PFA3_YARLI
ID PFA3_YARLI Reviewed; 401 AA.
AC Q6C4W5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Palmitoyltransferase PFA3;
DE EC=2.3.1.225;
DE AltName: Full=Protein fatty acyltransferase 3;
GN Name=PFA3; OrderedLocusNames=YALI0E23177g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC subfamily. {ECO:0000305}.
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DR EMBL; CR382131; CAG79896.1; -; Genomic_DNA.
DR RefSeq; XP_504297.1; XM_504297.1.
DR AlphaFoldDB; Q6C4W5; -.
DR SMR; Q6C4W5; -.
DR STRING; 4952.CAG79896; -.
DR EnsemblFungi; CAG79896; CAG79896; YALI0_E23177g.
DR GeneID; 2912928; -.
DR KEGG; yli:YALI0E23177g; -.
DR VEuPathDB; FungiDB:YALI0_E23177g; -.
DR HOGENOM; CLU_027721_0_0_1; -.
DR InParanoid; Q6C4W5; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
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..401
FT /note="Palmitoyltransferase PFA3"
FT /id="PRO_0000212958"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..56
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..220
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 127..177
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 351..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 401 AA; 45892 MW; 8664B960B35021F2 CRC64;
MQCRKCCFAC EKWCFIGAKA FLPLVVNFLI IWACWVHAWL VCWEPQLFES DTTFWRVYGV
AGVAIGIMCN VLYLKVCKVG PGSPTDIDNF SVPLVEYQNA CSAEGQHLTP PREMANSVCA
KENGGLRFCT KCIGWKPDRS HHCSNYKRCV LKFDHYCPWF ATAIGFHNHK YFVLFLWYVT
ILCFFCLGST GFVFYNHILE IGAMRGPDGN TDYVGAISVN VMILMVLALV FAIAVGTFAT
FSLYLVFNNQ STVEFLESTQ YRSAVPTAAY RYTFAPTSKT VGNVFDVGWK RNFQLVMGDK
WWMWLLPIQP SEAARGNGTQ FPLNKQVLQK IREAAAKEVQ IRDQNQAYIK QQRQQQQKRT
QYDLPQHLQP PPQEHYEYDD EAQDSGDDIP LINMVNKNNT K
