PFA4_KLULA
ID PFA4_KLULA Reviewed; 377 AA.
AC Q6CUB5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
DE Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN OrderedLocusNames=KLLA0C06204g;
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: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000255|HAMAP-Rule:MF_03199}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_03199};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
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DR EMBL; CR382123; CAH01325.1; -; Genomic_DNA.
DR RefSeq; XP_452474.1; XM_452474.1.
DR AlphaFoldDB; Q6CUB5; -.
DR STRING; 28985.XP_452474.1; -.
DR EnsemblFungi; CAH01325; CAH01325; KLLA0_C06204g.
DR GeneID; 2892046; -.
DR KEGG; kla:KLLA0_C06204g; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_0_1; -.
DR InParanoid; Q6CUB5; -.
DR OMA; DQLNLPW; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018345; P:protein palmitoylation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Palmitoyltransferase PFA4"
FT /id="PRO_0000212968"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 31..122
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 144..163
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 185..377
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT DOMAIN 78..128
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 108
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ SEQUENCE 377 AA; 44192 MW; B241E3F452A651D8 CRC64;
MAIKLKNRWL GVAIPAFLVA LIGYGSHYFI LSNFLSWNEQ IFYQTCQTMI WVSYYLAIYT
NPGIPPKDFK PSAEEWHNYC KKCRVYKPER AHHCKTCNQC VLAMDHHCPW TLNCVGHSNF
PHFMRFLFWV IFSTAYLLFL LIGRIYLLWS IRHTAFHHRS TSEIIFICIM TPMDAFVLLT
VSSLLGRCIY NQCLHGMTQI ESWEMDRIQS LHYKNRLLAQ VIDRLVERRP EILPAKQHEI
NKLLSKRYVN QEDFTNFPYD VNPWTNINNA MGPWYLWLWP WSKPPTIGTS FAKNELFFYD
PNSSIEDMLM SLPWPPDGLT HHSRALGSGS SIETIVSGGE QVIRDKSVDL RDRLGRNSWY
NDWGEDLSDF GVDTELE
