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NPC intracellular cholesterol transporter 1 (Niemann-Pick C1 protein)

 NPC1_MOUSE              Reviewed;        1277 AA.
O35604; G3X8W9; O35605;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
06-FEB-2013, sequence version 2.
20-JUN-2018, entry version 142.
RecName: Full=NPC intracellular cholesterol transporter 1 {ECO:0000312|MGI:MGI:1097712};
AltName: Full=Niemann-Pick C1 protein {ECO:0000303|PubMed:9211850};
Flags: Precursor;
Name=Npc1 {ECO:0000312|MGI:MGI:1097712};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=9211850; DOI=10.1126/science.277.5323.232;
Loftus S.K., Morris J.A., Carstea E.D., Gu J.Z., Cummings C.,
Brown A., Ellison J., Ohno K., Rosenfeld M.A., Tagle D.A.,
Pentchev P.G., Pavan W.J.;
"Murine model of Niemann-Pick C disease: mutation in a cholesterol
homeostasis gene.";
Science 277:232-235(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
SUBCELLULAR LOCATION.
PubMed=9990080; DOI=10.1073/pnas.96.4.1657;
Patel S.C., Suresh S., Kumar U., Hu C.Y., Cooney A.,
Blanchette-Mackie E.J., Neufeld E.B., Patel R.C., Brady R.O.,
Patel Y.C., Pentchev P.G., Ong W.-Y.;
"Localization of Niemann-Pick C1 protein in astrocytes: implications
for neuronal degeneration in Niemann-Pick type C disease.";
Proc. Natl. Acad. Sci. U.S.A. 96:1657-1662(1999).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
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).
[7]
INTERACTION WITH NPC2, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=22065762; DOI=10.1073/pnas.1110439108;
Deffieu M.S., Pfeffer S.R.;
"Niemann-Pick type C 1 function requires lumenal domain residues that
mediate cholesterol-dependent NPC2 binding.";
Proc. Natl. Acad. Sci. U.S.A. 108:18932-18936(2011).
-!- FUNCTION: Intracellular cholesterol transporter which acts in
concert with NPC2 and plays an important role in the egress of
cholesterol from the endosomal/lysosomal compartment. Both NPC1
and NPC2 function as the cellular 'tag team duo' (TTD) to catalyze
the mobilization of cholesterol within the multivesicular
environment of the late endosome (LE) to effect egress through the
limiting bilayer of the LE. NPC2 binds unesterified cholesterol
that has been released from LDLs in the lumen of the late
endosomes/lysosomes and transfers it to the cholesterol-binding
pocket of the N-terminal domain of NPC1. Cholesterol binds to NPC1
with the hydroxyl group buried in the binding pocket and is
exported from the limiting membrane of late endosomes/ lysosomes
to the ER and plasma membrane by an unknown mechanism. Binds
oxysterol with higher affinity than cholesterol. May play a role
in vesicular trafficking in glia, a process that may be crucial
for maintaining the structural and functional integrity of nerve
terminals.
-!- SUBUNIT: Interacts with TMEM97 (By similarity). Interacts (via the
second lumenal domain) with NPC2 in a cholestrol-dependent manner.
{ECO:0000250, ECO:0000269|PubMed:22065762}.
-!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
protein. Lysosome membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Expressed predominantly in perisynaptic
astrocytic glial processes. Also expressed in heart, spleen, lung,
liver, skeletal muscle, kidney, testis.
-!- INDUCTION: Activated by the drugs progesterone and U-18666A which
block cholesterol transport out of lysosomes and by the
lysosomotropic agent NAH4CL.
-!- 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.
-!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF003348; AAB63372.1; -; mRNA.
EMBL; AF003349; AAB63373.1; -; Genomic_DNA.
EMBL; AC102096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC102248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466622; EDL01560.1; -; Genomic_DNA.
CCDS; CCDS29064.1; -.
PIR; T30188; T30188.
RefSeq; NP_032746.2; NM_008720.2.
UniGene; Mm.3484; -.
ProteinModelPortal; O35604; -.
SMR; O35604; -.
STRING; 10090.ENSMUSP00000025279; -.
ChEMBL; CHEMBL2321610; -.
SwissLipids; SLP:000000479; -.
iPTMnet; O35604; -.
PhosphoSitePlus; O35604; -.
SwissPalm; O35604; -.
EPD; O35604; -.
MaxQB; O35604; -.
PaxDb; O35604; -.
PeptideAtlas; O35604; -.
PRIDE; O35604; -.
Ensembl; ENSMUST00000025279; ENSMUSP00000025279; ENSMUSG00000024413.
GeneID; 18145; -.
KEGG; mmu:18145; -.
UCSC; uc008ecb.1; mouse.
CTD; 4864; -.
MGI; MGI:1097712; Npc1.
eggNOG; KOG1933; Eukaryota.
eggNOG; ENOG410XR54; LUCA.
GeneTree; ENSGT00900000140845; -.
HOGENOM; HOG000036674; -.
HOVERGEN; HBG003913; -.
InParanoid; O35604; -.
KO; K12385; -.
OMA; MYNACRD; -.
OrthoDB; EOG091G00JD; -.
TreeFam; TF300416; -.
Reactome; R-MMU-8964038; LDL clearance.
ChiTaRS; Npc1; mouse.
PRO; PR:O35604; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024413; -.
CleanEx; MM_NPC1; -.
Genevisible; O35604; MM.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0031982; C:vesicle; IDA:MGI.
GO; GO:0015485; F:cholesterol binding; ISS:UniProtKB.
GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
GO; GO:0007628; P:adult walking behavior; IGI:MGI.
GO; GO:0006914; P:autophagy; ISO:MGI.
GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IDA:MGI.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:MGI.
GO; GO:0033344; P:cholesterol efflux; IMP:MGI.
GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0030301; P:cholesterol transport; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:MGI.
GO; GO:0090150; P:establishment of protein localization to membrane; ISO:MGI.
GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
GO; GO:0031579; P:membrane raft organization; ISO:MGI.
GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
GO; GO:0016242; P:negative regulation of macroautophagy; IMP:MGI.
GO; GO:0006486; P:protein glycosylation; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; ISO:MGI.
GO; GO:0042493; P:response to drug; IDA:MGI.
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;
Cholesterol metabolism; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Lipid metabolism; Lysosome; Membrane;
Reference proteome; Signal; Steroid metabolism; Sterol metabolism;
Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1277 NPC intracellular cholesterol transporter
1.
/FTId=PRO_0000023262.
TOPO_DOM 23 269 Lumenal. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TOPO_DOM 291 350 Cytoplasmic. {ECO:0000255}.
TRANSMEM 351 371 Helical. {ECO:0000255}.
TOPO_DOM 372 621 Lumenal. {ECO:0000255}.
TRANSMEM 622 642 Helical. {ECO:0000255}.
TOPO_DOM 643 653 Cytoplasmic. {ECO:0000255}.
TRANSMEM 654 674 Helical. {ECO:0000255}.
TOPO_DOM 675 683 Lumenal. {ECO:0000255}.
TRANSMEM 684 704 Helical. {ECO:0000255}.
TOPO_DOM 705 730 Cytoplasmic. {ECO:0000255}.
TRANSMEM 731 751 Helical. {ECO:0000255}.
TOPO_DOM 752 759 Lumenal. {ECO:0000255}.
TRANSMEM 760 780 Helical. {ECO:0000255}.
TOPO_DOM 781 832 Cytoplasmic. {ECO:0000255}.
TRANSMEM 833 853 Helical. {ECO:0000255}.
TOPO_DOM 854 1076 Lumenal. {ECO:0000255}.
TRANSMEM 1077 1094 Helical. {ECO:0000255}.
TOPO_DOM 1095 1097 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1098 1118 Helical. {ECO:0000255}.
TOPO_DOM 1119 1123 Lumenal. {ECO:0000255}.
TRANSMEM 1124 1144 Helical. {ECO:0000255}.
TOPO_DOM 1145 1145 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1146 1166 Helical. {ECO:0000255}.
TOPO_DOM 1167 1194 Lumenal. {ECO:0000255}.
TRANSMEM 1195 1215 Helical. {ECO:0000255}.
TOPO_DOM 1216 1226 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1227 1247 Helical. {ECO:0000255}.
TOPO_DOM 1248 1277 Lumenal. {ECO:0000255}.
DOMAIN 620 785 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
REGION 175 205 Important for cholesterol binding and
cholesterol transfer from NPC1 to
liposomes. {ECO:0000250}.
MOTIF 1274 1277 Di-leucine motif.
COMPBIAS 249 259 Poly-Pro.
BINDING 41 41 Cholesterol. {ECO:0000250}.
BINDING 79 79 Cholesterol. {ECO:0000250}.
SITE 108 108 Important for cholesterol binding.
{ECO:0000250}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 137 137 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 524 524 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 868 868 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 898 898 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 916 916 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 961 961 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 968 968 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1063 1063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 74 {ECO:0000250}.
DISULFID 31 42 {ECO:0000250}.
DISULFID 63 109 {ECO:0000250}.
DISULFID 75 113 {ECO:0000250}.
DISULFID 97 238 {ECO:0000250}.
DISULFID 100 160 {ECO:0000250}.
DISULFID 177 184 {ECO:0000250}.
DISULFID 227 243 {ECO:0000250}.
DISULFID 240 247 {ECO:0000250}.
CONFLICT 9 9 G -> GL (in Ref. 1; AAB63372).
{ECO:0000305}.
CONFLICT 135 135 Q -> P (in Ref. 1; AAB63372).
{ECO:0000305}.
CONFLICT 147 147 F -> Y (in Ref. 1; AAB63372).
{ECO:0000305}.
CONFLICT 445 445 D -> N (in Ref. 1; AAB63372).
{ECO:0000305}.
CONFLICT 478 478 N -> D (in Ref. 1; AAB63373).
{ECO:0000305}.
CONFLICT 874 875 DY -> AN (in Ref. 1; AAB63372).
{ECO:0000305}.
SEQUENCE 1277 AA; 142885 MW; 3B42230AAC86764E CRC64;
MGAHHPALGL LLLLLCPAQV FSQSCVWYGE CGIATGDKRY NCKYSGPPKP LPKDGYDLVQ
ELCPGLFFDN VSLCCDIQQL QTLKSNLQLP LQFLSRCPSC FYNLMTLFCE LTCSPHQSQF
LNVTATEDYF DPKTQENKTN VKELEYFVGQ SFANAMYNAC RDVEAPSSNE KALGLLCGRD
ARACNATNWI EYMFNKDNGQ APFTIIPVFS DLSILGMEPM RNATKGCNES VDEVTGPCSC
QDCSIVCGPK PQPPPPPMPW RIWGLDAMYV IMWVTYVAFL FVFFGALLAV WCHRRRYFVS
EYTPIDSNIA FSVNSSDKGE ASCCDPLGAA FDDCLRRMFT KWGAFCVRNP TCIIFFSLAF
ITVCSSGLVF VQVTTNPVEL WSAPHSQARL EKEYFDKHFG PFFRTEQLII QAPNTSVHIY
EPYPAGADVP FGPPLNKEIL HQVLDLQIAI ESITASYNNE TVTLQDICVA PLSPYNKNCT
IMSVLNYFQN SHAVLDSQVG DDFYIYADYH THFLYCVRAP ASLNDTSLLH GPCLGTFGGP
VFPWLVLGGY DDQNYNNATA LVITFPVNNY YNDTERLQRA WAWEKEFISF VKNYKNPNLT
ISFTAERSIE DELNRESNSD VFTVIISYVV MFLYISLALG HIQSCSRLLV DSKISLGIAG
ILIVLSSVAC SLGIFSYMGM PLTLIVIEVI PFLVLAVGVD NIFILVQTYQ RDERLQEETL
DQQLGRILGE VAPTMFLSSF SETSAFFFGA LSSMPAVHTF SLFAGMAVLI DFLLQITCFV
SLLGLDIKRQ EKNHLDILCC VRGADDGQGS HASESYLFRF FKNYFAPLLL KDWLRPIVVA
VFVGVLSFSV AVVNKVDIGL DQSLSMPNDS YVIDYFKSLA QYLHSGPPVY FVLEEGYNYS
SRKGQNMVCG GMGCDNDSLV QQIFNAAELD TYTRVGFAPS SWIDDYFDWV SPQSSCCRLY
NVTHQFCNAS VMDPTCVRCR PLTPEGKQRP QGKEFMKFLP MFLSDNPNPK CGKGGHAAYG
SAVNIVGDDT YIGATYFMTY HTILKTSADY TDAMKKARLI ASNITETMRS KGSDYRVFPY
SVFYVFYEQY LTIIDDTIFN LSVSLGSIFL VTLVVLGCEL WSAVIMCITI AMILVNMFGV
MWLWGISLNA VSLVNLVMSC GISVEFCSHI TRAFTMSTKG SRVSRAEEAL AHMGSSVFSG
ITLTKFGGIV VLAFAKSQIF EIFYFRMYLA MVLLGATHGL IFLPVLLSYI GPSVNKAKRH
TTYERYRGTE RERLLNF


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