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NPC intracellular cholesterol transporter 1 (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.
10-OCT-2018, entry version 183.
RecName: Full=NPC intracellular cholesterol transporter 1 {ECO:0000312|HGNC:HGNC:7897};
AltName: Full=Niemann-Pick C1 protein {ECO:0000303|PubMed:9211849};
Flags: Precursor;
Name=NPC1 {ECO:0000312|HGNC:HGNC:7897};
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), FUNCTION, 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]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF CYS-63;
74-CYS-CYS-75; CYS-97 AND 1275-LEU--PHE-1278.
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]
FUNCTION, 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, AND INTERACTION WITH NPC2.
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] {ECO:0000244|PDB:5F18, ECO:0000244|PDB:5F1B}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 374-620 IN COMPLEX WITH
EBOLAVIRUS GLYCOPROTEIN GP, INTERACTION WITH EBOLAVIRUS GLYCOPROTEIN
GP (MICROBIAL INFECTION), MUTAGENESIS OF 423-TYR-PRO-424; PHE-503;
PHE-504 AND TYR-506, AND DISULFIDE BONDS.
PubMed=26771495; DOI=10.1016/j.cell.2015.12.044;
Wang H., Shi Y., Song J., Qi J., Lu G., Yan J., Gao G.F.;
"Ebola Viral Glycoprotein Bound to Its Endosomal Receptor Niemann-Pick
C1.";
Cell 164:258-268(2016).
[22] {ECO:0000244|PDB:3JD8, ECO:0000244|PDB:5JNX}
STRUCTURE BY ELECTRON MICROSCOPY (4.43 ANGSTROMS), FUNCTION,
INTERACTION WITH NPC2 AND WITH EBOLAVIRUS GLYCOPROTEIN GP, TOPOLOGY,
GLYCOSYLATION AT ASN-122; ASN-135; ASN-158; ASN-185; ASN-222; ASN-524;
ASN-572; ASN-598 AND ASN-1064, DISULFIDE BONDS, CHARACTERIZATION OF
VARIANT NPC1 TRP-518, AND MUTAGENESIS OF 25-CYS--PRO-257;
175-LEU-LEU-176; 202-PRO-PHE-203 AND 249-PRO--PRO-257.
PubMed=27238017; DOI=10.1016/j.cell.2016.05.022;
Gong X., Qian H., Zhou X., Wu J., Wan T., Cao P., Huang W., Zhao X.,
Wang X., Wang P., Shi Y., Gao G.F., Zhou Q., Yan N.;
"Structural Insights into the Niemann-Pick C1 (NPC1)-Mediated
Cholesterol Transfer and Ebola Infection.";
Cell 165:1467-1478(2016).
[23] {ECO:0000244|PDB:5HNS}
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 387-618, GLYCOSYLATION AT
ASN-478; ASN-524; ASN-557; ASN-572 AND ASN-598, AND DISULFIDE BONDS.
PubMed=26846330; DOI=10.1002/1873-3468.12089;
Zhao Y., Ren J., Harlos K., Stuart D.I.;
"Structure of glycosylated NPC1 luminal domain C reveals insights into
NPC2 and Ebola virus interactions.";
FEBS Lett. 590:605-612(2016).
[24] {ECO:0000244|PDB:5KWY}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 374-620 IN COMPLEX WITH
NPC2, AND DISULFIDE BONDS.
PubMed=27551080; DOI=10.1073/pnas.1611956113;
Li X., Saha P., Li J., Blobel G., Pfeffer S.R.;
"Clues to the mechanism of cholesterol transfer from the structure of
NPC1 middle lumenal domain bound to NPC2.";
Proc. Natl. Acad. Sci. U.S.A. 113:10079-10084(2016).
[25] {ECO:0000244|PDB:5U73, ECO:0000244|PDB:5U74}
X-RAY CRYSTALLOGRAPHY (3.33 ANGSTROMS) OF 334-1278, FUNCTION,
TOPOLOGY, GLYCOSYLATION AT ASN-452; ASN-459; ASN-478; ASN-524;
ASN-557; ASN-598; ASN-916; ASN-931; ASN-961; ASN-968 AND ASN-1064,
MUTAGENESIS OF 230-SER--VAL-234; PRO-691 AND 909-CYS--ASP-917, AND
DISULFIDE BONDS.
PubMed=28784760; DOI=10.1073/pnas.1711716114;
Li X., Lu F., Trinh M.N., Schmiege P., Seemann J., Wang J., Blobel G.;
"3.3 A structure of Niemann-Pick C1 protein reveals insights into the
function of the C-terminal luminal domain in cholesterol transport.";
Proc. Natl. Acad. Sci. U.S.A. 114:9116-9121(2017).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
VARIANTS NPC1 GLY-177; 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 VARIANTS SER-237 AND 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).
[31]
VARIANTS NPC1 ARG-92; MET-137; 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, AND VARIANT SER-237.
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).
[32]
VARIANTS NPC1 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, AND VARIANT SER-237.
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).
[33]
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).
[34]
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).
[35]
VARIANTS NPC1 GLY-231; VAL-874 ASN-948 AND THR-1094, AND VARIANTS
SER-237; 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).
[36]
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).
[37]
FUNCTION, SUBCELLULAR LOCATION, VARIANT NPC1 ARG-113, VARIANT SER-237,
CHARACTERIZATION OF VARIANT NPC1 ARG-113, AND CHARACTERIZATION OF
VARIANT SER-237.
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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
(PubMed:9211849, PubMed:9927649, PubMed:10821832, PubMed:18772377,
PubMed:27238017, PubMed:12554680). Unesterified cholesterol that
has been released from LDLs in the lumen of the late
endosomes/lysosomes is transferred by NPC2 to the cholesterol-
binding pocket in the N-terminal domain of NPC1 (PubMed:9211849,
PubMed:9927649, PubMed:18772377, PubMed:19563754, PubMed:27238017,
PubMed:28784760). Cholesterol binds to NPC1 with the hydroxyl
group buried in the binding pocket (PubMed:19563754). 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 (Probable). {ECO:0000269|PubMed:10821832,
ECO:0000269|PubMed:12554680, ECO:0000269|PubMed:18772377,
ECO:0000269|PubMed:19563754, ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760, ECO:0000269|PubMed:9211849,
ECO:0000269|PubMed:9927649, ECO:0000305}.
-!- FUNCTION: (Microbial infection) Acts as an endosomal entry
receptor for ebolavirus. {ECO:0000269|PubMed:21866103,
ECO:0000269|PubMed:25855742}.
-!- SUBUNIT: Interacts (via the second lumenal domain) with NPC2
(PubMed:18772377, PubMed:27238017, PubMed:27551080). Interacts
with TMEM97 (PubMed:19583955). Interacts with TIM1
(PubMed:25855742). {ECO:0000269|PubMed:18772377,
ECO:0000269|PubMed:19583955, ECO:0000269|PubMed:25855742,
ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:27551080}.
-!- SUBUNIT: (Microbial infection) Interacts with ebolavirus
glycoprotein. {ECO:0000269|PubMed:21866103,
ECO:0000269|PubMed:26771495, ECO:0000269|PubMed:27238017}.
-!- 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:12554680}; Multi-pass membrane protein
{ECO:0000269|PubMed:10821832, ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}. Lysosome membrane
{ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:9927649}; Multi-
pass membrane protein {ECO:0000269|PubMed:10821832,
ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:28784760}.
-!- 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.
{ECO:0000269|PubMed:9927649}.
-!- PTM: N-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:27238017,
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; 5JNX; EM; 6.56 A; A=1-1278.
PDB; 5KWY; X-ray; 2.40 A; A/B=374-620.
PDB; 5U73; X-ray; 3.35 A; A=334-1278.
PDB; 5U74; X-ray; 3.33 A; A=334-1278.
PDBsum; 3GKH; -.
PDBsum; 3GKI; -.
PDBsum; 3GKJ; -.
PDBsum; 3JD8; -.
PDBsum; 5F18; -.
PDBsum; 5F1B; -.
PDBsum; 5HNS; -.
PDBsum; 5JNX; -.
PDBsum; 5KWY; -.
PDBsum; 5U73; -.
PDBsum; 5U74; -.
ProteinModelPortal; O15118; -.
SMR; O15118; -.
BioGrid; 110925; 18.
DIP; DIP-53217N; -.
ELM; O15118; -.
IntAct; O15118; 9.
STRING; 9606.ENSP00000269228; -.
BindingDB; O15118; -.
ChEMBL; CHEMBL1293277; -.
SwissLipids; SLP:000000478; -.
TCDB; 2.A.6.6.1; the resistance-nodulation-cell division (rnd) superfamily.
GlyConnect; 1571; -.
iPTMnet; O15118; -.
PhosphoSitePlus; O15118; -.
SwissPalm; O15118; -.
BioMuta; NPC1; -.
EPD; O15118; -.
MaxQB; O15118; -.
PaxDb; O15118; -.
PeptideAtlas; O15118; -.
PRIDE; O15118; -.
ProteomicsDB; 48453; -.
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; -.
HPA; HPA077445; -.
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; ENSGT00900000140845; -.
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; Expressed in 226 organ(s), highest expression level in secondary oocyte.
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; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:1905103; C:integral component of lysosomal membrane; IDA:UniProtKB.
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; HDA:UniProtKB.
GO; GO:0005764; C:lysosome; ISS:UniProtKB.
GO; GO:0016020; C:membrane; HDA: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:0038023; F:signaling 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:0032367; P:intracellular cholesterol transport; IMP: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: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; NPC1-like.
InterPro; IPR032190; NPC1_N.
InterPro; IPR003392; Ptc/Disp.
InterPro; IPR000731; SSD.
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 NPC intracellular cholesterol transporter
1.
/FTId=PRO_0000023261.
TOPO_DOM 23 261 Lumenal. {ECO:0000269|PubMed:27238017}.
TRANSMEM 262 282 Helical. {ECO:0000269|PubMed:27238017}.
TOPO_DOM 283 350 Cytoplasmic.
{ECO:0000269|PubMed:27238017}.
TRANSMEM 351 371 Helical. {ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
TOPO_DOM 372 620 Lumenal. {ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
TRANSMEM 621 641 Helical. {ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
TOPO_DOM 642 653 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
TRANSMEM 654 675 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 676 685 Lumenal. {ECO:0000269|PubMed:28784760}.
TRANSMEM 686 706 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 707 730 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
TRANSMEM 731 751 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 752 759 Lumenal. {ECO:0000269|PubMed:28784760}.
TRANSMEM 760 783 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 784 832 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
TRANSMEM 833 853 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 854 1097 Lumenal. {ECO:0000269|PubMed:28784760}.
TRANSMEM 1098 1118 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 1119 1124 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
TRANSMEM 1125 1145 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 1146 1150 Lumenal. {ECO:0000269|PubMed:28784760}.
TRANSMEM 1151 1171 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 1172 1194 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
TRANSMEM 1195 1215 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 1216 1223 Lumenal. {ECO:0000269|PubMed:28784760}.
TRANSMEM 1224 1244 Helical. {ECO:0000269|PubMed:28784760}.
TOPO_DOM 1245 1278 Cytoplasmic.
{ECO:0000269|PubMed:28784760}.
DOMAIN 620 785 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REGION 175 205 Important for cholesterol binding and
cholesterol transfer from NPC1 to
liposomes.
REGION 1275 1278 Required for location in lysosomes.
{ECO:0000269|PubMed:9927649}.
MOTIF 1275 1278 Di-leucine motif. {ECO:0000305}.
COMPBIAS 249 259 Poly-Pro.
BINDING 41 41 Cholesterol. {ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000269|PubMed:19563754,
ECO:0000305|PubMed:27238017}.
BINDING 79 79 Cholesterol. {ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000269|PubMed:19563754,
ECO:0000305|PubMed:27238017}.
SITE 108 108 Important for cholesterol binding.
{ECO:0000269|PubMed:19563754}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:10821832}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000269|PubMed:27238017,
ECO:0000305|PubMed:10821832}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:27238017}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000269|PubMed:27238017,
ECO:0000305|PubMed:10821832}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:28784760}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:28784760}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5HNS,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:27238017}.
CARBOHYD 598 598 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
CARBOHYD 916 916 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 931 931 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 961 961 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 968 968 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
CARBOHYD 1064 1064 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
CARBOHYD 1072 1072 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 74 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 31 42 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 63 109 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 75 113 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 97 238 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 100 160 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 177 184 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 227 243 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5JNX,
ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
DISULFID 240 247 {ECO:0000244|PDB:3GKH,
ECO:0000244|PDB:3GKI,
ECO:0000244|PDB:3GKJ,
ECO:0000269|PubMed:19563754}.
DISULFID 468 479 {ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5F18,
ECO:0000244|PDB:5F1B,
ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5JNX,
ECO:0000244|PDB:5KWY,
ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:26771495,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
DISULFID 516 533 {ECO:0000244|PDB:3JD8,
ECO:0000244|PDB:5F18,
ECO:0000244|PDB:5F1B,
ECO:0000244|PDB:5HNS,
ECO:0000244|PDB:5JNX,
ECO:0000244|PDB:5KWY,
ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:26771495,
ECO:0000269|PubMed:26846330,
ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:28784760}.
DISULFID 909 914 {ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
DISULFID 956 1011 {ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
DISULFID 957 979 {ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
DISULFID 967 976 {ECO:0000244|PDB:5U73,
ECO:0000244|PDB:5U74,
ECO:0000269|PubMed:28784760}.
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 (polymorphism; no effect on
function; colocalizes with the wild-type
protein with Rab7-positive late
endosomes; clears the lysosomal
cholesterol accumulation in NPC1-
deficient cells; dbSNP:rs80358251).
{ECO:0000269|PubMed:11182931,
ECO:0000269|PubMed:11333381,
ECO:0000269|PubMed:11349231,
ECO:0000269|PubMed:12408188,
ECO:0000269|PubMed:12554680,
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 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; dbSNP:rs1053321823).
{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; dbSNP:rs1064793791).
{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; dbSNP:rs1190383931).
{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; decreased affinity for
NPC2; decreased cholesterol transfer from
NPC2 to NPC1; dbSNP:rs377515417).
{ECO:0000269|PubMed:11479732,
ECO:0000269|PubMed:27238017}.
/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; dbSNP:rs765652543).
{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; dbSNP:rs1057518942).
{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; dbSNP:rs1393388896).
{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; dbSNP:rs1057519242).
{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; dbSNP:rs1160114136).
{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; dbSNP:rs1428599096).
{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; dbSNP:rs34715591).
{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 25 257 Missing: Decreases affinity for NPC2.
Abolishes cholesterol transfer from NPC2
to NPC1. {ECO:0000269|PubMed:27238017}.
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 74 75 CC->SS: Loss of function.
{ECO:0000269|PubMed:9927649}.
MUTAGEN 82 83 TL->AA: Strongly reduces cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 88 88 Q->A: Decreased affinity for NPC2 and
decreased cholesterol transfer from NPC2
to NPC1; when associated with A-92 and A-
96. {ECO:0000269|PubMed:27238017}.
MUTAGEN 92 92 Q->A: Decreased affinity for NPC2 and
decreased cholesterol transfer from NPC2
to NPC1; when associated with A-88 and A-
96. {ECO:0000269|PubMed:27238017}.
MUTAGEN 96 96 R->A: Decreased affinity for NPC2 and
decreased cholesterol transfer from NPC2
to NPC1; when associated with A-88 and A-
92. {ECO:0000269|PubMed:27238017}.
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. Decreases
affinity for NPC2. Strongly reduces
cholesterol transfer to liposomes in a
NPC2-dependent manner.
{ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
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. Abolishes
cholesterol transfer from NPC2 to NPC1.
{ECO:0000269|PubMed:19563754,
ECO:0000269|PubMed:27238017}.
MUTAGEN 204 205 TI->AA: Strongly reduces cholesterol and
25-hydroxycholesterol binding.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 230 234 Missing: Decreased cholesterol transport.
{ECO:0000269|PubMed:28784760}.
MUTAGEN 249 257 Missing: Decreases affinity for NPC2.
Abolishes cholesterol transfer from NPC2
to NPC1. {ECO:0000269|PubMed:27238017}.
MUTAGEN 423 424 YP->GG: Strongly reduces interaction with
ebolavirus glycoprotein.
{ECO:0000269|PubMed:26771495}.
MUTAGEN 503 503 F->A,G: Loss of interaction with
ebolavirus glycoprotein.
{ECO:0000269|PubMed:26771495}.
MUTAGEN 504 504 F->A,G: Loss of interaction with
ebolavirus glycoprotein.
{ECO:0000269|PubMed:26771495}.
MUTAGEN 506 506 Y->A: Loss of interaction with ebolavirus
glycoprotein.
{ECO:0000269|PubMed:26771495}.
MUTAGEN 660 660 G->R: Loss of function.
{ECO:0000269|PubMed:19563754}.
MUTAGEN 691 691 P->S: Abolishes cholesterol transport. No
effect on subcellular location.
{ECO:0000269|PubMed:28784760}.
MUTAGEN 909 917 CGGMGCNND->A: Abolishes cholesterol
transport. No effect on subcellular
location. {ECO:0000269|PubMed:28784760}.
MUTAGEN 1275 1278 Missing: Loss of location in lysosomes.
{ECO:0000269|PubMed:9927649}.
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 335 348 {ECO:0000244|PDB:5U74}.
HELIX 351 368 {ECO:0000244|PDB:5U74}.
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}.
TURN 617 620 {ECO:0000244|PDB:5U74}.
HELIX 621 637 {ECO:0000244|PDB:5U74}.
HELIX 654 678 {ECO:0000244|PDB:5U74}.
HELIX 684 711 {ECO:0000244|PDB:5U74}.
HELIX 720 749 {ECO:0000244|PDB:5U74}.
HELIX 755 776 {ECO:0000244|PDB:5U74}.
HELIX 778 791 {ECO:0000244|PDB:5U74}.
TURN 796 798 {ECO:0000244|PDB:5U73}.
HELIX 818 830 {ECO:0000244|PDB:5U74}.
TURN 832 834 {ECO:0000244|PDB:5U74}.
HELIX 835 851 {ECO:0000244|PDB:5U74}.
TURN 852 855 {ECO:0000244|PDB:5U74}.
TURN 862 865 {ECO:0000244|PDB:5U74}.
STRAND 868 870 {ECO:0000244|PDB:5U73}.
HELIX 872 882 {ECO:0000244|PDB:5U74}.
STRAND 888 893 {ECO:0000244|PDB:5U74}.
HELIX 902 906 {ECO:0000244|PDB:5U74}.
STRAND 911 913 {ECO:0000244|PDB:5U74}.
HELIX 919 928 {ECO:0000244|PDB:5U74}.
TURN 930 932 {ECO:0000244|PDB:5U74}.
HELIX 943 950 {ECO:0000244|PDB:5U74}.
HELIX 952 954 {ECO:0000244|PDB:5U74}.
STRAND 958 960 {ECO:0000244|PDB:5U74}.
TURN 961 963 {ECO:0000244|PDB:5U74}.
STRAND 969 971 {ECO:0000244|PDB:5U74}.
STRAND 974 980 {ECO:0000244|PDB:5U74}.
TURN 984 987 {ECO:0000244|PDB:5U74}.
HELIX 994 1004 {ECO:0000244|PDB:5U74}.
TURN 1016 1019 {ECO:0000244|PDB:5U74}.
HELIX 1020 1022 {ECO:0000244|PDB:5U74}.
STRAND 1025 1033 {ECO:0000244|PDB:5U74}.
STRAND 1036 1041 {ECO:0000244|PDB:5U74}.
HELIX 1048 1068 {ECO:0000244|PDB:5U74}.
STRAND 1078 1081 {ECO:0000244|PDB:5U73}.
HELIX 1085 1088 {ECO:0000244|PDB:5U74}.
HELIX 1090 1092 {ECO:0000244|PDB:5U74}.
HELIX 1094 1116 {ECO:0000244|PDB:5U74}.
STRAND 1117 1119 {ECO:0000244|PDB:5U74}.
HELIX 1121 1144 {ECO:0000244|PDB:5U74}.
HELIX 1151 1176 {ECO:0000244|PDB:5U74}.
HELIX 1183 1198 {ECO:0000244|PDB:5U74}.
TURN 1199 1202 {ECO:0000244|PDB:5U74}.
HELIX 1203 1215 {ECO:0000244|PDB:5U74}.
HELIX 1219 1223 {ECO:0000244|PDB:5U74}.
HELIX 1225 1241 {ECO:0000244|PDB:5U74}.
HELIX 1243 1251 {ECO:0000244|PDB:5U74}.
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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