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Reviewed, UniProtKB/Swiss-Prot O13332 (AUR1_CANAL)

Last modified November 3, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inositol phosphorylceramide synthase
      Short name=IPC synthase
    EC=2.-.-.-
Alternative name(s):
    Phosphatidylinositol:ceramide phosphoinositol transferase
    Aureobasidin A resistance protein homolog
Gene names
Name: AUR1
ORF Names: CaO19.1945, CaO19.9500
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the addition of a phosphorylinositol group onto ceramide to form inositol phosphorylceramide, an essential step in sphingolipid biosynthesis. Ref.3

Enzyme regulation

Inhibited by aureobasidin A (AbA), khafrefungin and rustmicin. Ref.3

Subcellular location

Golgi apparatus › Golgi stack membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the AUR1 family.

Biophysicochemical properties

Kinetic parameters:

KM=130 µM for phosphatidylinositol

KM=3.3 µM for C(6)-NBD-ceramide

Vmax=1864 pmol/min/mg enzyme for phosphatidylinositol

Vmax=884 pmol/min/mg enzyme for C(6)-NBD-ceramide

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Ontologies

Keywords
   Biological processLipid metabolism
Sphingolipid metabolism
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
   Molecular functionTransferase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processsphingolipid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functiontransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Inositol phosphorylceramide synthase
PRO_0000064764

Regions

Topological domain1 – 5454Cytoplasmic By similarity
Transmembrane55 – 7521 Potential
Topological domain76 – 772Lumenal By similarity
Transmembrane78 – 9821 Potential
Topological domain99 – 1002Cytoplasmic By similarity
Transmembrane101 – 12121 Potential
Topological domain122 – 16847Lumenal By similarity
Transmembrane169 – 18921 Potential
Topological domain190 – 1912Cytoplasmic By similarity
Transmembrane192 – 21221 Potential
Topological domain213 – 25846Lumenal By similarity
Transmembrane259 – 27921 Potential
Topological domain280 – 2812Cytoplasmic By similarity
Transmembrane282 – 30221 Potential
Topological domain303 – 3042Lumenal By similarity
Transmembrane305 – 32521 Potential
Topological domain326 – 471146Cytoplasmic By similarity
Compositional bias428 – 4347Poly-Glu

Amino acid modifications

Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3651I → V in AAB67233. Ref.1
Sequence conflict3881S → Q in AAB67233. Ref.1
Sequence conflict4241P → S in AAB67233. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
O13332-1 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 0CFE68ABF7125A7A

FASTA47153,458
        10         20         30         40         50         60 
MASSILRSKI IQKPYQLFHY YFLSEKAPGS TVSDLNFDTN IQTSLRKLKH HHWTVGEIFH 

        70         80         90        100        110        120 
YGFLVSILFF VFVVFPASFF IKLPIILAFA TCFLIPLTSQ FFLPALPVFT WLALYFTCAK 

       130        140        150        160        170        180 
IPQEWKPAIT VKVLPAMETI LYGDNLSNVL ATITTGVLDI LAWLPYGIIH FSFPFVLAAI 

       190        200        210        220        230        240 
IFLFGPPTAL RSFGFAFGYM NLLGVLIQMA FPAAPPWYKN LHGLEPANYS MHGSPGGLGR 

       250        260        270        280        290        300 
IDKLLGVDMY TTGFSNSSII FGAFPSLHSG CCIMEVLFLC WLFPRFKFVW VTYASWLWWS 

       310        320        330        340        350        360 
TMYLTHHYFV DLIGGAMLSL TVFEFTKYKY LPKNKEGLFC RWSYTEIEKI DIQEIDPLSY 

       370        380        390        400        410        420 
NYIPINSNDN ESRLYTRVYQ ESQVSPPSRA ETPEAFEMSN FSRSRQSSKT QVPLSNLTNN 

       430        440        450        460        470 
DQVPGINEED EEEEGDEISS STPSVFEDEP QGSTYAASSA TSVDDLDSKR N

« Hide

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References

« Hide 'large scale' references
[1]"Cloning of AUR1 homolog on Candida albicans."
Kondo A., Hashida-Okado T., Takesako K., Kato I.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: TIMM 0136.
[2]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.
[3]"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: 19047657] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.

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Cross-references

Sequence databases

AF013799 Genomic DNA. Translation: AAB67233.1.
AACQ01000082 Genomic DNA. Translation: EAK96634.1.
AACQ01000081 Genomic DNA. Translation: EAK96693.1.
RefSeqXP_715651.1.
XP_715708.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3642617.
3642715.
KEGGcal:CaO19.1945.
cal:CaO19.9500.

Organism-specific databases

CGDCAL0002586. AUR1.

Family and domain databases

InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAUR1_CANAL
AccessionPrimary (citable) accession number: O13332
Secondary accession number(s): Q5A1Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 28, 2009
Last modified: November 3, 2009
This is version 34 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents