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P53860 (PDR16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol transfer protein PDR16

Short name=PITP
Alternative name(s):
Pleiotropic drug resistance protein 16
SEC14 homolog 3
Gene names
Name:PDR16
Synonyms:SFH3
Ordered Locus Names:YNL231C
ORF Names:N1158
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has phosphatidylinositol transfer activity. Involved in the regulation of the phospholipid composition of plasma- and endomembranes. Altering plasma membrane composition may provide a possible mechanism for multidrug resistance. Involved in the regulation of sterol biosynthesis. Contributes to efficient phospholipase D1 activation in the regulation of phospholipid turnover. Ref.6 Ref.7

Subcellular location

Lipid droplet. Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein Potential Ref.8 Ref.9.

Miscellaneous

Present with 15361 molecules/cell in log phase SD medium.

Sequence similarities

Contains 1 CRAL-TRIO domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-29195,EBI-29195

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351Phosphatidylinositol transfer protein PDR16
PRO_0000210745

Regions

Domain135 – 295161CRAL-TRIO

Secondary structure

..................................................... 351
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P53860 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 24C5B3262016F037

FASTA35140,714
        10         20         30         40         50         60 
MFKRFSKKKE APEDPKNLIN IDKPIKELPA SIAIPKEKPL TGEQQKMYDE VLKHFSNPDL 

        70         80         90        100        110        120 
KVYTSEKNKS EDDLKPLEEE EKAWLTRECF LRYLRATKWV LKDCIDRITM TLAWRREFGI 

       130        140        150        160        170        180 
SHLGEEHGDK ITADLVAVEN ESGKQVILGY ENDARPILYL KPGRQNTKTS HRQVQHLVFM 

       190        200        210        220        230        240 
LERVIDFMPA GQDSLALLID FKDYPDVPKV PGNSKIPPIG VGKEVLHILQ THYPERLGKA 

       250        260        270        280        290        300 
LLTNIPWLAW TFLKLIHPFI DPLTREKLVF DEPFVKYVPK NELDSLYGGD LKFKYNHDVY 

       310        320        330        340        350 
WPALVETARE KRDHYFKRFQ SFGGIVGLSE VDLRGTHEKL LYPVKSESST V 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain."
Pandolfo D., de Antoni A., Lanfranchi G., Valle G.
Yeast 12:1071-1076(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Bienvenut W.V., Peters C.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 240-292 AND 319-334, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"PDR16 and PDR17, two homologous genes of Saccharomyces cerevisiae, affect lipid biosynthesis and resistance to multiple drugs."
van den Hazel H.B., Pichler H., do Valle Matta M.A., Leitner E., Goffeau A., Daum G.
J. Biol. Chem. 274:1934-1941(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Identification of a novel family of nonclassic yeast phosphatidylinositol transfer proteins whose function modulates phospholipase D activity and Sec14p-independent cell growth."
Li X., Routt S.M., Xie Z., Cui X., Fang M., Kearns M.A., Bard M., Kirsch D.R., Bankaitis V.A.
Mol. Biol. Cell 11:1989-2005(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Subcellular localization of yeast Sec14 homologues and their involvement in regulation of phospholipid turnover."
Schnabl M., Oskolkova O.V., Holic R., Brezna B., Pichler H., Zagorsek M., Kohlwein S.D., Paltauf F., Daum G., Griac P.
Eur. J. Biochem. 270:3133-3145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[12]"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].
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z69381 Genomic DNA. Translation: CAA93367.1.
Z71507 Genomic DNA. Translation: CAA96136.1.
AY558020 Genomic DNA. Translation: AAS56346.1.
BK006947 Genomic DNA. Translation: DAA10327.1.
PIRS63197.
RefSeqNP_014168.1. NM_001183069.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4FMMX-ray2.34A/B1-351[»]
4J7PX-ray2.00A/B2-351[»]
4J7QX-ray1.55A/B15-345[»]
ProteinModelPortalP53860.
SMRP53860. Positions 16-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35607. 28 interactions.
DIPDIP-5449N.
IntActP53860. 2 interactions.
MINTMINT-539790.
STRING4932.YNL231C.

Proteomic databases

MaxQBP53860.
PaxDbP53860.
PeptideAtlasP53860.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL231C; YNL231C; YNL231C.
GeneID855490.
KEGGsce:YNL231C.

Organism-specific databases

CYGDYNL231c.
SGDS000005175. PDR16.

Phylogenomic databases

eggNOGNOG242743.
GeneTreeENSGT00390000018675.
HOGENOMHOG000176881.
OMANEACLVR.
OrthoDBEOG70PC7T.

Enzyme and pathway databases

BioCycYEAST:G3O-33231-MONOMER.

Gene expression databases

GenevestigatorP53860.

Family and domain databases

Gene3D3.40.525.10. 1 hit.
InterProIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
SMARTSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979472.

Entry information

Entry namePDR16_YEAST
AccessionPrimary (citable) accession number: P53860
Secondary accession number(s): D6W0W1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references