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NPC1-like intracellular cholesterol transporter 1 (Niemann-Pick C1-like protein 1)

 NPCL1_MOUSE             Reviewed;        1333 AA.
Q6T3U4; Q5SVX1;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
10-OCT-2018, entry version 105.
RecName: Full=NPC1-like intracellular cholesterol transporter 1 {ECO:0000312|MGI:MGI:2685089};
AltName: Full=Niemann-Pick C1-like protein 1 {ECO:0000303|PubMed:14976318};
Flags: Precursor;
Name=Npc1l1 {ECO:0000312|MGI:MGI:2685089};
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=14976318; DOI=10.1126/science.1093131;
Altmann S.W., Davis H.R. Jr., Zhu L.-J., Yao X., Hoos L.M.,
Tetzloff G., Iyer S.P.N., Maguire M., Golovko A., Zeng M., Wang L.,
Murgolo N., Graziano M.P.;
"Niemann-Pick C1 like 1 protein is critical for intestinal cholesterol
absorption.";
Science 303:1201-1204(2004).
[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]
FUNCTION, AND INDUCTION.
PubMed=15173162; DOI=10.1074/jbc.M405817200;
Davis H.R. Jr., Zhu L.-J., Hoos L.M., Tetzloff G., Maguire M., Liu J.,
Yao X., Iyer S.P.N., Lam M.-H., Lund E.G., Detmers P.A.,
Graziano M.P., Altmann S.W.;
"Niemann-Pick C1 Like 1 (NPC1L1) is the intestinal phytosterol and
cholesterol transporter and a key modulator of whole-body cholesterol
homeostasis.";
J. Biol. Chem. 279:33586-33592(2004).
[4]
TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15671032; DOI=10.1074/jbc.M409110200;
Davies J.P., Scott C., Oishi K., Liapis A., Ioannou Y.A.;
"Inactivation of NPC1L1 causes multiple lipid transport defects and
protects against diet-induced hypercholesterolemia.";
J. Biol. Chem. 280:12710-12720(2005).
[5]
INDUCTION.
PubMed=15604518; DOI=10.1194/jlr.M400400-JLR200;
van der Veen J.N., Kruit J.K., Havinga R., Baller J.F.W., Chimini G.,
Lestavel S., Staels B., Groot P.H.E., Groen A.K., Kuipers F.;
"Reduced cholesterol absorption upon PPARdelta activation coincides
with decreased intestinal expression of NPC1L1.";
J. Lipid Res. 46:526-534(2005).
[6]
INTERACTION WITH LIMA1.
PubMed=29880681; DOI=10.1126/science.aao6575;
Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J.,
Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y.,
Li B.L., Ma Y.T., Song B.L.;
"A LIMA1 variant promotes low plasma LDL cholesterol and decreases
intestinal cholesterol absorption.";
Science 360:1087-1092(2018).
-!- FUNCTION: Plays a major role in cholesterol homeostasis. Is
critical for the uptake of both phytosterol and cholesterol across
the plasma membrane of the intestinal enterocyte. Is the direct
molecular target of ezetimibe, a drug that inhibits cholesterol
absorption (By similarity). The protein may have a function in the
transport of multiple lipids and their homeostasis, and may play a
critical role in regulating lipid metabolism. Acts as a negative
regulator of NPC2 and down-regulates its expression and secretion
by inhibiting its maturation and accelerating its degradation (By
similarity). {ECO:0000250, ECO:0000269|PubMed:14976318,
ECO:0000269|PubMed:15173162, ECO:0000269|PubMed:15671032}.
-!- SUBUNIT: Interacts with RAB11A, MYO5B and RAB11FIP2. Interaction
with RAB11A, MYO5B and RAB11FIP2 is required for proper transport
to the plasma membrane upon cholesterol depletion (By similarity).
Interacts with NPC2 (By similarity). Interacts with LIMA1
(PubMed:29880681). {ECO:0000250, ECO:0000269|PubMed:29880681}.
-!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
protein. Cell membrane {ECO:0000250|UniProtKB:Q6T3U3}; Multi-pass
membrane protein. Note=Subfractionation of brush border membranes
from proximal enterocytes suggests considerable association with
the apical membrane fraction. Exists as a predominantly cell
surface membrane expressed protein.
-!- TISSUE SPECIFICITY: Expressed in small intestine, stomach and
muscle, along with detectable expression in lung, heart, gall
bladder, brain, testis, skin and liver. Expression in liver is
extremely low. {ECO:0000269|PubMed:14976318,
ECO:0000269|PubMed:15671032}.
-!- INDUCTION: Cholesterol/cholate feeding resulted in down-regulation
of intestinal expression. Expression is decreased by 35% in the
jejunum upon PPARD activation. {ECO:0000269|PubMed:15173162,
ECO:0000269|PubMed:15604518}.
-!- PTM: Highly glycosylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice have multiple lipid transport defects
and have a protective effect against diet-induced hyperlipidemia.
They have also a deregulation of CAV1 transport and localization,
suggesting that the observed lipid transport defect may be the
indirect result of an inability of cells to properly target and/or
regulate CAV1 expression. {ECO:0000269|PubMed:15671032}.
-!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY437866; AAR97887.1; -; mRNA.
EMBL; AL607152; CAI24395.1; -; Genomic_DNA.
CCDS; CCDS24413.1; -.
UniGene; Mm.212492; -.
ProteinModelPortal; Q6T3U4; -.
SMR; Q6T3U4; -.
STRING; 10090.ENSMUSP00000004505; -.
BindingDB; Q6T3U4; -.
ChEMBL; CHEMBL1075296; -.
iPTMnet; Q6T3U4; -.
PhosphoSitePlus; Q6T3U4; -.
MaxQB; Q6T3U4; -.
PaxDb; Q6T3U4; -.
PRIDE; Q6T3U4; -.
MGI; MGI:2685089; Npc1l1.
eggNOG; KOG1933; Eukaryota.
eggNOG; ENOG410XR54; LUCA.
HOGENOM; HOG000036674; -.
HOVERGEN; HBG003913; -.
InParanoid; Q6T3U4; -.
PhylomeDB; Q6T3U4; -.
TreeFam; TF300416; -.
PRO; PR:Q6T3U4; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_NPC1L1; -.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0031526; C:brush border membrane; ISO:MGI.
GO; GO:0044214; C:spanning component of plasma membrane; ISO:MGI.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
GO; GO:0031489; F:myosin V binding; ISO:MGI.
GO; GO:0017137; F:Rab GTPase binding; ISO:MGI.
GO; GO:0071501; P:cellular response to sterol depletion; ISO:MGI.
GO; GO:0006695; P:cholesterol biosynthetic process; ISO:MGI.
GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
GO; GO:0030301; P:cholesterol transport; ISO:MGI.
GO; GO:0030299; P:intestinal cholesterol absorption; ISO:MGI.
GO; GO:0042157; P:lipoprotein metabolic process; ISO:MGI.
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;
Cell membrane; Cholesterol metabolism; Complete proteome;
Disulfide bond; Glycoprotein; Lipid metabolism; Membrane;
Reference proteome; Signal; Steroid metabolism; Sterol metabolism;
Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1333 NPC1-like intracellular cholesterol
transporter 1.
/FTId=PRO_0000023267.
TOPO_DOM 21 284 Extracellular. {ECO:0000255}.
TRANSMEM 285 305 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 306 352 Cytoplasmic. {ECO:0000255}.
TRANSMEM 353 373 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 374 632 Extracellular. {ECO:0000255}.
TRANSMEM 633 653 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 654 665 Cytoplasmic. {ECO:0000255}.
TRANSMEM 666 686 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 687 696 Extracellular. {ECO:0000255}.
TRANSMEM 697 717 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 718 742 Cytoplasmic. {ECO:0000255}.
TRANSMEM 743 763 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 764 776 Extracellular. {ECO:0000255}.
TRANSMEM 777 797 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 798 846 Cytoplasmic. {ECO:0000255}.
TRANSMEM 847 867 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 868 1113 Extracellular. {ECO:0000255}.
TRANSMEM 1114 1134 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 1135 1142 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1143 1163 Helical; Name=10. {ECO:0000255}.
TOPO_DOM 1164 1165 Extracellular. {ECO:0000255}.
TRANSMEM 1166 1186 Helical; Name=11. {ECO:0000255}.
TOPO_DOM 1187 1206 Cytoplasmic. {ECO:0000255}.
TRANSMEM 1207 1227 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 1228 1242 Extracellular. {ECO:0000255}.
TRANSMEM 1243 1263 Helical; Name=13. {ECO:0000255}.
TOPO_DOM 1264 1333 Cytoplasmic. {ECO:0000255}.
DOMAIN 632 797 SSD. {ECO:0000255|PROSITE-
ProRule:PRU00199}.
COMPBIAS 267 270 Poly-Pro.
COMPBIAS 500 503 Poly-Leu.
DISULFID 32 90 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 38 56 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 77 125 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 91 129 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 113 254 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 116 172 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 189 197 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 243 259 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 256 263 {ECO:0000250|UniProtKB:Q9UHC9}.
DISULFID 471 485 {ECO:0000250|UniProtKB:O15118}.
DISULFID 525 542 {ECO:0000250|UniProtKB:O15118}.
DISULFID 920 925 {ECO:0000250|UniProtKB:O15118}.
DISULFID 967 1025 {ECO:0000250|UniProtKB:O15118}.
DISULFID 981 990 {ECO:0000250|UniProtKB:O15118}.
CONFLICT 476 476 N -> K (in Ref. 2; CAI24395).
{ECO:0000305}.
SEQUENCE 1333 AA; 147132 MW; 7771520D9B352735 CRC64;
MAAAWQGWLL WALLLNSAQG ELYTPTHKAG FCTFYEECGK NPELSGGLTS LSNISCLSNT
PARHVTGDHL ALLQRVCPRL YNGPNDTYAC CSTKQLVSLD SSLSITKALL TRCPACSENF
VSIHCHNTCS PDQSLFINVT RVVQRDPGQL PAVVAYEAFY QRSFAEKAYE SCSRVRIPAA
ASLAVGSMCG VYGSALCNAQ RWLNFQGDTG NGLAPLDITF HLLEPGQALA DGMKPLDGKI
TPCNESQGED SAACSCQDCA ASCPVIPPPP ALRPSFYMGR MPGWLALIII FTAVFVLLSV
VLVYLRVASN RNKNKTAGSQ EAPNLPRKRR FSPHTVLGRF FESWGTRVAS WPLTVLALSF
IVVIALSVGL TFIELTTDPV ELWSAPKSQA RKEKAFHDEH FGPFFRTNQI FVTAKNRSSY
KYDSLLLGPK NFSGILSLDL LQELLELQER LRHLQVWSHE AQRNISLQDI CYAPLNPHNT
SLTDCCVNSL LQYFQNNHTL LLLTANQTLN GQTSLVDWKD HFLYCANAPL TYKDGTALAL
SCIADYGAPV FPFLAVGGYQ GTDYSEAEAL IITFSINNYP ADDPRMAHAK LWEEAFLKEM
QSFQRSTADK FQIAFSAERS LEDEINRTTI QDLPVFAISY LIVFLYISLA LGSYSRWSRV
AVDSKATLGL GGVAVVLGAV VAAMGFYSYL GVPSSLVIIQ VVPFLVLAVG ADNIFIFVLE
YQRLPRMPGE QREAHIGRTL GSVAPSMLLC SLSEAICFFL GALTSMPAVR TFALTSGLAI
IFDFLLQMTA FVALLSLDSK RQEASRPDVV CCFSSRNLPP PKQKEGLLLC FFRKIYTPFL
LHRFIRPVVL LLFLVLFGAN LYLMCNISVG LDQDLALPKD SYLIDYFLFL NRYLEVGPPV
YFDTTSGYNF STEAGMNAIC SSAGCESFSL TQKIQYASEF PNQSYVAIAA SSWVDDFIDW
LTPSSSCCRI YTRGPHKDEF CPSTDTSFNC LKNCMNRTLG PVRPTTEQFH KYLPWFLNDT
PNIRCPKGGL AAYRTSVNLS SDGQIIASQF MAYHKPLRNS QDFTEALRAS RLLAANITAE
LRKVPGTDPN FEVFPYTISN VFYQQYLTVL PEGIFTLALC FVPTFVVCYL LLGLDIRSGI
LNLLSIIMIL VDTIGLMAVW GISYNAVSLI NLVTAVGMSV EFVSHITRSF AVSTKPTRLE
RAKDATIFMG SAVFAGVAMT NFPGILILGF AQAQLIQIFF FRLNLLITLL GLLHGLVFLP
VVLSYLGPDV NQALVLEEKL ATEAAMVSEP SCPQYPFPAD ANTSDYVNYG FNPEFIPEIN
AASSSLPKSD QKF


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