ID NPCL1_HUMAN Reviewed; 1359 AA. AC Q9UHC9; A4D2J7; B7ZLE6; D3DVK9; Q17RV5; Q6R3Q4; Q9UHC8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=NPC1-like intracellular cholesterol transporter 1 {ECO:0000312|HGNC:HGNC:7898}; DE Short=NPC1L1 {ECO:0000303|PubMed:15928087}; DE AltName: Full=Niemann-Pick C1-like protein 1 {ECO:0000303|PubMed:10783261}; DE Flags: Precursor; GN Name=NPC1L1 {ECO:0000312|HGNC:HGNC:7898}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE SPECIFICITY. RX PubMed=10783261; DOI=10.1006/geno.2000.6151; RA Davies J.P., Levy B., Ioannou Y.A.; RT "Evidence for a Niemann-Pick C (NPC) gene family: identification and RT characterization of NPC1L1."; RL Genomics 65:137-145(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=14976318; DOI=10.1126/science.1093131; RA Altmann S.W., Davis H.R. Jr., Zhu L.-J., Yao X., Hoos L.M., Tetzloff G., RA Iyer S.P.N., Maguire M., Golovko A., Zeng M., Wang L., Murgolo N., RA Graziano M.P.; RT "Niemann-Pick C1 like 1 protein is critical for intestinal cholesterol RT absorption."; RL Science 303:1201-1204(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TOPOLOGY. RX PubMed=19325169; DOI=10.1194/jlr.m800669-jlr200; RA Wang J., Chu B.-B., Ge L., Li B.-L., Yan Y., Song B.L.; RT "Membrane topology of human NPC1L1, a key protein in enterohepatic RT cholesterol absorption."; RL J. Lipid Res. 50:1653-1662(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=15671032; DOI=10.1074/jbc.m409110200; RA Davies J.P., Scott C., Oishi K., Liapis A., Ioannou Y.A.; RT "Inactivation of NPC1L1 causes multiple lipid transport defects and RT protects against diet-induced hypercholesterolemia."; RL J. Biol. Chem. 280:12710-12720(2005). RN [9] RP INDUCTION. RX PubMed=15604518; DOI=10.1194/jlr.m400400-jlr200; RA van der Veen J.N., Kruit J.K., Havinga R., Baller J.F.W., Chimini G., RA Lestavel S., Staels B., Groot P.H.E., Groen A.K., Kuipers F.; RT "Reduced cholesterol absorption upon PPARdelta activation coincides with RT decreased intestinal expression of NPC1L1."; RL J. Lipid Res. 46:526-534(2005). RN [10] RP FUNCTION. RX PubMed=15928087; DOI=10.1073/pnas.0500269102; RA Garcia-Calvo M., Lisnock J., Bull H.G., Hawes B.E., Burnett D.A., RA Braun M.P., Crona J.H., Davis H.R. Jr., Dean D.C., Detmers P.A., RA Graziano M.P., Hughes M., MacIntyre D.E., Ogawa A., O'neill K.A., RA Iyer S.P.N., Shevell D.E., Smith M.M., Tang Y.S., Makarewicz A.M., RA Ujjainwalla F., Altmann S.W., Chapman K.T., Thornberry N.A.; RT "The target of ezetimibe is Niemann-Pick C1-like 1 (NPC1L1)."; RL Proc. Natl. Acad. Sci. U.S.A. 102:8132-8137(2005). RN [11] RP INTERACTION WITH RAB11A; MYO5B AND RAB11FIP2. RX PubMed=19542231; DOI=10.1074/jbc.m109.034355; RA Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L., RA Song B.-L.; RT "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol- RT regulated translocation of NPC1L1 to the cell surface."; RL J. Biol. Chem. 284:22481-22490(2009). RN [12] RP FUNCTION, AND INTERACTION WITH NPC2. RX PubMed=22095670; DOI=10.1002/hep.24772; RA Yamanashi Y., Takada T., Shoda J., Suzuki H.; RT "Novel function of Niemann-Pick C1-like 1 as a negative regulator of RT Niemann-Pick C2 protein."; RL Hepatology 55:953-964(2012). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 22-284, DISULFIDE BONDS, AND RP GLYCOSYLATION AT ASN-54 AND ASN-138. RX PubMed=21525977; DOI=10.1371/journal.pone.0018722; RA Kwon H.J., Palnitkar M., Deisenhofer J.; RT "The structure of the NPC1L1 N-terminal domain in a closed conformation."; RL PLoS ONE 6:E18722-E18722(2011). RN [14] RP VARIANTS LEU-55 AND ASN-1233, AND POLYMORPHISM. RX PubMed=15679830; DOI=10.1111/j.1399-0004.2004.00388.x; RA Wang J., Williams C.M., Hegele R.A.; RT "Compound heterozygosity for two non-synonymous polymorphisms in NPC1L1 in RT a non-responder to ezetimibe."; RL Clin. Genet. 67:175-177(2005). RN [15] RP VARIANTS 167-GLN--PHE-1359 DEL; 406-ARG--PHE-1359 DEL; 483-TYR--PHE-1359 RP DEL; 592-TRP--PHE-1359 DEL; 601-ARG--PHE-1359 DEL; 604-GLN--PHE-1359 DEL; RP 738-ARG--PHE-1359 DEL; 803-GLU--PHE-1359 DEL; 967-CYS--PHE-1359 DEL AND RP 1325-ARG--PHE-1359 DEL, POLYMORPHISM, AND INVOLVEMENT IN LDLCQ7. RX PubMed=25390462; DOI=10.1056/nejmoa1405386; RG Myocardial Infarction Genetics Consortium Investigators; RA Stitziel N.O., Won H.H., Morrison A.C., Peloso G.M., Do R., Lange L.A., RA Fontanillas P., Gupta N., Duga S., Goel A., Farrall M., Saleheen D., RA Ferrario P., Koenig I., Asselta R., Merlini P.A., Marziliano N., RA Notarangelo M.F., Schick U., Auer P., Assimes T.L., Reilly M., Wilensky R., RA Rader D.J., Hovingh G.K., Meitinger T., Kessler T., Kastrati A., RA Laugwitz K.L., Siscovick D., Rotter J.I., Hazen S.L., Tracy R., Cresci S., RA Spertus J., Jackson R., Schwartz S.M., Natarajan P., Crosby J., Muzny D., RA Ballantyne C., Rich S.S., O'Donnell C.J., Abecasis G., Sunaev S., RA Nickerson D.A., Buring J.E., Ridker P.M., Chasman D.I., Austin E., RA Kullo I.J., Weeke P.E., Shaffer C.M., Bastarache L.A., Denny J.C., RA Roden D.M., Palmer C., Deloukas P., Lin D.Y., Tang Z.Z., Erdmann J., RA Schunkert H., Danesh J., Marrugat J., Elosua R., Ardissino D., RA McPherson R., Watkins H., Reiner A.P., Wilson J.G., Altshuler D., RA Gibbs R.A., Lander E.S., Boerwinkle E., Gabriel S., Kathiresan S.; RT "Inactivating mutations in NPC1L1 and protection from coronary heart RT disease."; RL N. Engl. J. Med. 371:2072-2082(2014). RN [16] RP INTERACTION WITH LIMA1, AND MUTAGENESIS OF 1300-LEU--GLU-1303; RP 1304-GLN--ARG-1306 AND 1308-GLU-GLU-1309. RX PubMed=29880681; DOI=10.1126/science.aao6575; RA Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J., RA Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y., Li B.L., RA Ma Y.T., Song B.L.; RT "A LIMA1 variant promotes low plasma LDL cholesterol and decreases RT intestinal cholesterol absorption."; RL Science 360:1087-1092(2018). CC -!- FUNCTION: Plays a major role in cholesterol homeostasis CC (PubMed:22095670). Critical for the uptake of cholesterol across the CC plasma membrane of the intestinal enterocyte (PubMed:22095670). CC Involved in plant sterol absorption, it transports sitosterol, although CC at lower rates than cholesterol (By similarity). Is the direct CC molecular target of ezetimibe, a drug that inhibits cholesterol CC absorption and is approved for the treatment of hypercholesterolemia CC (PubMed:15928087). May have a function in the transport of multiple CC lipids and their homeostasis, thereby influencing lipid metabolism CC regulation (PubMed:15671032). May be involved in caveolin trafficking CC from the plasma membrane (By similarity). In addition, acts as a CC negative regulator of NPC2 and down-regulates its expression and CC secretion by inhibiting its maturation and accelerating its degradation CC (PubMed:22095670). {ECO:0000250|UniProtKB:Q6T3U3, CC ECO:0000250|UniProtKB:Q6T3U4, ECO:0000269|PubMed:15928087, CC ECO:0000269|PubMed:22095670, ECO:0000305|PubMed:15671032}. CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747, CC ChEBI:CHEBI:16113; Evidence={ECO:0000305|PubMed:15671032, CC ECO:0000305|PubMed:22095670}; CC -!- CATALYTIC ACTIVITY: CC Reaction=sitosterol(out) = sitosterol(in); Xref=Rhea:RHEA:70723, CC ChEBI:CHEBI:27693; Evidence={ECO:0000250|UniProtKB:Q6T3U3}; CC -!- SUBUNIT: Interacts with RAB11A, MYO5B and RAB11FIP2. Interaction with CC RAB11A, MYO5B and RAB11FIP2 is required for proper transport to the CC plasma membrane upon cholesterol depletion. Interacts with NPC2. CC Interacts with LIMA1 (PubMed:29880681). {ECO:0000269|PubMed:19542231, CC ECO:0000269|PubMed:22095670, ECO:0000269|PubMed:29880681}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:15671032}; Multi-pass membrane protein CC {ECO:0000269|PubMed:15671032}. Cell membrane CC {ECO:0000250|UniProtKB:Q6T3U3}; Multi-pass membrane protein CC {ECO:0000250}. Cytoplasmic vesicle membrane CC {ECO:0000269|PubMed:15671032}; Multi-pass membrane protein CC {ECO:0000269|PubMed:15671032}. Note=Subfractionation of brush border CC membranes from proximal enterocytes suggests considerable association CC with the apical membrane fraction. Exists as a predominantly cell CC surface membrane expressed protein (By similarity). According to CC PubMed:15671032, localizes in a subcellular vesicular compartment rich CC in RAB5. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9UHC9-1; Sequence=Displayed; CC Name=2; Synonyms=NPC1L1DELTAE15; CC IsoId=Q9UHC9-2; Sequence=VSP_015314; CC Name=3; Synonyms=NPCL1T; CC IsoId=Q9UHC9-3; Sequence=VSP_015312, VSP_015313; CC Name=4; CC IsoId=Q9UHC9-4; Sequence=VSP_054503, VSP_015314; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in liver. Also CC expressed in small intestine, pancreas, kidney, lung, pancreas, spleen, CC heart, gall bladder, brain, testis, stomach and muscle. CC {ECO:0000269|PubMed:10783261, ECO:0000269|PubMed:14976318, CC ECO:0000269|PubMed:15671032}. CC -!- INDUCTION: Expression is decreased in Caco-2 cells upon PPARD CC activation. {ECO:0000269|PubMed:15604518}. CC -!- PTM: Highly glycosylated. {ECO:0000250}. CC -!- POLYMORPHISM: Genetic variations in NPC1L1 influence low density CC lipoprotein cholesterol (LDL-C) content defining the low density CC lipoprotein cholesterol level quantitative trait locus 7 (LDLCQ7) CC [MIM:617966]. Inactivating variants may confer a lower risk of coronary CC heart disease (PubMed:25390462). Rare NPC1L1 variants also influence CC response to ezetimibe, a drug that reduces plasma LDL-C by blocking CC sterol absorption in enterocytes (PubMed:15679830). CC {ECO:0000269|PubMed:15679830, ECO:0000269|PubMed:25390462}. CC -!- MISCELLANEOUS: Target of cholesterol lowering drugs. CC {ECO:0000269|PubMed:21525977}. CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF192522; AAF20396.1; -; mRNA. DR EMBL; AF192523; AAF20397.1; -; mRNA. DR EMBL; AY515256; AAS56939.1; -; mRNA. DR EMBL; AY437865; AAR97886.1; -; mRNA. DR EMBL; FJ481111; ACL18055.1; -; mRNA. DR EMBL; AC004938; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236960; EAL23753.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61096.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61097.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61098.1; -; Genomic_DNA. DR EMBL; BC117178; AAI17179.1; -; mRNA. DR EMBL; BC143756; AAI43757.1; -; mRNA. DR CCDS; CCDS43575.1; -. [Q9UHC9-2] DR CCDS; CCDS5491.1; -. [Q9UHC9-1] DR CCDS; CCDS75587.1; -. [Q9UHC9-3] DR RefSeq; NP_001095118.1; NM_001101648.1. DR RefSeq; NP_001287896.1; NM_001300967.1. [Q9UHC9-3] DR RefSeq; NP_037521.2; NM_013389.2. [Q9UHC9-1] DR PDB; 3QNT; X-ray; 2.83 A; A=22-284. DR PDB; 7DF8; EM; 3.03 A; A=1-1301. DR PDB; 7DFW; EM; 2.69 A; A=1-1315. DR PDB; 7DFZ; EM; 3.58 A; A=1-1300. DR PDB; 7N4U; EM; 3.34 A; A/B=1-1359. DR PDB; 7N4V; EM; 3.58 A; A/B=1-1359. DR PDB; 7N4X; EM; 3.33 A; A=1-1359. DR PDBsum; 3QNT; -. DR PDBsum; 7DF8; -. DR PDBsum; 7DFW; -. DR PDBsum; 7DFZ; -. DR PDBsum; 7N4U; -. DR PDBsum; 7N4V; -. DR PDBsum; 7N4X; -. DR AlphaFoldDB; Q9UHC9; -. DR EMDB; EMD-24178; -. DR EMDB; EMD-24179; -. DR EMDB; EMD-24180; -. DR EMDB; EMD-30662; -. DR EMDB; EMD-30666; -. DR EMDB; EMD-30668; -. DR SMR; Q9UHC9; -. DR BioGRID; 118936; 2. DR IntAct; Q9UHC9; 1. DR STRING; 9606.ENSP00000289547; -. DR BindingDB; Q9UHC9; -. DR ChEMBL; CHEMBL2027; -. DR DrugBank; DB00973; Ezetimibe. DR DrugBank; DB11635; Tocofersolan. DR DrugBank; DB00163; Vitamin E. DR DrugCentral; Q9UHC9; -. DR GuidetoPHARMACOLOGY; 2629; -. DR SwissLipids; SLP:000001532; -. DR TCDB; 2.A.6.6.6; the resistance-nodulation-cell division (rnd) superfamily. DR GlyCosmos; Q9UHC9; 11 sites, No reported glycans. DR GlyGen; Q9UHC9; 11 sites. DR iPTMnet; Q9UHC9; -. DR PhosphoSitePlus; Q9UHC9; -. DR SwissPalm; Q9UHC9; -. DR BioMuta; NPC1L1; -. DR DMDM; 425906049; -. DR jPOST; Q9UHC9; -. DR MassIVE; Q9UHC9; -. DR PaxDb; 9606-ENSP00000289547; -. DR PeptideAtlas; Q9UHC9; -. DR ProteomicsDB; 7220; -. DR ProteomicsDB; 84317; -. [Q9UHC9-1] DR ProteomicsDB; 84318; -. [Q9UHC9-2] DR ProteomicsDB; 84319; -. [Q9UHC9-3] DR Pumba; Q9UHC9; -. DR Antibodypedia; 13403; 224 antibodies from 22 providers. DR DNASU; 29881; -. DR Ensembl; ENST00000289547.8; ENSP00000289547.4; ENSG00000015520.15. [Q9UHC9-1] DR Ensembl; ENST00000423141.1; ENSP00000404670.1; ENSG00000015520.15. [Q9UHC9-3] DR GeneID; 29881; -. DR KEGG; hsa:29881; -. DR UCSC; uc003tlb.4; human. [Q9UHC9-1] DR AGR; HGNC:7898; -. DR CTD; 29881; -. DR DisGeNET; 29881; -. DR GeneCards; NPC1L1; -. DR HGNC; HGNC:7898; NPC1L1. DR HPA; ENSG00000015520; Group enriched (intestine, liver). DR MalaCards; NPC1L1; -. DR MIM; 608010; gene. DR MIM; 617966; phenotype. DR neXtProt; NX_Q9UHC9; -. DR OpenTargets; ENSG00000015520; -. DR Orphanet; 426; NON RARE IN EUROPE: Familial hypobetalipoproteinemia. DR PharmGKB; PA31699; -. DR VEuPathDB; HostDB:ENSG00000015520; -. DR eggNOG; KOG1933; Eukaryota. DR GeneTree; ENSGT00940000159904; -. DR HOGENOM; CLU_002359_6_0_1; -. DR InParanoid; Q9UHC9; -. DR OrthoDB; 2786103at2759; -. DR PhylomeDB; Q9UHC9; -. DR TreeFam; TF300416; -. DR PathwayCommons; Q9UHC9; -. DR Reactome; R-HSA-8963678; Intestinal lipid absorption. [Q9UHC9-2] DR SignaLink; Q9UHC9; -. DR SIGNOR; Q9UHC9; -. DR BioGRID-ORCS; 29881; 21 hits in 1156 CRISPR screens. DR ChiTaRS; NPC1L1; human. DR GenomeRNAi; 29881; -. DR Pharos; Q9UHC9; Tclin. DR PRO; PR:Q9UHC9; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UHC9; Protein. DR Bgee; ENSG00000015520; Expressed in jejunal mucosa and 101 other cell types or tissues. DR ExpressionAtlas; Q9UHC9; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0008431; F:vitamin E binding; IDA:UniProtKB. DR GO; GO:0071501; P:cellular response to sterol depletion; IDA:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; IMP:HGNC-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central. DR GO; GO:0030301; P:cholesterol transport; IMP:UniProtKB. DR GO; GO:0030299; P:intestinal cholesterol absorption; IMP:HGNC-UCL. DR GO; GO:0042157; P:lipoprotein metabolic process; IMP:HGNC-UCL. DR GO; GO:0042360; P:vitamin E metabolic process; IDA:UniProtKB. DR GO; GO:0051180; P:vitamin transport; IDA:UniProtKB. DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2. DR InterPro; IPR032190; NPC1_N. DR InterPro; IPR003392; Ptc/Disp. DR InterPro; IPR000731; SSD. DR PANTHER; PTHR45727; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1. DR PANTHER; PTHR45727:SF3; NPC1-LIKE INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1. DR Pfam; PF16414; NPC1_N; 1. DR Pfam; PF02460; Patched; 1. DR Pfam; PF12349; Sterol-sensing; 1. DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2. DR PROSITE; PS50156; SSD; 1. DR Genevisible; Q9UHC9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cholesterol metabolism; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Lipid metabolism; KW Membrane; Reference proteome; Signal; Steroid metabolism; KW Sterol metabolism; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..1359 FT /note="NPC1-like intracellular cholesterol transporter 1" FT /id="PRO_0000023266" FT TOPO_DOM 22..284 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 285..305 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 306..351 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 352..372 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 373..632 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 633..653 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 654..666 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 667..687 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 688..696 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 697..717 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 718..742 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 743..763 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 764..776 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 777..797 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 798..846 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 847..867 FT /note="Helical; Name=8" FT /evidence="ECO:0000255" FT TOPO_DOM 868..1139 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 1140..1160 FT /note="Helical; Name=9" FT /evidence="ECO:0000255" FT TOPO_DOM 1161..1168 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 1169..1189 FT /note="Helical; Name=10" FT /evidence="ECO:0000255" FT TOPO_DOM 1190..1191 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 1192..1212 FT /note="Helical; Name=11" FT /evidence="ECO:0000255" FT TOPO_DOM 1213..1236 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 1237..1257 FT /note="Helical; Name=12" FT /evidence="ECO:0000255" FT TOPO_DOM 1258..1268 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 1269..1289 FT /note="Helical; Name=13" FT /evidence="ECO:0000255" FT TOPO_DOM 1290..1359 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 632..797 FT /note="SSD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21525977" FT CARBOHYD 132 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:21525977" FT CARBOHYD 244 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 416 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 431 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 464 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 479 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 497 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 506 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 626 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 33..90 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 39..57 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 78..125 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 91..129 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 113..254 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 116..172 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 189..197 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 243..259 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 256..263 FT /evidence="ECO:0000269|PubMed:21525977" FT DISULFID 471..485 FT /evidence="ECO:0000250|UniProtKB:O15118" FT DISULFID 525..542 FT /evidence="ECO:0000250|UniProtKB:O15118" FT DISULFID 920..925 FT /evidence="ECO:0000250|UniProtKB:O15118" FT DISULFID 966..1024 FT /evidence="ECO:0000250|UniProtKB:O15118" FT DISULFID 980..989 FT /evidence="ECO:0000250|UniProtKB:O15118" FT VAR_SEQ 723..724 FT /note="RL -> GP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10783261" FT /id="VSP_015312" FT VAR_SEQ 725..1359 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10783261" FT /id="VSP_015313" FT VAR_SEQ 850..895 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054503" FT VAR_SEQ 1046..1072 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:10783261, FT ECO:0000303|PubMed:14976318, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:19325169" FT /id="VSP_015314" FT VARIANT 55 FT /note="V -> L (found in a non-responder to ezetimibe FT treatment; dbSNP:rs119457968)" FT /evidence="ECO:0000269|PubMed:15679830" FT /id="VAR_023369" FT VARIANT 167..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080844" FT VARIANT 406..1359 FT /note="Missing (protective factor against coronary heart FT disease; correlated with low LDL-C content)" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080845" FT VARIANT 483..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080846" FT VARIANT 510 FT /note="M -> I (in dbSNP:rs1468384)" FT /id="VAR_056659" FT VARIANT 592..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080847" FT VARIANT 601..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080848" FT VARIANT 604..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080849" FT VARIANT 738..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080850" FT VARIANT 803..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080851" FT VARIANT 967..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080852" FT VARIANT 1233 FT /note="I -> N (found in a non-responder to ezetimibe FT treatment; dbSNP:rs52815063)" FT /evidence="ECO:0000269|PubMed:15679830" FT /id="VAR_023370" FT VARIANT 1308 FT /note="E -> K (in dbSNP:rs217435)" FT /id="VAR_056660" FT VARIANT 1325..1359 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:25390462" FT /id="VAR_080853" FT MUTAGEN 1300..1303 FT /note="LALE->AAAA: Does not affect interaction with LIMA1." FT /evidence="ECO:0000269|PubMed:29880681" FT MUTAGEN 1304..1306 FT /note="QKR->AAA: Abolishes interaction with LIMA1." FT /evidence="ECO:0000269|PubMed:29880681" FT MUTAGEN 1308..1309 FT /note="EE->AA: Does not affect interaction with LIMA1." FT /evidence="ECO:0000269|PubMed:29880681" FT CONFLICT 1073 FT /note="T -> A (in Ref. 1; AAF20396 and 7; AAI43757)" FT /evidence="ECO:0000305" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 68..77 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 93..109 FT /evidence="ECO:0007829|PDB:3QNT" FT TURN 110..112 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 114..129 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 152..161 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 199..206 FT /evidence="ECO:0007829|PDB:3QNT" FT TURN 209..212 FT /evidence="ECO:0007829|PDB:3QNT" FT STRAND 215..223 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:3QNT" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:3QNT" FT TURN 256..258 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:3QNT" FT HELIX 335..350 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 352..367 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 389..401 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 406..411 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 425..427 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 429..432 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 438..452 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 455..458 FT /evidence="ECO:0007829|PDB:7DF8" FT TURN 459..461 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 463..466 FT /evidence="ECO:0007829|PDB:7DF8" FT HELIX 467..470 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 474..476 FT /evidence="ECO:0007829|PDB:7N4X" FT STRAND 477..479 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:7N4X" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 490..494 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 505..511 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 513..516 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 518..527 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 535..538 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 545..548 FT /evidence="ECO:0007829|PDB:7N4U" FT HELIX 552..554 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 556..558 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 560..562 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 569..576 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 585..606 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 608..610 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 620..625 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 630..632 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 633..636 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 638..646 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 647..649 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 657..659 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 660..663 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 666..689 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 696..723 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 732..761 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 767..798 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 802..805 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 808..810 FT /evidence="ECO:0007829|PDB:7N4X" FT HELIX 828..832 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 833..840 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 843..863 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 864..866 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 873..876 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 877..880 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 883..893 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 899..904 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 913..917 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 921..924 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 930..938 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 941..943 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 946..951 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 953..960 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 961..978 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 986..994 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 998..1000 FT /evidence="ECO:0007829|PDB:7N4X" FT HELIX 1005..1017 FT /evidence="ECO:0007829|PDB:7DFW" FT TURN 1029..1031 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 1032..1038 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 1040..1042 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 1073..1080 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1086..1107 FT /evidence="ECO:0007829|PDB:7DFW" FT STRAND 1119..1122 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1126..1129 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1131..1133 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1135..1156 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1162..1185 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1192..1204 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1206..1217 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1224..1252 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1253..1256 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1260..1265 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1268..1282 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1285..1291 FT /evidence="ECO:0007829|PDB:7DFW" FT HELIX 1298..1300 FT /evidence="ECO:0007829|PDB:7N4U" FT HELIX 1301..1312 FT /evidence="ECO:0007829|PDB:7DFW" SQ SEQUENCE 1359 AA; 148728 MW; 594F698B48D66DE7 CRC64; MAEAGLRGWL LWALLLRLAQ SEPYTTIHQP GYCAFYDECG KNPELSGSLM TLSNVSCLSN TPARKITGDH LILLQKICPR LYTGPNTQAC CSAKQLVSLE ASLSITKALL TRCPACSDNF VNLHCHNTCS PNQSLFINVT RVAQLGAGQL PAVVAYEAFY QHSFAEQSYD SCSRVRVPAA ATLAVGTMCG VYGSALCNAQ RWLNFQGDTG NGLAPLDITF HLLEPGQAVG SGIQPLNEGV ARCNESQGDD VATCSCQDCA ASCPAIARPQ ALDSTFYLGQ MPGSLVLIII LCSVFAVVTI LLVGFRVAPA RDKSKMVDPK KGTSLSDKLS FSTHTLLGQF FQGWGTWVAS WPLTILVLSV IPVVALAAGL VFTELTTDPV ELWSAPNSQA RSEKAFHDQH FGPFFRTNQV ILTAPNRSSY RYDSLLLGPK NFSGILDLDL LLELLELQER LRHLQVWSPE AQRNISLQDI CYAPLNPDNT SLYDCCINSL LQYFQNNRTL LLLTANQTLM GQTSQVDWKD HFLYCANAPL TFKDGTALAL SCMADYGAPV FPFLAIGGYK GKDYSEAEAL IMTFSLNNYP AGDPRLAQAK LWEEAFLEEM RAFQRRMAGM FQVTFMAERS LEDEINRTTA EDLPIFATSY IVIFLYISLA LGSYSSWSRV MVDSKATLGL GGVAVVLGAV MAAMGFFSYL GIRSSLVILQ VVPFLVLSVG ADNIFIFVLE YQRLPRRPGE PREVHIGRAL GRVAPSMLLC SLSEAICFFL GALTPMPAVR TFALTSGLAV ILDFLLQMSA FVALLSLDSK RQEASRLDVC CCVKPQELPP PGQGEGLLLG FFQKAYAPFL LHWITRGVVL LLFLALFGVS LYSMCHISVG LDQELALPKD SYLLDYFLFL NRYFEVGAPV YFVTTLGYNF SSEAGMNAIC SSAGCNNFSF TQKIQYATEF PEQSYLAIPA SSWVDDFIDW LTPSSCCRLY ISGPNKDKFC PSTVNSLNCL KNCMSITMGS VRPSVEQFHK YLPWFLNDRP NIKCPKGGLA AYSTSVNLTS DGQVLDTVAI LSPRLEYSGT ISAHCNLYLL DSTSRFMAYH KPLKNSQDYT EALRAARELA ANITADLRKV PGTDPAFEVF PYTITNVFYE QYLTILPEGL FMLSLCLVPT FAVSCLLLGL DLRSGLLNLL SIVMILVDTV GFMALWGISY NAVSLINLVS AVGMSVEFVS HITRSFAIST KPTWLERAKE ATISMGSAVF AGVAMTNLPG ILVLGLAKAQ LIQIFFFRLN LLITLLGLLH GLVFLPVILS YVGPDVNPAL ALEQKRAEEA VAAVMVASCP NHPSRVSTAD NIYVNHSFEG SIKGAGAISN FLPNNGRQF //