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Epididymal secretory protein E1 (Human epididymis-specific protein 1) (He1) (Niemann-Pick disease type C2 protein)

 NPC2_HUMAN              Reviewed;         151 AA.
P61916; B4DQV7; Q15668; Q29413;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
05-DEC-2018, entry version 144.
RecName: Full=NPC intracellular cholesterol transporter 2 {ECO:0000312|HGNC:HGNC:14537};
AltName: Full=Epididymal secretory protein E1;
AltName: Full=Human epididymis-specific protein 1;
Short=He1 {ECO:0000303|PubMed:11125141, ECO:0000303|PubMed:8418812};
AltName: Full=Niemann-Pick disease type C2 protein {ECO:0000303|PubMed:17018531};
Flags: Precursor;
Name=NPC2 {ECO:0000312|HGNC:HGNC:14537}; Synonyms=HE1;
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).
TISSUE=Epididymis;
PubMed=8418812; DOI=10.1002/mrd.1080340104;
Krull N., Ivell R., Osterhoff C., Kirchhoff C.;
"Region-specific variation of gene expression in the human epididymis
as revealed by in situ hybridization with tissue-specific cDNAs.";
Mol. Reprod. Dev. 34:16-24(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary;
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).
[5]
PROTEIN SEQUENCE OF N-TERMINUS, GLYCOSYLATION AT ASN-58 AND ASN-135,
AND FUNCTION.
TISSUE=Brain;
PubMed=17018531; DOI=10.1074/jbc.M608743200;
Liou H.L., Dixit S.S., Xu S., Tint G.S., Stock A.M., Lobel P.;
"NPC2, the protein deficient in Niemann-Pick C2 disease, consists of
multiple glycoforms that bind a variety of sterols.";
J. Biol. Chem. 281:36710-36723(2006).
[6]
INVOLVEMENT IN NPC2, PROTEIN SEQUENCE OF N-TERMINUS, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=11125141; DOI=10.1126/science.290.5500.2298;
Naureckiene S., Sleat D.E., Lackland H., Fensom A., Vanier M.T.,
Wattiaux R., Jadot M., Lobel P.;
"Identification of HE1 as the second gene of Niemann-Pick C disease.";
Science 290:2298-2301(2000).
[7]
INTERACTION WITH DHDDS.
PubMed=15110773; DOI=10.1016/j.bbrc.2004.04.007;
Kharel Y., Takahashi S., Yamashita S., Koyama T.;
"In vivo interaction between the human dehydrodolichyl diphosphate
synthase and the Niemann-Pick C2 protein revealed by a yeast two-
hybrid system.";
Biochem. Biophys. Res. Commun. 318:198-203(2004).
[8]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[9]
FUNCTION.
PubMed=18823126; DOI=10.1021/bi801328u;
Xu Z., Farver W., Kodukula S., Storch J.;
"Regulation of sterol transport between membranes and NPC2.";
Biochemistry 47:11134-11143(2008).
[10]
FUNCTION, INTERACTION WITH NPC1, AND CHARACTERIZATION OF VARIANT NPC2
SER-120.
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 NEDD4L, AND TISSUE SPECIFICITY.
PubMed=19664597; DOI=10.1016/j.bbrc.2009.07.158;
Araki N., Ishigami T., Ushio H., Minegishi S., Umemura M., Miyagi Y.,
Aoki I., Morinaga H., Tamura K., Toya Y., Uchino K., Umemura S.;
"Identification of NPC2 protein as interaction molecule with C2 domain
of human Nedd4L.";
Biochem. Biophys. Res. Commun. 388:290-296(2009).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH NUS1.
PubMed=19723497; DOI=10.1016/j.cmet.2009.07.003;
Harrison K.D., Miao R.Q., Fernandez-Hernando C., Suarez Y.,
Davalos A., Sessa W.C.;
"Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates
intracellular cholesterol trafficking.";
Cell Metab. 10:208-218(2009).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-135.
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).
[14]
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).
[15]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=21315718; DOI=10.1053/j.gastro.2011.01.050;
Yamanashi Y., Takada T., Yoshikado T., Shoda J., Suzuki H.;
"NPC2 regulates biliary cholesterol secretion via stimulation of
ABCG5/G8-mediated cholesterol transport.";
Gastroenterology 140:1664-1674(2011).
[16]
INTERACTION WITH NPC1L1.
PubMed=22095670; DOI=10.1002/hep.24772;
Yamanashi Y., Takada T., Shoda J., Suzuki H.;
"Novel function of Niemann-Pick C1-like 1 as a negative regulator of
Niemann-Pick C2 protein.";
Hepatology 55:953-964(2012).
[17]
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).
[18]
REVIEW ON FUNCTION.
PubMed=19232397; DOI=10.1016/j.bbalip.2009.02.001;
Storch J., Xu Z.;
"Niemann-Pick C2 (NPC2) and intracellular cholesterol trafficking.";
Biochim. Biophys. Acta 1791:671-678(2009).
[19]
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).
[20]
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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
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).
[23]
FUNCTION, AND INTERACTION WITH NPC1.
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).
[24]
FUNCTION.
PubMed=29580834; DOI=10.1016/j.chemphyslip.2018.03.006;
Berzina Z., Solanko L.M., Mehadi A.S., Jensen M.L.V., Lund F.W.,
Modzel M., Szomek M., Solanko K.A., Dupont A., Nielsen G.K.,
Heegaard C.W., Ejsing C.S., Wuestner D.;
"Niemann-Pick C2 protein regulates sterol transport between plasma
membrane and late endosomes in human fibroblasts.";
Chem. Phys. Lipids 213:48-61(2018).
[25] {ECO:0000244|PDB:5KWY}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-151 IN COMPLEX WITH
CHOLESTEROL AND NPC1, INTERACTION WITH NPC1, GLYCOSYLATION AT ASN-58
AND ASN-135, 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).
[26]
VARIANT NPC2 PRO-67.
PubMed=11567215; DOI=10.1086/324068;
Millat G., Chikh K., Naureckiene S., Sleat D.E., Fensom A.H.,
Higaki K., Elleder M., Lobel P., Vanier M.T.;
"Niemann-Pick disease type C: spectrum of HE1 mutations and
genotype/phenotype correlations in the NPC2 group.";
Am. J. Hum. Genet. 69:1013-1021(2001).
[27]
VARIANT NPC2 MET-39.
PubMed=12447927; DOI=10.1002/ana.10366;
Klunemann H.H., Elleder M., Kaminski W.E., Snow K., Peyser J.M.,
O'Brien J.F., Munoz D., Schmitz G., Klein H.E., Pendlebury W.W.;
"Frontal lobe atrophy due to a mutation in the cholesterol binding
protein HE1/NPC2.";
Ann. Neurol. 52:743-749(2002).
[28]
VARIANTS NPC2 MET-30; PHE-47 AND PHE-93.
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).
[29]
VARIANT NPC2 ARG-99, CHARACTERIZATION OF VARIANTS NPC2 METH-39;
PHE-47; PRO-67; PHE-93 AND ARG-99, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=15937921; DOI=10.1002/humu.20173;
Chikh K., Rodriguez C., Vey S., Vanier M.T., Millat G.;
"Niemann-Pick type C disease: subcellular location and functional
characterization of NPC2 proteins with naturally occurring missense
mutations.";
Hum. Mutat. 26:20-28(2005).
[30]
VARIANT NPC2 SER-120.
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).
-!- FUNCTION: Intracellular cholesterol transporter which acts in
concert with NPC1 and plays an important role in the egress of
cholesterol from the lysosomal compartment (PubMed:17018531,
PubMed:11125141, PubMed:18772377, PubMed:29580834,
PubMed:15937921). 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:17018531, PubMed:18772377,
PubMed:27238017). May bind and mobilize cholesterol that is
associated with membranes (PubMed:18823126). NPC2 binds
cholesterol with a 1:1 stoichiometry (PubMed:17018531). Can bind a
variety of sterols, including lathosterol, desmosterol and the
plant sterols stigmasterol and beta-sitosterol (PubMed:17018531).
The secreted form of NCP2 regulates biliary cholesterol secretion
via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By
similarity). {ECO:0000250|UniProtKB:Q9Z0J0,
ECO:0000269|PubMed:11125141, ECO:0000269|PubMed:15937921,
ECO:0000269|PubMed:17018531, ECO:0000269|PubMed:18772377,
ECO:0000269|PubMed:18823126, ECO:0000269|PubMed:27238017,
ECO:0000269|PubMed:29580834}.
-!- SUBUNIT: Interacts with NPC1 (via the second lumenal domain) in a
cholestrol-dependent manner (PubMed:18772377, PubMed:27238017,
PubMed:27551080). Interacts with NUS1/NgBR, the interaction
stabilizes NCP2 and regulates cholesterol trafficking
(PubMed:19723497). Interacts with DHDDS (PubMed:15110773).
Interacts with NEDD4L (via C2 domain) (PubMed:19664597). Interacts
with NPC1L1 (PubMed:22095670). {ECO:0000269|PubMed:15110773,
ECO:0000269|PubMed:18772377, ECO:0000269|PubMed:19664597,
ECO:0000269|PubMed:19723497, ECO:0000269|PubMed:22095670,
ECO:0000269|PubMed:27238017, ECO:0000269|PubMed:27551080}.
-!- INTERACTION:
Q7Z3B1:NEGR1; NbExp=9; IntAct=EBI-2368946, EBI-4314838;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11125141,
ECO:0000269|PubMed:15937921, ECO:0000269|PubMed:19723497,
ECO:0000269|PubMed:21315718}. Endoplasmic reticulum
{ECO:0000269|PubMed:19723497}. Lysosome
{ECO:0000269|PubMed:15937921, ECO:0000269|PubMed:19723497,
ECO:0000305|PubMed:11125141}. Note=Interaction with cell-surface
M6PR mediates endocytosis and targeting to lysosomes.
{ECO:0000305|PubMed:11125141}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P61916-1; Sequence=Displayed;
Name=2;
IsoId=P61916-2; Sequence=VSP_056459;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in gallbladder bile
(PubMed:21315718). Detected in fibroblasts, kidney, liver, spleen,
small intestine, placenta and testis (at protein level)
(PubMed:11125141). Epididymis. {ECO:0000269|PubMed:11125141,
ECO:0000269|PubMed:19664597, ECO:0000269|PubMed:21315718}.
-!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
infection. {ECO:0000269|PubMed:16548883}.
-!- DOMAIN: Binds cholesterol in a hydrophobic pocket; there are no
hydrogen bonds between the sterol and the protein.
{ECO:0000250|UniProtKB:P79345}.
-!- DISEASE: Niemann-Pick disease C2 (NPC2) [MIM:607625]: 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 C2 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. {ECO:0000269|PubMed:11125141,
ECO:0000269|PubMed:11567215, ECO:0000269|PubMed:12447927,
ECO:0000269|PubMed:12955717, ECO:0000269|PubMed:15937921,
ECO:0000269|PubMed:16126423, ECO:0000269|PubMed:18772377}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the NPC2 family. {ECO:0000305}.
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EMBL; X67698; CAA47928.1; -; mRNA.
EMBL; AK298975; BAG61069.1; -; mRNA.
EMBL; AC005479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002532; AAH02532.1; -; mRNA.
CCDS; CCDS32121.1; -. [P61916-1]
PIR; I38365; I38365.
RefSeq; NP_006423.1; NM_006432.3. [P61916-1]
UniGene; Hs.433222; -.
PDB; 5KWY; X-ray; 2.40 A; C/D=20-151.
PDBsum; 5KWY; -.
ProteinModelPortal; P61916; -.
SMR; P61916; -.
BioGrid; 115828; 30.
IntAct; P61916; 5.
MINT; P61916; -.
STRING; 9606.ENSP00000451112; -.
SwissLipids; SLP:000000475; -.
TCDB; 2.A.6.6.1; the resistance-nodulation-cell division (rnd) superfamily.
GlyConnect; 1215; -.
iPTMnet; P61916; -.
PhosphoSitePlus; P61916; -.
BioMuta; NPC2; -.
DMDM; 48429027; -.
EPD; P61916; -.
MaxQB; P61916; -.
PaxDb; P61916; -.
PeptideAtlas; P61916; -.
PRIDE; P61916; -.
ProteomicsDB; 57337; -.
TopDownProteomics; P61916-2; -. [P61916-2]
DNASU; 10577; -.
Ensembl; ENST00000541064; ENSP00000442488; ENSG00000119655. [P61916-2]
Ensembl; ENST00000555619; ENSP00000451112; ENSG00000119655. [P61916-1]
GeneID; 10577; -.
KEGG; hsa:10577; -.
UCSC; uc001xpy.4; human. [P61916-1]
CTD; 10577; -.
DisGeNET; 10577; -.
EuPathDB; HostDB:ENSG00000119655.8; -.
GeneCards; NPC2; -.
GeneReviews; NPC2; -.
HGNC; HGNC:14537; NPC2.
HPA; HPA000835; -.
MalaCards; NPC2; -.
MIM; 601015; gene.
MIM; 607625; phenotype.
neXtProt; NX_P61916; -.
OpenTargets; ENSG00000119655; -.
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; PA31700; -.
eggNOG; KOG4063; Eukaryota.
eggNOG; ENOG4111Q8S; LUCA.
GeneTree; ENSGT00390000006223; -.
HOGENOM; HOG000007181; -.
HOVERGEN; HBG018181; -.
InParanoid; P61916; -.
KO; K13443; -.
PhylomeDB; P61916; -.
TreeFam; TF317963; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-8964038; LDL clearance.
ChiTaRS; NPC2; human.
GenomeRNAi; 10577; -.
PMAP-CutDB; P61916; -.
PRO; PR:P61916; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119655; Expressed in 234 organ(s), highest expression level in corpus epididymis.
CleanEx; HS_NPC2; -.
ExpressionAtlas; P61916; baseline and differential.
Genevisible; P61916; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB.
GO; GO:0017127; F:cholesterol transporter activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
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:0046836; P:glycolipid transport; TAS:HGNC.
GO; GO:0032367; P:intracellular cholesterol transport; IDA:UniProtKB.
GO; GO:0032366; P:intracellular sterol transport; IDA:HGNC.
GO; GO:0034383; P:low-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0015914; P:phospholipid transport; TAS:HGNC.
GO; GO:0019747; P:regulation of isoprenoid metabolic process; TAS:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
CDD; cd00916; Npc2_like; 1.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR003172; ML_dom.
InterPro; IPR033916; ML_Npc2-like.
InterPro; IPR039670; NPC2-like.
PANTHER; PTHR11306; PTHR11306; 1.
Pfam; PF02221; E1_DerP2_DerF2; 1.
SMART; SM00737; ML; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Cholesterol metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Lipid metabolism; Lipid transport; Lysosome; Niemann-Pick disease;
Polymorphism; Reference proteome; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:11125141,
ECO:0000269|PubMed:17018531}.
CHAIN 20 151 NPC intracellular cholesterol transporter
2.
/FTId=PRO_0000019854.
MOD_RES 116 116 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z0J0}.
CARBOHYD 58 58 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5KWY,
ECO:0000269|PubMed:17018531,
ECO:0000269|PubMed:27551080}.
CARBOHYD 135 135 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:5KWY,
ECO:0000269|PubMed:17018531,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:27551080}.
DISULFID 27 140 {ECO:0000244|PDB:5KWY,
ECO:0000269|PubMed:27551080}.
DISULFID 42 47 {ECO:0000244|PDB:5KWY,
ECO:0000269|PubMed:27551080}.
DISULFID 93 99 {ECO:0000244|PDB:5KWY,
ECO:0000269|PubMed:27551080}.
VAR_SEQ 122 147 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056459.
VARIANT 30 30 V -> M (in NPC2; dbSNP:rs151220873).
{ECO:0000269|PubMed:12955717}.
/FTId=VAR_043303.
VARIANT 39 39 V -> M (in NPC2; results in the synthesis
of functional recombinant proteins
correctly targeted to lysosomes;
dbSNP:rs80358261).
{ECO:0000269|PubMed:12447927,
ECO:0000269|PubMed:15937921}.
/FTId=VAR_015848.
VARIANT 47 47 C -> F (in NPC2; leads to the synthesis
of misfolded recombinant proteins that
colocalized with an endoplasmic reticulum
marker; normally secreted but unable to
correct cholesterol storage in NPC2-
deficient cells).
{ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:15937921}.
/FTId=VAR_043304.
VARIANT 67 67 S -> P (in NPC2; leads to the synthesis
of misfolded recombinant proteins that
colocalized with an endoplasmic reticulum
marker; normally secreted but unable to
correct cholesterol storage in NPC2-
deficient cells; dbSNP:rs11694).
{ECO:0000269|PubMed:11567215,
ECO:0000269|PubMed:15937921}.
/FTId=VAR_015849.
VARIANT 86 86 P -> L (in dbSNP:rs4688).
/FTId=VAR_011899.
VARIANT 93 93 C -> F (in NPC2; leads to the synthesis
of misfolded recombinant proteins that
colocalized with an endoplasmic reticulum
marker; normally secreted but unable to
correct cholesterol storage in NPC2-
deficient cells; dbSNP:rs143960270).
{ECO:0000269|PubMed:12955717,
ECO:0000269|PubMed:15937921}.
/FTId=VAR_043305.
VARIANT 99 99 C -> R (in NPC2; leads to the synthesis
of misfolded recombinant proteins that
colocalized with an endoplasmic reticulum
marker; normally secreted but unable to
correct cholesterol storage in NPC2-
deficient cells; dbSNP:rs80358264).
{ECO:0000269|PubMed:15937921}.
/FTId=VAR_043306.
VARIANT 120 120 P -> S (in NPC2; unable to bind
cholesterol; dbSNP:rs104894458).
{ECO:0000269|PubMed:16126423,
ECO:0000269|PubMed:18772377}.
/FTId=VAR_043307.
STRAND 25 27 {ECO:0000244|PDB:5KWY}.
STRAND 30 41 {ECO:0000244|PDB:5KWY}.
STRAND 47 50 {ECO:0000244|PDB:5KWY}.
STRAND 53 65 {ECO:0000244|PDB:5KWY}.
STRAND 71 78 {ECO:0000244|PDB:5KWY}.
STRAND 81 84 {ECO:0000244|PDB:5KWY}.
HELIX 92 94 {ECO:0000244|PDB:5KWY}.
STRAND 99 101 {ECO:0000244|PDB:5KWY}.
STRAND 105 115 {ECO:0000244|PDB:5KWY}.
STRAND 123 131 {ECO:0000244|PDB:5KWY}.
STRAND 137 150 {ECO:0000244|PDB:5KWY}.
SEQUENCE 151 AA; 16570 MW; B141B611805DC910 CRC64;
MRFLAATFLL LALSTAAQAE PVQFKDCGSV DGVIKEVNVS PCPTQPCQLS KGQSYSVNVT
FTSNIQSKSS KAVVHGILMG VPVPFPIPEP DGCKSGINCP IQKDKTYSYL NKLPVKSEYP
SIKLVVEWQL QDDKNQSLFC WEIPVQIVSH L


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