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Protein

Palmitoyltransferase PFA4

Gene

PFA4

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

Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function. Palmitoylates several amino acid permeases (PubMed:16751107). Palmitoylates chitin synthase CHS3, which is required for its proper export from the ER (PubMed:16818716). Can palmitoylate RAS2 in vitro (PubMed:12379641).UniRule annotation3 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081S-palmitoyl cysteine intermediateUniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:G3O-33420-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Palmitoyltransferase PFA41 PublicationUniRule annotation (EC:2.3.1.225UniRule annotation1 Publication)
Alternative name(s):
Protein S-acyltransferase1 PublicationUniRule annotation
Short name:
PATUniRule annotation
Protein fatty acyltransferase 4UniRule annotation
Gene namesi
Name:PFA41 PublicationUniRule annotation
Ordered Locus Names:YOL003CImported
ORF Names:UNE378
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL003C.
SGDiS000005363. PFA4.

Subcellular locationi

  • Endoplasmic reticulum membrane UniRule annotation1 Publication; Multi-pass membrane protein UniRule annotation1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicUniRule annotation1 Publication
Transmembranei10 – 3021HelicalUniRule annotationAdd
BLAST
Topological domaini31 – 4010LumenalUniRule annotation1 Publication
Transmembranei41 – 6121HelicalUniRule annotationAdd
BLAST
Topological domaini62 – 11958CytoplasmicUniRule annotation1 PublicationAdd
BLAST
Transmembranei120 – 14021HelicalUniRule annotationAdd
BLAST
Topological domaini141 – 16424LumenalUniRule annotation1 PublicationAdd
BLAST
Transmembranei165 – 18521HelicalUniRule annotationAdd
BLAST
Topological domaini186 – 378193CytoplasmicUniRule annotation1 PublicationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Leads to the retention of non-palmitoylated CHS3 in the endoplasmic reticulum and reduced levels of chitin on the cell wall.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081C → A: Causes mislocalization of chitin synthase CHS3 (PubMed:16818716). Reduces, but does not abolish catalytic activity. Lacks autopalmitoylation (PubMed:26224664). 2 Publications
Mutagenesisi108 – 1081C → R: Reduces, but does not abolish catalytic activity. Lacks autopalmitoylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 378378Palmitoyltransferase PFA4PRO_0000212972Add
BLAST

Post-translational modificationi

Autopalmitoylated.2 Publications

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ12006.

PTM databases

iPTMnetiQ12006.

Interactioni

Protein-protein interaction databases

BioGridi34401. 57 interactions.
DIPiDIP-4248N.
IntActiQ12006. 3 interactions.
MINTiMINT-508085.

Structurei

3D structure databases

ProteinModelPortaliQ12006.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini78 – 12851DHHCPROSITE-ProRule annotationAdd
BLAST

Domaini

The DHHC domain is required for palmitoyltransferase activity.UniRule annotation

Sequence similaritiesi

Belongs to the DHHC palmitoyltransferase family. PFA4 subfamily.UniRule annotation
Contains 1 DHHC domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00840000129737.
HOGENOMiHOG000248636.
InParanoidiQ12006.
KOiK18932.
OMAiERSHHCK.
OrthoDBiEOG7Z95WQ.

Family and domain databases

HAMAPiMF_03199. DHHC_PAT_PFA4.
InterProiIPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
PfamiPF01529. zf-DHHC. 1 hit.
[Graphical view]
PROSITEiPS50216. DHHC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12006-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVKLRWPWL GIAIPTFLIS FIGYGAHYFI LSNFLSVPKQ ITFEFCLSMI
60 70 80 90 100
WLSYYLAICT NPGRPLPNYK PPPDIWRNFC KKCQSYKPER SHHCKTCNQC
110 120 130 140 150
VLMMDHHCPW TMNCVGFANY PHFLRFLFWI IVTTSVLFCI QAKRIYFIWQ
160 170 180 190 200
QRHLPGYFFK KSELIFLTIS SPLNSFVLLT ITILFLRCLF NQILNGRSQI
210 220 230 240 250
ESWDMDRLES LFNSGRLTQK LIDNTWRIYP ESRSFQNKKD AEEHLTKKRP
260 270 280 290 300
RFDELVNFPY DFDLYTNALL YLGPIHLWLW PYGVPTGDGN NFPKNGISKY
310 320 330 340 350
EANSSLEDHI LSLPWPPDGG KTNTVFNHGS STIEMRNESG EQLIRTRLPQ
360 370
NGRHASREKW YNDWGESLDD FGVDVDME
Length:378
Mass (Da):44,488
Last modified:November 1, 1996 - v1
Checksum:i52156A3BF98F5755
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43491 Genomic DNA. Translation: AAC49477.1.
Z74745 Genomic DNA. Translation: CAA99002.1.
AY558023 Genomic DNA. Translation: AAS56349.1.
BK006948 Genomic DNA. Translation: DAA10780.1.
PIRiS61981.
RefSeqiNP_014640.1. NM_001183257.1.

Genome annotation databases

EnsemblFungiiYOL003C; YOL003C; YOL003C.
GeneIDi854159.
KEGGisce:YOL003C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43491 Genomic DNA. Translation: AAC49477.1.
Z74745 Genomic DNA. Translation: CAA99002.1.
AY558023 Genomic DNA. Translation: AAS56349.1.
BK006948 Genomic DNA. Translation: DAA10780.1.
PIRiS61981.
RefSeqiNP_014640.1. NM_001183257.1.

3D structure databases

ProteinModelPortaliQ12006.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34401. 57 interactions.
DIPiDIP-4248N.
IntActiQ12006. 3 interactions.
MINTiMINT-508085.

PTM databases

iPTMnetiQ12006.

Proteomic databases

MaxQBiQ12006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL003C; YOL003C; YOL003C.
GeneIDi854159.
KEGGisce:YOL003C.

Organism-specific databases

EuPathDBiFungiDB:YOL003C.
SGDiS000005363. PFA4.

Phylogenomic databases

GeneTreeiENSGT00840000129737.
HOGENOMiHOG000248636.
InParanoidiQ12006.
KOiK18932.
OMAiERSHHCK.
OrthoDBiEOG7Z95WQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33420-MONOMER.

Miscellaneous databases

PROiQ12006.

Family and domain databases

HAMAPiMF_03199. DHHC_PAT_PFA4.
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 sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes."
    Sterky F., Holmberg A., Pettersson B., Uhlen M.
    Yeast 12:1091-1095(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [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. "Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins."
    Zhao L., Lobo S., Dong X., Ault A.D., Deschenes R.J.
    J. Biol. Chem. 277:49352-49359(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation."
    Valdez-Taubas J., Pelham H.R.B.
    EMBO J. 24:2524-2532(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "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.
  8. Cited for: FUNCTION.
  9. "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3."
    Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.
    J. Cell Biol. 174:19-25(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-108, DISRUPTION PHENOTYPE.
  10. "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.
  11. "The canonical DHHC motif is not absolutely required for the activity of the yeast S-acyltransferases Swf1 and Pfa4."
    Gonzalez Montoro A., Chumpen Ramirez S., Valdez Taubas J.
    J. Biol. Chem. 290:22448-22459(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-108.

Entry informationi

Entry nameiPFA4_YEAST
AccessioniPrimary (citable) accession number: Q12006
Secondary accession number(s): D6W264
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 118 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.