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Protein

Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1

Gene

pdf1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential protein. Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during vacuolar degradation. Required for efficient N-glycosylation. Necessary for maintaining optimal levels of dolichol-linked oligosaccharides.By similarity1 Publication

Catalytic activityi

Palmitoyl-[protein] + H2O = palmitate + [protein].
Dolichyl diphosphate + H2O = dolichyl phosphate + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei125By similarity1
Active sitei245By similarity1
Active sitei298By similarity1
Sitei373Crucial for post-translational processingBy similarity1

GO - Molecular functioni

GO - Biological processi

  • lipid biosynthetic process Source: GO_Central
  • protein N-linked glycosylation Source: GO_Central
  • sphingolipid biosynthetic process Source: PomBase
  • vacuolar acidification Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.2.22. 5613.
ReactomeiR-SPO-75876. Synthesis of very long-chain fatty acyl-CoAs.

Protein family/group databases

ESTHERischpo-SPBC530.12C. Palmitoyl-protein_thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
Cleaved into the following 2 chains:
Palmitoyl-protein thioesterase1 PublicationBy similarity (EC:3.1.2.22)
Short name:
PPTBy similarity
Alternative name(s):
Palmitoyl-protein hydrolaseBy similarity
DolichyldiphosphataseBy similarity (EC:3.6.1.43)
Alternative name(s):
Dolichyl pyrophosphate phosphatase1 PublicationBy similarity
Gene namesi
Name:pdf1
Synonyms:yhc1Imported
ORF Names:SPBC530.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC530.12c.
PomBaseiSPBC530.12c. pdf1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 405LumenalSequence analysisAdd BLAST381
Transmembranei406 – 426HelicalSequence analysisAdd BLAST21
Topological domaini427 – 428CytoplasmicSequence analysis2
Transmembranei429 – 449HelicalSequence analysisAdd BLAST21
Topological domaini450 – 488LumenalSequence analysisAdd BLAST39
Transmembranei489 – 511HelicalSequence analysisAdd BLAST23
Topological domaini512 – 519CytoplasmicSequence analysis8
Transmembranei520 – 540HelicalSequence analysisAdd BLAST21
Topological domaini541 – 552LumenalSequence analysisAdd BLAST12
Transmembranei553 – 573HelicalSequence analysisAdd BLAST21
Topological domaini574 – 622CytoplasmicSequence analysisAdd BLAST49

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Vacuole

Pathology & Biotechi

Disruption phenotypei

Cells show lethality and the dolichyldiphosphatase domain alone can rescue the lethal phenotype, but the growth rate of these cells is slower than in wild-type cells. Cells containing wild-type palmitoyl-protein thioesterase (PPT) and inactivated dolichyldiphosphatase reverse the growth retardation phenotype. Cells containing no functional copy of palmitoyl-protein thioesterase are viable, but abnormally sensitive to sodium orthovanadate and elevated external pH. These sensitivities are reversed when the cells are transformed with plasmid containing wild-type PPT and an inactivating mutation in the dolichyldiphosphatase domain.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125S → A: Sensitive to vanadate and elevation of external pH. 1 Publication1
Mutagenesisi245D → A: Sensitive to vanadate and elevation of external pH. 1 Publication1
Mutagenesisi322 – 622Missing : Lethal. 1 PublicationAdd BLAST301
Mutagenesisi363R → A: No prevention of cleavage of the linker domain, but increases the ratio of the unprocessed from the processed form. 1 Publication1
Mutagenesisi373R → A: Abolished cleavage of the linker domain. 1 Publication1
Mutagenesisi497H → A: Lethal. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000349154? – 622Dolichyldiphosphatase
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000034915225 – 622Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1Add BLAST598
ChainiPRO_000034915325 – ?Palmitoyl-protein thioesterase

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi106 ↔ 138By similarity
Glycosylationi223N-linked (GlcNAc...)Sequence analysis1
Glycosylationi260N-linked (GlcNAc...)Sequence analysis1
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Proteolytically cleaved, possibly by krp1.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO59747.
PRIDEiO59747.

Interactioni

Protein-protein interaction databases

MINTiMINT-4675865.

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the palmitoyl-protein thioesterase family.Sequence analysis
In the C-terminal section; belongs to the dolichyldiphosphatase family.Sequence analysis

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

InParanoidiO59747.
KOiK01074.
OrthoDBiEOG092C2RUC.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
IPR002472. Palm_thioest.
[Graphical view]
PfamiPF02089. Palm_thioest. 1 hit.
PF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
SSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O59747-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSCSSFLIF FLFSWVLLPM KSFAIPIISL DKVRLAINDG ASEQLPVVIW
60 70 80 90 100
HGLGDTPTSF TLTEVSQRVQ KLTKGAVYAI RVGDNEFEDI KAGYLGKLED
110 120 130 140 150
QLDEVCDLIG NEDSLSNGFY ALGLSQGGLF LRALAQTCDA AKIRSLITLG
160 170 180 190 200
SPHSGINTIP GCSPTNLICK AVVHSILGLG IWHSWIQNHV VQAQYYRTEK
210 220 230 240 250
QYDKYLENNK FLTHLNNEVL HDNYTRNIEK LKELDNLVAV SFERDDIVEP
260 270 280 290 300
PYSTGFGWIN ETTGENIEME DFVLYESLGL KDLVNQGKLE TISFPGRHLQ
310 320 330 340 350
MRWGDFDALV LKYFKDEKEE KTELEESTRP SNFLSTYFVS PLVSAIDGTV
360 370 380 390 400
DYLHGKSLFP EKRNFKELTM RKRSIVTPED SEEVYPYISE FVAASNVSEE
410 420 430 440 450
KGPKSFANLA FITIFSHFFY HIDDMWRSTL GLFSLIPQII GIIYLTVMFT
460 470 480 490 500
GRELDTFMQF GGQVVNEFIN YVVKVSLKYP RPADIEYGVG YGMPSSHSQF
510 520 530 540 550
MGFFSAYMIA WDYKYRRSQC FSMLSFAKYA IYLTLSTFVC SSRYLLDFHY
560 570 580 590 600
LTQVVYGYMI GFGVGLFWVY LVGKLRSLGV TKWLLSLPPL QFFYIKDTIP
610 620
HSKDNHKRQW LESKQFKNQK SN
Length:622
Mass (Da):71,196
Last modified:October 3, 2012 - v2
Checksum:i48FFF42EFCAD1962
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19178.2.
PIRiT40528.
RefSeqiNP_595325.2. NM_001021232.2.

Genome annotation databases

EnsemblFungiiSPBC530.12c.1; SPBC530.12c.1:pep; SPBC530.12c.
GeneIDi2540904.
KEGGispo:SPBC530.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19178.2.
PIRiT40528.
RefSeqiNP_595325.2. NM_001021232.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4675865.

Protein family/group databases

ESTHERischpo-SPBC530.12C. Palmitoyl-protein_thioesterase.

Proteomic databases

MaxQBiO59747.
PRIDEiO59747.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC530.12c.1; SPBC530.12c.1:pep; SPBC530.12c.
GeneIDi2540904.
KEGGispo:SPBC530.12c.

Organism-specific databases

EuPathDBiFungiDB:SPBC530.12c.
PomBaseiSPBC530.12c. pdf1.

Phylogenomic databases

InParanoidiO59747.
KOiK01074.
OrthoDBiEOG092C2RUC.

Enzyme and pathway databases

BRENDAi3.1.2.22. 5613.
ReactomeiR-SPO-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

PROiO59747.

Family and domain databases

Gene3Di1.20.144.10. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000326. P_Acid_Pase_2/haloperoxidase.
IPR002472. Palm_thioest.
[Graphical view]
PfamiPF02089. Palm_thioest. 1 hit.
PF01569. PAP2. 1 hit.
[Graphical view]
SMARTiSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
SSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPDF1_SCHPO
AccessioniPrimary (citable) accession number: O59747
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 3, 2012
Last modified: November 30, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.