIANT 1205 1205 T -> K (in NPC1; dbSNP:rs758902805).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043295.
VARIANT 1205 1205 T -> R (in NPC1).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_043296.
VARIANT 1212 1212 V -> L (in NPC1; dbSNP:rs753419933).
{ECO:0000269|PubMed:15774455}.
/FTId=VAR_043297.
VARIANT 1213 1213 L -> F (in NPC1; juvenile form;
dbSNP:rs120074131).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_008841.
VARIANT 1213 1213 L -> V (in NPC1; dbSNP:rs766178353).
{ECO:0000269|PubMed:10521290}.
/FTId=VAR_008842.
VARIANT 1216 1216 A -> V (in NPC1).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043298.
VARIANT 1220 1220 I -> T.
/FTId=VAR_008843.
VARIANT 1224 1224 F -> L (in NPC1).
{ECO:0000269|PubMed:16098014}.
/FTId=VAR_043299.
VARIANT 1236 1236 G -> E (in NPC1; dbSNP:rs761653115).
{ECO:0000269|PubMed:11182931}.
/FTId=VAR_043300.
VARIANT 1240 1240 G -> R (in NPC1; dbSNP:rs745892286).
{ECO:0000269|PubMed:16126423}.
/FTId=VAR_043301.
VARIANT 1249 1249 S -> G (in NPC1).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043302.
VARIANT 1266 1266 R -> Q (common polymorphism in Japanese;
dbSNP:rs1805084).
{ECO:0000269|PubMed:10480349,
ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:15774455,
ECO:0000269|PubMed:16098014}.
/FTId=VAR_008844.
MUTAGEN 26 27 VW->AA: Nearly abolishes 25-
hydroxycholesterol binding. Reduces
cholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 39 41 RYN->AAA: Strongly reduces cholesterol
and 25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 41 41 N->A: Nearly abolishes cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 63 63 C->S: Loss of function.
{ECO:0000269|PubMed:9927649}.
MUTAGEN 70 70 N->Q: Reduces glycosylation; when
associated with Q-122 and Q-185. No
effect on cholesterol and 25-
hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 82 83 TL->AA: Strongly reduces cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 97 97 C->S: Loss of function.
{ECO:0000269|PubMed:9927649}.
MUTAGEN 101 102 FY->AA: Strongly reduces 25-
hydroxycholesterol binding. No effect on
cholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 106 108 NLF->AAA: Nearly abolishes cholesterol
and 25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 110 112 ELT->AAA: No effect on cholesterol and
25-hydroxycholesterol binding and
transfer. {ECO:0000269|PubMed:19563754}.
MUTAGEN 122 122 N->Q: Reduces glycosylation; when
associated with Q-70 and Q-185. No effect
on cholesterol and 25-hydroxycholesterol
binding. {ECO:0000269|PubMed:19563754}.
MUTAGEN 144 145 LQ->AA: Strongly reduces 25-
hydroxycholesterol binding. No effect on
cholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 146 147 YY->AA: Strongly reduces 25-
hydroxycholesterol binding. No effect on
cholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 175 176 LL->AA: No effect on cholesterol or 25-
hydroxycholesterol binding. Strongly
reduces cholesterol transfer to liposomes
in a NPC2-dependent manner.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 180 182 DAD->AAA: Strongly reduces cholesterol
transfer to liposomes in a NPC2-dependent
manner. {ECO:0000269|PubMed:19563754}.
MUTAGEN 185 185 N->Q: Reduces glycosylation; when
associated with Q-70 and Q-122. No effect
on cholesterol and 25-hydroxycholesterol
binding. Strongly reduces cholesterol
transfer to liposomes in a NPC2-dependent
manner. {ECO:0000269|PubMed:19563754}.
MUTAGEN 187 188 TN->AA: Strongly reduces 25-
hydroxycholesterol binding and
cholesterol transfer to liposomes in a
NPC2-dependent manner.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 191 192 EY->AA: No effect on cholesterol or 25-
hydroxycholesterol binding. Nearly
abolishes cholesterol transfer to
liposomes in a NPC2-dependent manner.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 195 196 NK->AA: Strongly reduces 25-
hydroxycholesterol binding. No effect on
cholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 197 198 DN->AA: Strongly reduces cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 199 200 GQ->AA: Strongly reduces 25-
hydroxycholesterol binding and
cholesterol transfer to liposomes in a
NPC2-dependent manner.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 202 203 PF->AA: Abolishes cholesterol and 25-
hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 204 205 TI->AA: Strongly reduces cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 660 660 G->R: Loss of function.
{ECO:0000269|PubMed:19563754}.
STRAND 26 35 {ECO:0000244|PDB:3GKJ}.
STRAND 38 43 {ECO:0000244|PDB:3GKJ}.
HELIX 53 55 {ECO:0000244|PDB:3GKJ}.
HELIX 56 62 {ECO:0000244|PDB:3GKJ}.
HELIX 64 66 {ECO:0000244|PDB:3GKJ}.
STRAND 72 74 {ECO:0000244|PDB:3GKJ}.
HELIX 77 85 {ECO:0000244|PDB:3GKJ}.
HELIX 88 94 {ECO:0000244|PDB:3GKJ}.
HELIX 98 113 {ECO:0000244|PDB:3GKJ}.
HELIX 117 120 {ECO:0000244|PDB:3GKJ}.
STRAND 121 130 {ECO:0000244|PDB:3GKJ}.
TURN 132 134 {ECO:0000244|PDB:3GKJ}.
STRAND 137 148 {ECO:0000244|PDB:3GKJ}.
HELIX 150 160 {ECO:0000244|PDB:3GKJ}.
STRAND 168 171 {ECO:0000244|PDB:3GKJ}.
HELIX 173 176 {ECO:0000244|PDB:3GKJ}.
STRAND 177 179 {ECO:0000244|PDB:3GKJ}.
TURN 181 183 {ECO:0000244|PDB:3GKJ}.
HELIX 186 193 {ECO:0000244|PDB:3GKJ}.
HELIX 196 198 {ECO:0000244|PDB:3GKJ}.
STRAND 199 209 {ECO:0000244|PDB:3GKJ}.
HELIX 240 242 {ECO:0000244|PDB:3GKJ}.
HELIX 244 246 {ECO:0000244|PDB:3GKJ}.
HELIX 350 365 {ECO:0000244|PDB:5I31}.
STRAND 367 371 {ECO:0000244|PDB:5I31}.
HELIX 380 382 {ECO:0000244|PDB:5KWY}.
HELIX 385 398 {ECO:0000244|PDB:5F18}.
TURN 399 402 {ECO:0000244|PDB:5F18}.
STRAND 403 411 {ECO:0000244|PDB:5F18}.
STRAND 418 420 {ECO:0000244|PDB:5F18}.
STRAND 423 425 {ECO:0000244|PDB:5HNS}.
STRAND 429 431 {ECO:0000244|PDB:5F18}.
HELIX 433 435 {ECO:0000244|PDB:5F18}.
HELIX 437 451 {ECO:0000244|PDB:5F18}.
STRAND 454 457 {ECO:0000244|PDB:5F18}.
STRAND 460 463 {ECO:0000244|PDB:5F18}.
HELIX 464 467 {ECO:0000244|PDB:5F18}.
TURN 471 475 {ECO:0000244|PDB:5F18}.
HELIX 484 488 {ECO:0000244|PDB:5F18}.
HELIX 492 495 {ECO:0000244|PDB:5F18}.
STRAND 505 507 {ECO:0000244|PDB:5F18}.
HELIX 509 516 {ECO:0000244|PDB:5F18}.
TURN 526 530 {ECO:0000244|PDB:5F18}.
STRAND 536 538 {ECO:0000244|PDB:5F18}.
HELIX 543 546 {ECO:0000244|PDB:5F18}.
STRAND 547 549 {ECO:0000244|PDB:5F18}.
HELIX 555 557 {ECO:0000244|PDB:5F18}.
STRAND 559 568 {ECO:0000244|PDB:5F18}.
HELIX 574 592 {ECO:0000244|PDB:5F18}.
STRAND 600 603 {ECO:0000244|PDB:5F18}.
HELIX 608 611 {ECO:0000244|PDB:5KWY}.
HELIX 621 638 {ECO:0000244|PDB:5I31}.
HELIX 660 671 {ECO:0000244|PDB:5I31}.
STRAND 672 674 {ECO:0000244|PDB:5I31}.
HELIX 677 679 {ECO:0000244|PDB:5I31}.
STRAND 680 682 {ECO:0000244|PDB:5I31}.
HELIX 685 687 {ECO:0000244|PDB:5I31}.
HELIX 690 707 {ECO:0000244|PDB:5I31}.
TURN 728 730 {ECO:0000244|PDB:5I31}.
HELIX 731 746 {ECO:0000244|PDB:5I31}.
HELIX 755 775 {ECO:0000244|PDB:5I31}.
TURN 776 778 {ECO:0000244|PDB:5I31}.
HELIX 779 789 {ECO:0000244|PDB:5I31}.
HELIX 834 851 {ECO:0000244|PDB:5I31}.
HELIX 866 874 {ECO:0000244|PDB:5I31}.
HELIX 906 911 {ECO:0000244|PDB:5I31}.
HELIX 912 915 {ECO:0000244|PDB:5I31}.
STRAND 916 918 {ECO:0000244|PDB:5I31}.
HELIX 928 932 {ECO:0000244|PDB:5I31}.
HELIX 940 943 {ECO:0000244|PDB:5I31}.
TURN 954 957 {ECO:0000244|PDB:5I31}.
STRAND 959 961 {ECO:0000244|PDB:5I31}.
HELIX 1038 1051 {ECO:0000244|PDB:5I31}.
TURN 1052 1054 {ECO:0000244|PDB:5I31}.
HELIX 1084 1088 {ECO:0000244|PDB:5I31}.
HELIX 1094 1115 {ECO:0000244|PDB:5I31}.
HELIX 1125 1137 {ECO:0000244|PDB:5I31}.
TURN 1138 1140 {ECO:0000244|PDB:5I31}.
HELIX 1147 1152 {ECO:0000244|PDB:5I31}.
HELIX 1155 1157 {ECO:0000244|PDB:5I31}.
HELIX 1158 1170 {ECO:0000244|PDB:5I31}.
TURN 1186 1190 {ECO:0000244|PDB:5I31}.
HELIX 1191 1200 {ECO:0000244|PDB:5I31}.
STRAND 1203 1205 {ECO:0000244|PDB:5I31}.
TURN 1217 1220 {ECO:0000244|PDB:5I31}.
HELIX 1222 1235 {ECO:0000244|PDB:5I31}.
HELIX 1238 1242 {ECO:0000244|PDB:5I31}.
TURN 1243 1245 {ECO:0000244|PDB:5I31}.
SEQUENCE 1278 AA; 142167 MW; DA1523E09822E5C7 CRC64;
MTARGLALGL LLLLLCPAQV FSQSCVWYGE CGIAYGDKRY NCEYSGPPKP LPKDGYDLVQ
ELCPGFFFGN VSLCCDVRQL QTLKDNLQLP LQFLSRCPSC FYNLLNLFCE LTCSPRQSQF
LNVTATEDYV DPVTNQTKTN VKELQYYVGQ SFANAMYNAC RDVEAPSSND KALGLLCGKD
ADACNATNWI EYMFNKDNGQ APFTITPVFS DFPVHGMEPM NNATKGCDES VDEVTAPCSC
QDCSIVCGPK PQPPPPPAPW TILGLDAMYV IMWITYMAFL LVFFGAFFAV WCYRKRYFVS
EYTPIDSNIA FSVNASDKGE ASCCDPVSAA FEGCLRRLFT RWGSFCVRNP GCVIFFSLVF
ITACSSGLVF VRVTTNPVDL WSAPSSQARL EKEYFDQHFG PFFRTEQLII RAPLTDKHIY
QPYPSGADVP FGPPLDIQIL HQVLDLQIAI ENITASYDNE TVTLQDICLA PLSPYNTNCT
ILSVLNYFQN SHSVLDHKKG DDFFVYADYH THFLYCVRAP ASLNDTSLLH DPCLGTFGGP
VFPWLVLGGY DDQNYNNATA LVITFPVNNY YNDTEKLQRA QAWEKEFINF VKNYKNPNLT
ISFTAERSIE DELNRESDSD VFTVVISYAI MFLYISLALG HMKSCRRLLV DSKVSLGIAG
ILIVLSSVAC SLGVFSYIGL PLTLIVIEVI PFLVLAVGVD NIFILVQAYQ RDERLQGETL
DQQLGRVLGE VAPSMFLSSF SETVAFFLGA LSVMPAVHTF SLFAGLAVFI DFLLQITCFV
SLLGLDIKRQ EKNRLDIFCC VRGAEDGTSV QASESCLFRF FKNSYSPLLL KDWMRPIVIA
IFVGVLSFSI AVLNKVDIGL DQSLSMPDDS YMVDYFKSIS QYLHAGPPVY FVLEEGHDYT
SSKGQNMVCG GMGCNNDSLV QQIFNAAQLD NYTRIGFAPS SWIDDYFDWV KPQSSCCRVD
NITDQFCNAS VVDPACVRCR PLTPEGKQRP QGGDFMRFLP MFLSDNPNPK CGKGGHAAYS
SAVNILLGHG TRVGATYFMT YHTVLQTSAD FIDALKKARL IASNVTETMG INGSAYRVFP
YSVFYVFYEQ YLTIIDDTIF NLGVSLGAIF LVTMVLLGCE LWSAVIMCAT IAMVLVNMFG
VMWLWGISLN AVSLVNLVMS CGISVEFCSH ITRAFTVSMK GSRVERAEEA LAHMGSSVFS
GITLTKFGGI VVLAFAKSQI FQIFYFRMYL AMVLLGATHG LIFLPVLLSY IGPSVNKAKS
CATEERYKGT ERERLLNF


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