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Protein

Phosphatidylinositol transfer protein PDR16

Gene

PDR16

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

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.2 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. phosphatidylinositol transporter activity Source: SGD

GO - Biological processi

  1. negative regulation of sexual sporulation resulting in formation of a cellular spore Source: SGD
  2. phospholipid biosynthetic process Source: SGD
  3. phospholipid transport Source: SGD
  4. response to drug Source: SGD
  5. sterol biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33231-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol transfer protein PDR16
Short name:
PITP
Alternative name(s):
Pleiotropic drug resistance protein 16
SEC14 homolog 3
Gene namesi
Name:PDR16
Synonyms:SFH3
Ordered Locus Names:YNL231C
ORF Names:N1158
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL231c.
SGDiS000005175. PDR16.

Subcellular locationi

GO - Cellular componenti

  1. cell periphery Source: SGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. lipid particle Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351Phosphatidylinositol transfer protein PDR16PRO_0000210745Add
BLAST

Proteomic databases

MaxQBiP53860.
PaxDbiP53860.
PeptideAtlasiP53860.

Expressioni

Gene expression databases

GenevestigatoriP53860.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-29195,EBI-29195

Protein-protein interaction databases

BioGridi35607. 29 interactions.
DIPiDIP-5449N.
IntActiP53860. 2 interactions.
MINTiMINT-539790.
STRINGi4932.YNL231C.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 213Combined sources
Helixi42 – 5615Combined sources
Beta strandi61 – 644Combined sources
Beta strandi74 – 763Combined sources
Helixi79 – 846Combined sources
Helixi87 – 9610Combined sources
Turni97 – 993Combined sources
Helixi101 – 11818Combined sources
Helixi125 – 1273Combined sources
Helixi133 – 1364Combined sources
Helixi137 – 1404Combined sources
Beta strandi144 – 1507Combined sources
Beta strandi156 – 1605Combined sources
Helixi162 – 1643Combined sources
Helixi171 – 18616Combined sources
Beta strandi195 – 2006Combined sources
Helixi221 – 23111Combined sources
Beta strandi237 – 2448Combined sources
Helixi247 – 25610Combined sources
Helixi257 – 2593Combined sources
Helixi262 – 2654Combined sources
Beta strandi268 – 2725Combined sources
Helixi274 – 2763Combined sources
Helixi280 – 2823Combined sources
Helixi285 – 2873Combined sources
Beta strandi289 – 2935Combined sources
Helixi297 – 32125Combined sources
Helixi330 – 3334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FMMX-ray2.34A/B1-351[»]
4J7PX-ray2.00A/B2-351[»]
4J7QX-ray1.55A/B15-345[»]
4M8ZX-ray1.93A/B1-351[»]
ProteinModelPortaliP53860.
SMRiP53860. Positions 16-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 295161CRAL-TRIOPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CRAL-TRIO domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG242743.
GeneTreeiENSGT00390000018675.
HOGENOMiHOG000176881.
InParanoidiP53860.
OMAiVWMLERT.
OrthoDBiEOG70PC7T.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53860-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRFSKKKE APEDPKNLIN IDKPIKELPA SIAIPKEKPL TGEQQKMYDE
60 70 80 90 100
VLKHFSNPDL KVYTSEKNKS EDDLKPLEEE EKAWLTRECF LRYLRATKWV
110 120 130 140 150
LKDCIDRITM TLAWRREFGI SHLGEEHGDK ITADLVAVEN ESGKQVILGY
160 170 180 190 200
ENDARPILYL KPGRQNTKTS HRQVQHLVFM LERVIDFMPA GQDSLALLID
210 220 230 240 250
FKDYPDVPKV PGNSKIPPIG VGKEVLHILQ THYPERLGKA LLTNIPWLAW
260 270 280 290 300
TFLKLIHPFI DPLTREKLVF DEPFVKYVPK NELDSLYGGD LKFKYNHDVY
310 320 330 340 350
WPALVETARE KRDHYFKRFQ SFGGIVGLSE VDLRGTHEKL LYPVKSESST

V
Length:351
Mass (Da):40,714
Last modified:October 1, 1996 - v1
Checksum:i24C5B3262016F037
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69381 Genomic DNA. Translation: CAA93367.1.
Z71507 Genomic DNA. Translation: CAA96136.1.
AY558020 Genomic DNA. Translation: AAS56346.1.
BK006947 Genomic DNA. Translation: DAA10327.1.
PIRiS63197.
RefSeqiNP_014168.1. NM_001183069.1.

Genome annotation databases

EnsemblFungiiYNL231C; YNL231C; YNL231C.
GeneIDi855490.
KEGGisce:YNL231C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69381 Genomic DNA. Translation: CAA93367.1.
Z71507 Genomic DNA. Translation: CAA96136.1.
AY558020 Genomic DNA. Translation: AAS56346.1.
BK006947 Genomic DNA. Translation: DAA10327.1.
PIRiS63197.
RefSeqiNP_014168.1. NM_001183069.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4FMMX-ray2.34A/B1-351[»]
4J7PX-ray2.00A/B2-351[»]
4J7QX-ray1.55A/B15-345[»]
4M8ZX-ray1.93A/B1-351[»]
ProteinModelPortaliP53860.
SMRiP53860. Positions 16-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35607. 29 interactions.
DIPiDIP-5449N.
IntActiP53860. 2 interactions.
MINTiMINT-539790.
STRINGi4932.YNL231C.

Proteomic databases

MaxQBiP53860.
PaxDbiP53860.
PeptideAtlasiP53860.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL231C; YNL231C; YNL231C.
GeneIDi855490.
KEGGisce:YNL231C.

Organism-specific databases

CYGDiYNL231c.
SGDiS000005175. PDR16.

Phylogenomic databases

eggNOGiNOG242743.
GeneTreeiENSGT00390000018675.
HOGENOMiHOG000176881.
InParanoidiP53860.
OMAiVWMLERT.
OrthoDBiEOG70PC7T.

Enzyme and pathway databases

BioCyciYEAST:G3O-33231-MONOMER.

Miscellaneous databases

NextBioi979472.

Gene expression databases

GenevestigatoriP53860.

Family and domain databases

Gene3Di3.40.525.10. 1 hit.
InterProiIPR001251. CRAL-TRIO_dom.
IPR011074. CRAL/TRIO_N_dom.
[Graphical view]
PfamiPF00650. CRAL_TRIO. 1 hit.
PF03765. CRAL_TRIO_N. 1 hit.
[Graphical view]
SMARTiSM01100. CRAL_TRIO_N. 1 hit.
SM00516. SEC14. 1 hit.
[Graphical view]
SUPFAMiSSF46938. SSF46938. 1 hit.
SSF52087. SSF52087. 1 hit.
PROSITEiPS50191. CRAL_TRIO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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.
    , 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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Bienvenut W.V., Peters C.
    Submitted (MAY-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(1998) [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(1999) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. 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(2006) [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(2007) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDR16_YEAST
AccessioniPrimary (citable) accession number: P53860
Secondary accession number(s): D6W0W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 4, 2015
This is version 120 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 15361 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

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 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.