Reviewed, UniProtKB/Swiss-Prot O59747 (PDF1_SCHPO)

Names and origin

Protein names

Recommended name:
    Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1
Cleaved into the following 2 chains:
    1- Recommended name:
            Palmitoyl-protein thioesterase
                Short name=PPT
              EC=3.1.2.22
        Alternative name(s):
            Palmitoyl-protein hydrolase
    2- Recommended name:
            Dolichyldiphosphatase
              EC=3.6.1.43
        Alternative name(s):
            Dolichyl pyrophosphate phosphatase

Gene names

Name:	pdf1
Synonyms:	yhc1
ORF Names:	SPBC530.12c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.1 UniProtKB P45478 UniProtKB P53223
Catalytic activity	Palmitoyl-protein + H2O = palmitate + protein. UniProtKB P45478 Dolichyl diphosphate + H2O = dolichyl phosphate + phosphate. UniProtKB P53223
Subcellular location	Vacuole Potential. Endoplasmic reticulum membrane; Multi-pass membrane protein Potential. Ref.1 Ref.3
Post-translational modification	Proteolytically cleaved, possibly by krp1. Ref.1
Disruption phenotype	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. Ref.1
Sequence similarities	In the N-terminal section; belongs to the palmitoyl-protein thioesterase family. In the C-terminal section; belongs to the dolichyldiphosphatase family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Vacuole
Domain	Transmembrane
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro vacuolar acidification Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe
Cellular component	endoplasmic reticulum Ref.3 Inferred from direct assay. Source: GeneDB_SPombe integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell vacuole Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	dolichyldiphosphatase activity Ref.1 Traceable author statement. Source: GeneDB_SPombe palmitoyl-(protein) hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 603	603	Palmitoyl-protein thioesterase-dolichyl pyrophosphate phosphatase fusion 1		PRO_0000349152
	Chain	1 – ?		Palmitoyl-protein thioesterase Ref.1		PRO_0000349153
	Chain	? – 603		Dolichyldiphosphatase Ref.1		PRO_0000349154
Regions
	Transmembrane	387 – 407	21	Potential
	Transmembrane	410 – 430	21	Potential
	Transmembrane	470 – 492	23	Potential
	Transmembrane	501 – 521	21	Potential
	Transmembrane	534 – 554	21	Potential
Sites
	Active site	106	1	By similarity UniProtKB P45478
	Active site	226	1	By similarity UniProtKB P45478
	Active site	279	1	By similarity UniProtKB P45478
	Site	354	1	Crucial for post-translational processing Ref.1
Amino acid modifications
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Glycosylation	241	1	N-linked (GlcNAc...) Potential
	Glycosylation	377	1	N-linked (GlcNAc...) Potential
	Disulfide bond	87 ↔ 119		By similarity UniProtKB P45478
Experimental info
	Mutagenesis	106	1	S → A: Sensitive to vanadate and elevation of external pH. Ref.1
	Mutagenesis	226	1	D → A: Sensitive to vanadate and elevation of external pH. Ref.1
	Mutagenesis	303 – 603	301	Missing: Lethal. Ref.1
	Mutagenesis	344	1	R → A: No prevention of cleavage of the linker domain, but increases the ratio of the unprocessed from the processed form. Ref.1
	Mutagenesis	354	1	R → A: Abolished cleavage of the linker domain. Ref.1
	Mutagenesis	478	1	H → A: Lethal. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O59747-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 0BD505208B1F12AF	FASTA	603	68,963
	10 20 30 40 50 60 MKSFAIPIIS LDKVRLAIND GASEQLPVVI WHGLGDTPTS FTLTEVSQRV QKLTKGAVYA 70 80 90 100 110 120 IRVGDNEFED IKAGYLGKLE DQLDEVCDLI GNEDSLSNGF YALGLSQGGL FLRALAQTCD 130 140 150 160 170 180 AAKIRSLITL GSPHSGINTI PGCSPTNLIC KAVVHSILGL GIWHSWIQNH VVQAQYYRTE 190 200 210 220 230 240 KQYDKYLENN KFLTHLNNEV LHDNYTRNIE KLKELDNLVA VSFERDDIVE PPYSTGFGWI 250 260 270 280 290 300 NETTGENIEM EDFVLYESLG LKDLVNQGKL ETISFPGRHL QMRWGDFDAL VLKYFKDEKE 310 320 330 340 350 360 EKTELEESTR PSNFLSTYFV SPLVSAIDGT VDYLHGKSLF PEKRNFKELT MRKRSIVTPE 370 380 390 400 410 420 DSEEVYPYIS EFVAASNVSE EKGPKSFANL AFITIFSHFF YHIDDMWRST LGLFSLIPQI 430 440 450 460 470 480 IGIIYLTVMF TGRELDTFMQ FGGQVVNEFI NYVVKVSLKY PRPADIEYGV GYGMPSSHSQ 490 500 510 520 530 540 FMGFFSAYMI AWDYKYRRSQ CFSMLSFAKY AIYLTLSTFV CSSRYLLDFH YLTQVVYGYM 550 560 570 580 590 600 IGFGVGLFWV YLVGKLRSLG VTKWLLSLPP LQFFYIKDTI PHSKDNHKRQ WLESKQFKNQ KSN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"pdf1, a palmitoyl protein thioesterase 1 ortholog in Schizosaccharomyces pombe: a yeast model of infantile Batten disease." Cho S.K., Hofmann S.L. Eukaryot. Cell 3:302-310(2004) [PubMed: 15075260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE, MUTAGENESIS OF SER-106; ASP-226; 303-THR--ASN-603; ARG-344; ARG-354 AND HIS-478, DISRUPTION PHENOTYPE.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA19178.1.
PIR	T40528.
RefSeq	NP_595325.1.
3D structure databases
HSSP	HSSP built from PDB template 1EI9 based on UniProtKB P45478.
ModBase	Search...
Protein-protein interaction databases
STRING	O59747.
Genome annotation databases
GeneID	2540904.
GenomeReviews	Gene locus pdf1 in contig CU329671_GR.
KEGG	spo:SPBC530.12c.
NMPDR	fig|4896.1.peg.1191.
Organism-specific databases
GeneDB_Spombe	SPBC530.12c.
Gene expression databases
ArrayExpress	O59747.
Family and domain databases
InterPro	IPR000326. P_Acid_Pase_2/haloperoxidase. IPR002472. Palm_thioest. [Graphical view]
Pfam	PF02089. Palm_thioest. 1 hit. PF01569. PAP2. 1 hit. [Graphical view]
SMART	SM00014. acidPPc. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDF1_SCHPO

Accession

Primary (citable) accession number: O59747

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	August 1, 1998
Last modified:	October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)