Phosphatidylinositol transfer protein PDR16 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P53860 (PDR16_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Endoplasmic reticulum Lipid droplet Membrane Microsome
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phospholipid biosynthetic process Inferred from genetic interaction Ref.6. Source: SGD response to drug Inferred from genetic interaction Ref.6. Source: SGD sterol biosynthetic process Inferred from genetic interaction Ref.6. Source: SGD
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lipid particle Inferred from direct assay Ref.8. Source: SGD plasma membrane Inferred from direct assay PubMed 16622836. Source: SGD
Molecular_function	phosphatidylinositol transporter activity Inferred from direct assay Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 351

351

Phosphatidylinositol transfer protein PDR16

PRO_0000210745

Regions

Domain

135 – 295

161

CRAL-TRIO

Amino acid modifications

Modified residue

346

Phosphoserine Ref.11

Modified residue

348

Phosphoserine Ref.11

Modified residue

349

Phosphoserine Ref.11

Modified residue

350

Phosphothreonine Ref.11

Sequences

Sequence

Length

Mass (Da)

Tools

P53860 [UniParc].

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

FASTA

351

40,714

        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' referencesShow '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. Hani J. Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. 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, 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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-348; SER-349 AND THR-350, MASS SPECTROMETRY.
+	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.

PIR

S63197.

RefSeq

NP_014168.1. NM_001183069.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FMM	X-ray	2.34	A/B	1-351	[»]

ProteinModelPortal

P53860.

SMR

P53860. Positions 77-312.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5449N.

IntAct

P53860. 1 interaction.

MINT

MINT-539790.

STRING

4932.YNL231C.

Proteomic databases

PaxDb

P53860.

PeptideAtlas

P53860.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL231C; YNL231C; YNL231C.

GeneID

855490.

KEGG

sce:YNL231C.

Organism-specific databases

CYGD

YNL231c.

SGD

S000005175. PDR16.

Phylogenomic databases

eggNOG

NOG242743.

GeneTree

ENSGT00390000018675.

HOGENOM

HOG000176881.

OMA

IHPVGTI.

OrthoDB

EOG4VDT78.

Gene expression databases

Genevestigator

P53860.

GermOnline

YNL231C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.525.10. 1 hit.

InterPro

IPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]

Pfam

PF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]

SMART

SM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]

SUPFAM

SSF52087. CRAL_TRIO_C. 1 hit.
SSF46938. Sec14p_like_N. 1 hit.

PROSITE

PS50191. CRAL_TRIO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

979472.

Entry information

Entry name

PDR16_YEAST

Accession

Primary (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 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XIV

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents