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Protein

Palmitoyltransferase PFA5

Gene

PFA5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.

GO - Molecular functioni

GO - Biological processi

  • protein palmitoylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-29987-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase PFA5 (EC:2.3.1.225)
Alternative name(s):
Protein fatty acyltransferase 5
Gene namesi
Name:PFA5
Ordered Locus Names:YDR459C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR459C.
SGDiS000002867. PFA5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421HelicalSequence analysisAdd
BLAST
Topological domaini35 – 5521LumenalSequence analysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence analysisAdd
BLAST
Topological domaini77 – 17397CytoplasmicSequence analysisAdd
BLAST
Transmembranei174 – 19421HelicalSequence analysisAdd
BLAST
Topological domaini195 – 21723LumenalSequence analysisAdd
BLAST
Transmembranei218 – 23821HelicalSequence analysisAdd
BLAST
Topological domaini239 – 374136CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Palmitoyltransferase PFA5PRO_0000212983Add
BLAST

Post-translational modificationi

Autopalmitoylated.

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

BioGridi32513. 17 interactions.
DIPiDIP-5400N.
IntActiQ03289. 1 interaction.
MINTiMINT-505085.

Structurei

3D structure databases

ProteinModelPortaliQ03289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini129 – 17951DHHCPROSITE-ProRule annotationAdd
BLAST

Domaini

The DHHC domain is required for palmitoyltransferase activity.By similarity

Sequence similaritiesi

Contains 1 DHHC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000001066.
InParanoidiQ03289.
KOiK18932.
OMAiPRFDHYC.
OrthoDBiEOG73NGFX.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. DHHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03289-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSWNIRIR RRSWFRFILP IIVLGLLCYG TWAYCHKLCY EQVDKRLRQK
60 70 80 90 100
SVSVGLICAV CFLDVVVIFI WLQIVILVGP GTQPHVAPFL ILPIASEEKT
110 120 130 140 150
SNTSQNTSVE YDAVVPPKCY QSDPHGYPIW CSECQSLKME RTHHSSELGH
160 170 180 190 200
CIPRFDHYCM WIGTVIGRDN YRLFVQFAAY FSTLLLIMWV SICVYIRIIT
210 220 230 240 250
QHNHNYSPNL NANIISTLVF AILGWLLTAS LLASSIFYMS QNKTSLEAII
260 270 280 290 300
DSKRKKFGTR KIFCYYSEAN KLRFVVEFDR SEFHSFWDKK SILANIKDFM
310 320 330 340 350
GSNILMWIIP LGKPYTSRCK SDGKSGSKTT LVEILGPYEE TLSDYTIQAI
360 370
EDKISRGEYL ATLRASGDDS DPAY
Length:374
Mass (Da):42,923
Last modified:November 1, 1996 - v1
Checksum:i2AAB3E78B2FD0F89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64921.1.
BK006938 Genomic DNA. Translation: DAA12293.1.
PIRiS69627.
RefSeqiNP_010747.1. NM_001180767.1.

Genome annotation databases

EnsemblFungiiYDR459C; YDR459C; YDR459C.
GeneIDi852070.
KEGGisce:YDR459C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33050 Genomic DNA. Translation: AAB64921.1.
BK006938 Genomic DNA. Translation: DAA12293.1.
PIRiS69627.
RefSeqiNP_010747.1. NM_001180767.1.

3D structure databases

ProteinModelPortaliQ03289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32513. 17 interactions.
DIPiDIP-5400N.
IntActiQ03289. 1 interaction.
MINTiMINT-505085.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR459C; YDR459C; YDR459C.
GeneIDi852070.
KEGGisce:YDR459C.

Organism-specific databases

EuPathDBiFungiDB:YDR459C.
SGDiS000002867. PFA5.

Phylogenomic databases

HOGENOMiHOG000001066.
InParanoidiQ03289.
KOiK18932.
OMAiPRFDHYC.
OrthoDBiEOG73NGFX.

Enzyme and pathway databases

BioCyciYEAST:G3O-29987-MONOMER.

Miscellaneous databases

PROiQ03289.

Family and domain databases

InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. DHHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p."
    Smotrys J.E., Schoenfish M.J., Stutz M.A., Linder M.E.
    J. Cell Biol. 170:1091-1099(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPALMITOYLATION.
  4. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiPFA5_YEAST
AccessioniPrimary (citable) accession number: Q03289
Secondary accession number(s): D6VT83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 108 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.