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Protein

Inositol phosphorylceramide synthase catalytic subunit AUR1

Gene

AUR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic component of the inositol phosphorylceramide synthase which catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis.3 Publications

Enzyme regulationi

Inhibited by aureobasidin A (AbA), khafrefungin and rustmicin.1 Publication

Kineticsi

  1. KM=555 µM for phosphatidylinositol1 Publication
  2. KM=3.0 µM for C(6)-NBD-ceramide1 Publication
  1. Vmax=824 pmol/min/mg enzyme for phosphatidylinositol1 Publication
  2. Vmax=367 pmol/min/mg enzyme for C(6)-NBD-ceramide1 Publication

GO - Molecular functioni

  • inositol phosphoceramide synthase activity Source: SGD

GO - Biological processi

  • inositolphosphoceramide metabolic process Source: SGD
  • sphingolipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-630.
YEAST:MONOMER3O-630.
SABIO-RKP36107.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol phosphorylceramide synthase catalytic subunit AUR1 (EC:2.-.-.-)
Short name:
IPC synthase catalytic subunit AUR1
Alternative name(s):
Aureobasidin A resistance protein
Phosphatidylinositol:ceramide phosphoinositol transferase
Gene namesi
Name:AUR1
Ordered Locus Names:YKL004W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL004W.
SGDiS000001487. AUR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4141CytoplasmicSequence analysisAdd
BLAST
Transmembranei42 – 6221HelicalSequence analysisAdd
BLAST
Topological domaini63 – 642LumenalSequence analysis
Transmembranei65 – 8521HelicalSequence analysisAdd
BLAST
Topological domaini86 – 872CytoplasmicSequence analysis
Transmembranei88 – 10821HelicalSequence analysisAdd
BLAST
Topological domaini109 – 15547LumenalSequence analysisAdd
BLAST
Transmembranei156 – 17621HelicalSequence analysisAdd
BLAST
Topological domaini177 – 1782CytoplasmicSequence analysis
Transmembranei179 – 19921HelicalSequence analysisAdd
BLAST
Topological domaini200 – 24546LumenalSequence analysisAdd
BLAST
Transmembranei246 – 26621HelicalSequence analysisAdd
BLAST
Topological domaini267 – 2682CytoplasmicSequence analysis
Transmembranei269 – 28921HelicalSequence analysisAdd
BLAST
Topological domaini290 – 2912LumenalSequence analysis
Transmembranei292 – 31221HelicalSequence analysisAdd
BLAST
Topological domaini313 – 40189CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • Golgi apparatus Source: SGD
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • inositol phosphoceramide synthase complex Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi137 – 1371L → F: AbA resistant; when associated with Y-157. 1 Publication
Mutagenesisi157 – 1571H → Y: AbA resistant; when associated with F-137. 1 Publication
Mutagenesisi158 – 1581F → Y in AUR1-1; AbA resistant. 1 Publication
Mutagenesisi294 – 2941H → A: Abolishes catalytic activity. 1 Publication

Chemistry

ChEMBLiCHEMBL1641344.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Inositol phosphorylceramide synthase catalytic subunit AUR1PRO_0000064766Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence analysis
Modified residuei392 – 3921PhosphoserineCombined sources
Modified residuei395 – 3951PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP36107.
PeptideAtlasiP36107.

PTM databases

iPTMnetiP36107.

Interactioni

Subunit structurei

Component of the inositol phosphorylceramide synthase complex composed of at least AUR1 and KEI1.

Binary interactionsi

WithEntry#Exp.IntActNotes
KEI1Q063462EBI-2046036,EBI-38431

Protein-protein interaction databases

BioGridi34129. 172 interactions.
DIPiDIP-7196N.
IntActiP36107. 12 interactions.
MINTiMINT-1356606.

Chemistry

BindingDBiP36107.

Structurei

3D structure databases

ProteinModelPortaliP36107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AUR1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00530000066622.
HOGENOMiHOG000196614.
InParanoidiP36107.
OMAiMYTTAFS.
OrthoDBiEOG7V76FR.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR026841. Aur1/Ipt1.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF14378. PAP2_3. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

P36107-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANPFSRWFL SERPPNCHVA DLETSLDPHQ TLLKVQKYKP ALSDWVHYIF
60 70 80 90 100
LGSIMLFVFI TNPAPWIFKI LFYCFLGTLF IIPATSQFFF NALPILTWVA
110 120 130 140 150
LYFTSSYFPD DRRPPITVKV LPAVETILYG DNLSDILATS TNSFLDILAW
160 170 180 190 200
LPYGLFHFGA PFVVAAILFV FGPPTVLQGY AFAFGYMNLF GVIMQNVFPA
210 220 230 240 250
APPWYKILYG LQSANYDMHG SPGGLARIDK LLGINMYTTA FSNSSVIFGA
260 270 280 290 300
FPSLHSGCAT MEALFFCYCF PKLKPLFIAY VCWLWWSTMY LTHHYFVDLM
310 320 330 340 350
AGSVLSYVIF QYTKYTHLPI VDTSLFCRWS YTSIEKYDIS KSDPLAADSN
360 370 380 390 400
DIESVPLSNL ELDFDLNMTD EPSVSPSLFD GSTSVSRSSA TSITSLGVKR

A
Length:401
Mass (Da):45,193
Last modified:June 1, 1994 - v1
Checksum:i997F92318DF656A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49090 Genomic DNA. Translation: AAB06940.1.
Z28004 Genomic DNA. Translation: CAA81836.1.
BK006944 Genomic DNA. Translation: DAA09153.1.
PIRiS37815.
RefSeqiNP_012922.1. NM_001179570.1.

Genome annotation databases

EnsemblFungiiYKL004W; YKL004W; YKL004W.
GeneIDi853866.
KEGGisce:YKL004W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49090 Genomic DNA. Translation: AAB06940.1.
Z28004 Genomic DNA. Translation: CAA81836.1.
BK006944 Genomic DNA. Translation: DAA09153.1.
PIRiS37815.
RefSeqiNP_012922.1. NM_001179570.1.

3D structure databases

ProteinModelPortaliP36107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34129. 172 interactions.
DIPiDIP-7196N.
IntActiP36107. 12 interactions.
MINTiMINT-1356606.

Chemistry

BindingDBiP36107.
ChEMBLiCHEMBL1641344.

PTM databases

iPTMnetiP36107.

Proteomic databases

MaxQBiP36107.
PeptideAtlasiP36107.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL004W; YKL004W; YKL004W.
GeneIDi853866.
KEGGisce:YKL004W.

Organism-specific databases

EuPathDBiFungiDB:YKL004W.
SGDiS000001487. AUR1.

Phylogenomic databases

GeneTreeiENSGT00530000066622.
HOGENOMiHOG000196614.
InParanoidiP36107.
OMAiMYTTAFS.
OrthoDBiEOG7V76FR.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-630.
YEAST:MONOMER3O-630.
SABIO-RKP36107.

Miscellaneous databases

NextBioi975127.
PROiP36107.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
InterProiIPR026841. Aur1/Ipt1.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF14378. PAP2_3. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AUR1, a novel gene conferring aureobasidin resistance on Saccharomyces cerevisiae: a study of defective morphologies in Aur1p-depleted cells."
    Hashida-Okado T., Ogawa A., Endo M., Yasumoto R., Takesako K., Kato I.
    Mol. Gen. Genet. 251:236-244(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF PHE-158.
    Strain: AR9-4A.
  2. "The AUR1 gene in Saccharomyces cerevisiae encodes dominant resistance to the antifungal agent aureobasidin A (LY295337)."
    Heidler S.A., Radding J.A.
    Antimicrob. Agents Chemother. 39:2765-2769(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LEU-137 AND HIS-157.
  3. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Sphingolipid synthesis as a target for antifungal drugs. Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene."
    Nagiec M.M., Nagiec E.E., Baltisberger J.A., Wells G.B., Lester R.L., Dickson R.C.
    J. Biol. Chem. 272:9809-9817(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae."
    Levine T.P., Wiggins C.A., Munro S.
    Mol. Biol. Cell 11:2267-2281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF HIS-294.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Inhibition of inositol phosphorylceramide synthase by the cyclic peptide aureobasidin A."
    Aeed P.A., Young C.L., Nagiec M.M., Elhammer A.P.
    Antimicrob. Agents Chemother. 53:496-504(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  12. "Kei1: a novel subunit of inositolphosphorylceramide synthase, essential for its enzyme activity and Golgi localization."
    Sato K., Noda Y., Yoda K.
    Mol. Biol. Cell 20:4444-4457(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KEI1.
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAUR1_YEAST
AccessioniPrimary (citable) accession number: P36107
Secondary accession number(s): D6VXT3, Q92324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 11, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4170 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.