AUR1_YEAST
ID AUR1_YEAST Reviewed; 401 AA.
AC P36107; D6VXT3; Q92324;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Inositol phosphorylceramide synthase catalytic subunit AUR1 {ECO:0000303|PubMed:10888667};
DE Short=IPC synthase catalytic subunit AUR1 {ECO:0000303|PubMed:10888667};
DE EC=2.7.1.227 {ECO:0000269|PubMed:10888667};
DE AltName: Full=Aureobasidin A resistance protein {ECO:0000303|PubMed:8668135};
DE AltName: Full=Phosphatidylinositol:ceramide phosphoinositol transferase {ECO:0000303|PubMed:10888667};
GN Name=AUR1 {ECO:0000303|PubMed:8668135}; OrderedLocusNames=YKL004W;
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 [GENOMIC DNA], AND MUTAGENESIS OF PHE-158.
RC STRAIN=AR9-4A;
RX PubMed=8668135; DOI=10.1007/bf02172923;
RA Hashida-Okado T., Ogawa A., Endo M., Yasumoto R., Takesako K., Kato I.;
RT "AUR1, a novel gene conferring aureobasidin resistance on Saccharomyces
RT cerevisiae: a study of defective morphologies in Aur1p-depleted cells.";
RL Mol. Gen. Genet. 251:236-244(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LEU-137 AND HIS-157.
RX PubMed=8593016; DOI=10.1128/aac.39.12.2765;
RA Heidler S.A., Radding J.A.;
RT "The AUR1 gene in Saccharomyces cerevisiae encodes dominant resistance to
RT the antifungal agent aureobasidin A (LY295337).";
RL Antimicrob. Agents Chemother. 39:2765-2769(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=9092515; DOI=10.1074/jbc.272.15.9809;
RA Nagiec M.M., Nagiec E.E., Baltisberger J.A., Wells G.B., Lester R.L.,
RA Dickson R.C.;
RT "Sphingolipid synthesis as a target for antifungal drugs. Complementation
RT of the inositol phosphorylceramide synthase defect in a mutant strain of
RT Saccharomyces cerevisiae by the AUR1 gene.";
RL J. Biol. Chem. 272:9809-9817(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP MUTAGENESIS OF HIS-294.
RX PubMed=10888667; DOI=10.1091/mbc.11.7.2267;
RA Levine T.P., Wiggins C.A., Munro S.;
RT "Inositol phosphorylceramide synthase is located in the Golgi apparatus of
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 11:2267-2281(2000).
RN [7]
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 [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=19047657; DOI=10.1128/aac.00633-08;
RA Aeed P.A., Young C.L., Nagiec M.M., Elhammer A.P.;
RT "Inhibition of inositol phosphorylceramide synthase by the cyclic peptide
RT aureobasidin A.";
RL Antimicrob. Agents Chemother. 53:496-504(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KEI1.
RX PubMed=19726565; DOI=10.1091/mbc.e09-03-0235;
RA Sato K., Noda Y., Yoda K.;
RT "Kei1: a novel subunit of inositolphosphorylceramide synthase, essential
RT for its enzyme activity and Golgi localization.";
RL Mol. Biol. Cell 20:4444-4457(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalytic component of the inositol phosphorylceramide
CC synthase which catalyzes the addition of a phosphorylinositol group
CC onto ceramide to form inositol phosphorylceramide, an essential step in
CC sphingolipid biosynthesis. {ECO:0000269|PubMed:10888667,
CC ECO:0000269|PubMed:19047657, ECO:0000269|PubMed:19726565,
CC ECO:0000269|PubMed:9092515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + an N-
CC (2R-hydroxy-very-long-chain fatty acyl)-(R)-4-hydroxysphingoid base =
CC a 1,2-diacyl-sn-glycerol + a 1D-myo-inositol-1-phospho-N-[(R)-2-
CC hydroxy-very-long-chain fatty acyl]-(R)-4-hydroxysphingoid base;
CC Xref=Rhea:RHEA:64536, ChEBI:CHEBI:17815, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:155886, ChEBI:CHEBI:155926; EC=2.7.1.227;
CC Evidence={ECO:0000269|PubMed:10888667};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64537;
CC Evidence={ECO:0000269|PubMed:10888667};
CC -!- ACTIVITY REGULATION: Inhibited by aureobasidin A (AbA), khafrefungin
CC and rustmicin. {ECO:0000269|PubMed:19047657}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=555 uM for phosphatidylinositol {ECO:0000269|PubMed:19047657};
CC KM=3.0 uM for C(6)-NBD-ceramide {ECO:0000269|PubMed:19047657};
CC Vmax=824 pmol/min/mg enzyme for phosphatidylinositol
CC {ECO:0000269|PubMed:19047657};
CC Vmax=367 pmol/min/mg enzyme for C(6)-NBD-ceramide
CC {ECO:0000269|PubMed:19047657};
CC -!- SUBUNIT: Component of the inositol phosphorylceramide synthase complex
CC composed of at least AUR1 and KEI1.
CC -!- INTERACTION:
CC P36107; Q06346: KEI1; NbExp=2; IntAct=EBI-2046036, EBI-38431;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:10888667, ECO:0000269|PubMed:19726565}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10888667,
CC ECO:0000269|PubMed:19726565}.
CC -!- MISCELLANEOUS: Present with 4170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AUR1 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; U49090; AAB06940.1; -; Genomic_DNA.
DR EMBL; Z28004; CAA81836.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09153.1; -; Genomic_DNA.
DR PIR; S37815; S37815.
DR RefSeq; NP_012922.1; NM_001179570.1.
DR AlphaFoldDB; P36107; -.
DR BioGRID; 34129; 388.
DR ComplexPortal; CPX-2894; Inositol phosphorylceramide synthase complex.
DR DIP; DIP-7196N; -.
DR IntAct; P36107; 12.
DR MINT; P36107; -.
DR STRING; 4932.YKL004W; -.
DR BindingDB; P36107; -.
DR ChEMBL; CHEMBL1641344; -.
DR SwissLipids; SLP:000001845; -.
DR iPTMnet; P36107; -.
DR MaxQB; P36107; -.
DR PaxDb; P36107; -.
DR PRIDE; P36107; -.
DR DNASU; 853866; -.
DR EnsemblFungi; YKL004W_mRNA; YKL004W; YKL004W.
DR GeneID; 853866; -.
DR KEGG; sce:YKL004W; -.
DR SGD; S000001487; AUR1.
DR VEuPathDB; FungiDB:YKL004W; -.
DR eggNOG; ENOG502QPQM; Eukaryota.
DR GeneTree; ENSGT00940000176762; -.
DR HOGENOM; CLU_030747_2_0_1; -.
DR InParanoid; P36107; -.
DR OMA; MSHCFPQ; -.
DR BioCyc; MetaCyc:MON3O-630; -.
DR BioCyc; YEAST:MON3O-630; -.
DR BRENDA; 2.7.1.227; 984.
DR SABIO-RK; P36107; -.
DR PRO; PR:P36107; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36107; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070916; C:inositol phosphoceramide synthase complex; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045140; F:inositol phosphoceramide synthase activity; IDA:SGD.
DR GO; GO:0006673; P:inositol phosphoceramide metabolic process; IDA:SGD.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IMP:SGD.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..401
FT /note="Inositol phosphorylceramide synthase catalytic
FT subunit AUR1"
FT /id="PRO_0000064766"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..64
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..155
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..245
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..291
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT REGION 374..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 137
FT /note="L->F: AbA resistant; when associated with Y-157."
FT /evidence="ECO:0000269|PubMed:8593016"
FT MUTAGEN 157
FT /note="H->Y: AbA resistant; when associated with F-137."
FT /evidence="ECO:0000269|PubMed:8593016"
FT MUTAGEN 158
FT /note="F->Y: In AUR1-1; AbA resistant."
FT /evidence="ECO:0000269|PubMed:8668135"
FT MUTAGEN 294
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:10888667"
SQ SEQUENCE 401 AA; 45193 MW; 997F92318DF656A7 CRC64;
MANPFSRWFL SERPPNCHVA DLETSLDPHQ TLLKVQKYKP ALSDWVHYIF LGSIMLFVFI
TNPAPWIFKI LFYCFLGTLF IIPATSQFFF NALPILTWVA LYFTSSYFPD DRRPPITVKV
LPAVETILYG DNLSDILATS TNSFLDILAW LPYGLFHFGA PFVVAAILFV FGPPTVLQGY
AFAFGYMNLF GVIMQNVFPA APPWYKILYG LQSANYDMHG SPGGLARIDK LLGINMYTTA
FSNSSVIFGA FPSLHSGCAT MEALFFCYCF PKLKPLFIAY VCWLWWSTMY LTHHYFVDLM
AGSVLSYVIF QYTKYTHLPI VDTSLFCRWS YTSIEKYDIS KSDPLAADSN DIESVPLSNL
ELDFDLNMTD EPSVSPSLFD GSTSVSRSSA TSITSLGVKR A
