ID PFA3_KLULA Reviewed; 325 AA.
AC Q6CPU8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Palmitoyltransferase PFA3;
DE EC=2.3.1.225;
DE AltName: Full=Protein fatty acyltransferase 3;
GN Name=PFA3; OrderedLocusNames=KLLA0E02068g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at
CC one or more of its N-terminal cysteine residues, which is required for
CC its proper membrane localization (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382125; CAG99128.1; -; Genomic_DNA.
DR RefSeq; XP_454041.1; XM_454041.1.
DR AlphaFoldDB; Q6CPU8; -.
DR SMR; Q6CPU8; -.
DR STRING; 284590.Q6CPU8; -.
DR PaxDb; 284590-Q6CPU8; -.
DR DNASU; 2894120; -.
DR GeneID; 2894120; -.
DR KEGG; kla:KLLA0_E02069g; -.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_0_0_1; -.
DR InParanoid; Q6CPU8; -.
DR OMA; CFVVMHI; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..325
FT /note="Palmitoyltransferase PFA3"
FT /id="PRO_0000212956"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..35
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..185
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 103..153
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 325 AA; 37933 MW; EB814ED28147DE97 CRC64;
MLLDRIGFYF PKALSNFLIL YTCCICFSRI DILPRIVNVV LLITLSSFAL YTYWKIIRVG
AGSPLEYSFL KIQSIDNVLN RTEQPPDIIK DNCIFVKRDG SFRFCQTCEI WKPDRCHHCS
KCNKCFLKMD HHCPWFASCV GFRNQKFFVQ FLAYTTVYSL YVLLMTSAQL YSWFRQMKYK
SELLDLHLLV VWVLSVIAAI ATFAFTTYTI WLVTKNETTI EQYEWGNIRH DLEIYGDSIN
CNMGSVDNVF DLGSRSANFN CVMGASWAEL LLPIQVRADD PFDPYANQGL FFPVQSDTYR
IYRESVNLQQ RLITRLTLRP SIEHI
//
