NPC1_YEAST
ID NPC1_YEAST Reviewed; 1170 AA.
AC Q12200; D6W406;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NPC intracellular sterol transporter 1-related protein 1 {ECO:0000305};
DE AltName: Full=Niemann-Pick type C-related protein 1 {ECO:0000312|SGD:S000005927};
DE Flags: Precursor;
GN Name=NCR1 {ECO:0000312|SGD:S000005927}; OrderedLocusNames=YPL006W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-718.
RX PubMed=14970192; DOI=10.1083/jcb.200310046;
RA Malathi K., Higaki K., Tinkelenberg A.H., Balderes D.A.,
RA Almanzar-Paramio D., Wilcox L.J., Erdeniz N., Redican F., Padamsee M.,
RA Liu Y., Khan S., Alcantara F., Carstea E.D., Morris J.A., Sturley S.L.;
RT "Mutagenesis of the putative sterol-sensing domain of yeast Niemann Pick C-
RT related protein reveals a primordial role in subcellular sphingolipid
RT distribution.";
RL J. Cell Biol. 164:547-556(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15522102; DOI=10.1111/j.1600-0854.2004.00241.x;
RA Zhang S., Ren J., Li H., Zhang Q., Armstrong J.S., Munn A.L., Yang H.;
RT "Ncr1p, the yeast ortholog of mammalian Niemann Pick C1 protein, is
RT dispensable for endocytic transport.";
RL Traffic 5:1017-1030(2004).
RN [7]
RP FUNCTION.
RX PubMed=16138904; DOI=10.1111/j.1600-0854.2005.00327.x;
RA Berger A.C., Hanson P.K., Wylie Nichols J., Corbett A.H.;
RT "A yeast model system for functional analysis of the Niemann-Pick type C
RT protein 1 homolog, Ncr1p.";
RL Traffic 6:907-917(2005).
CC -!- FUNCTION: Involved in sphingolipid trafficking. May recycle
CC sphingolipids between cellular membranous compartments.
CC {ECO:0000269|PubMed:14970192, ECO:0000269|PubMed:16138904}.
CC -!- INTERACTION:
CC Q12200; P33302: PDR5; NbExp=2; IntAct=EBI-32032, EBI-13038;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14970192, ECO:0000269|PubMed:15522102}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14970192, ECO:0000269|PubMed:15522102}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the patched family. {ECO:0000305}.
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DR EMBL; U33335; AAB68099.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88380.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95035.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11422.1; -; Genomic_DNA.
DR PIR; S52525; S52525.
DR RefSeq; NP_015319.1; NM_001183820.1.
DR PDB; 6R4L; X-ray; 3.50 A; A=1-1170.
DR PDBsum; 6R4L; -.
DR AlphaFoldDB; Q12200; -.
DR SMR; Q12200; -.
DR BioGRID; 36171; 207.
DR IntAct; Q12200; 7.
DR MINT; Q12200; -.
DR STRING; 4932.YPL006W; -.
DR TCDB; 2.A.6.6.3; the resistance-nodulation-cell division (rnd) superfamily.
DR MaxQB; Q12200; -.
DR PaxDb; Q12200; -.
DR PRIDE; Q12200; -.
DR EnsemblFungi; YPL006W_mRNA; YPL006W; YPL006W.
DR GeneID; 856101; -.
DR KEGG; sce:YPL006W; -.
DR SGD; S000005927; NCR1.
DR VEuPathDB; FungiDB:YPL006W; -.
DR eggNOG; KOG1933; Eukaryota.
DR GeneTree; ENSGT00940000156182; -.
DR HOGENOM; CLU_002359_0_1_1; -.
DR InParanoid; Q12200; -.
DR OMA; CPDNGLA; -.
DR BioCyc; YEAST:G3O-33925-MON; -.
DR Reactome; R-SCE-8963678; Intestinal lipid absorption.
DR Reactome; R-SCE-8964038; LDL clearance.
DR PRO; PR:Q12200; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12200; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0032934; F:sterol binding; IDA:SGD.
DR GO; GO:0006665; P:sphingolipid metabolic process; IMP:SGD.
DR GO; GO:0015918; P:sterol transport; IDA:SGD.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR Pfam; PF16414; NPC1_N; 1.
DR Pfam; PF02460; Patched; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Lipid metabolism;
KW Lipid transport; Membrane; Reference proteome; Signal;
KW Sphingolipid metabolism; Transmembrane; Transmembrane helix; Transport;
KW Vacuole.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1170
FT /note="NPC intracellular sterol transporter 1-related
FT protein 1"
FT /id="PRO_0000268685"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1000..1020
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1054..1074
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1099..1119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1133..1153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 557..717
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..75
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 29..41
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 64..110
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 76..114
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 98..230
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 101..156
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 223..235
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 232..239
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 438..447
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 473..480
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 822..828
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 868..925
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 869..891
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT DISULFID 879..888
FT /evidence="ECO:0000250|UniProtKB:O15118"
FT MUTAGEN 718
FT /note="Y->D: Sphingolipids mislocalization and no growth at
FT 38 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:14970192"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 257..278
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 319..323
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 338..358
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 393..400
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 422..426
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 452..456
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 466..475
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 490..493
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 503..511
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 516..531
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 547..554
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 574..582
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 588..608
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 615..643
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 652..680
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 687..706
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 707..709
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 710..721
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 739..743
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 745..747
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 749..766
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 767..769
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 776..779
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 787..796
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 800..807
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 815..817
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 833..841
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 853..859
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 863..865
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 870..874
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 888..892
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 899..902
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 908..917
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 923..925
FT /evidence="ECO:0007829|PDB:6R4L"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 933..938
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 941..943
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 946..953
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 959..971
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 973..975
FT /evidence="ECO:0007829|PDB:6R4L"
FT STRAND 981..984
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 993..995
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 997..1019
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1023..1046
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1053..1076
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1088..1120
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1124..1129
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1131..1146
FT /evidence="ECO:0007829|PDB:6R4L"
FT HELIX 1148..1157
FT /evidence="ECO:0007829|PDB:6R4L"
SQ SEQUENCE 1170 AA; 132645 MW; F976EBDB36C36C92 CRC64;
MNVLWIIALV GQLMRLVQGT ATCAMYGNCG KKSVFGNELP CPVPRSFEPP VLSDETSKLL
VEVCGEEWKE VRYACCTKDQ VVALRDNLQK AQPLISSCPA CLKNFNNLFC HFTCAADQGR
FVNITKVEKS KEDKDIVAEL DVFMNSSWAS EFYDSCKNIK FSATNGYAMD LIGGGAKNYS
QFLKFLGDAK PMLGGSPFQI NYKYDLANEE KEWQEFNDEV YACDDAQYKC ACSDCQESCP
HLKPLKDGVC KVGPLPCFSL SVLIFYTICA LFAFMWYYLC KRKKNGAMIV DDDIVPESGS
LDESETNVFE SFNNETNFFN GKLANLFTKV GQFSVENPYK ILITTVFSIF VFSFIIFQYA
TLETDPINLW VSKNSEKFKE KEYFDDNFGP FYRTEQIFVV NETGPVLSYE TLHWWFDVEN
FITEELQSSE NIGYQDLCFR PTEDSTCVIE SFTQYFQGAL PNKDSWKREL QECGKFPVNC
LPTFQQPLKT NLLFSDDDIL NAHAFVVTLL LTNHTQSANR WEERLEEYLL DLKVPEGLRI
SFNTEISLEK ELNNNNDIST VAISYLMMFL YATWALRRKD GKTRLLLGIS GLLIVLASIV
CAAGFLTLFG LKSTLIIAEV IPFLILAIGI DNIFLITHEY DRNCEQKPEY SIDQKIISAI
GRMSPSILMS LLCQTGCFLI AAFVTMPAVH NFAIYSTVSV IFNGVLQLTA YVSILSLYEK
RSNYKQITGN EETKESFLKT FYFKMLTQKR LIIIIFSAWF FTSLVFLPEI QFGLDQTLAV
PQDSYLVDYF KDVYSFLNVG PPVYMVVKNL DLTKRQNQQK ICGKFTTCER DSLANVLEQE
RHRSTITEPL ANWLDDYFMF LNPQNDQCCR LKKGTDEVCP PSFPSRRCET CFQQGSWNYN
MSGFPEGKDF MEYLSIWINA PSDPCPLGGR APYSTALVYN ETSVSASVFR TAHHPLRSQK
DFIQAYSDGV RISSSFPELD MFAYSPFYIF FVQYQTLGPL TLKLIGSAII LIFFISSVFL
QNIRSSFLLA LVVTMIIVDI GALMALLGIS LNAVSLVNLI ICVGLGVEFC VHIVRSFTVV
PSETKKDANS RVLYSLNTIG ESVIKGITLT KFIGVCVLAF AQSKIFDVFY FRMWFTLIIV
AALHALLFLP ALLSLFGGES YRDDSIEAED
