ERFB_CANGA
ID ERFB_CANGA Reviewed; 326 AA.
AC Q6FSS4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Palmitoyltransferase ERF2;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE AltName: Full=DHHC cysteine-rich domain-containing protein ERF2;
DE AltName: Full=Ras protein acyltransferase;
GN Name=ERF2; OrderedLocusNames=CAGL0G08217g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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: The ERF2-ERF4 complex is a palmitoyltransferase specific for
CC Ras proteins. {ECO:0000250|UniProtKB:Q06551}.
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:0000250|UniProtKB:Q8VDZ4};
CC -!- SUBUNIT: Interacts with ERF4. {ECO:0000250|UniProtKB:Q06551}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q06551}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q06551}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; CR380953; CAG59647.1; -; Genomic_DNA.
DR RefSeq; XP_446720.1; XM_446720.1.
DR AlphaFoldDB; Q6FSS4; -.
DR SMR; Q6FSS4; -.
DR STRING; 5478.XP_446720.1; -.
DR EnsemblFungi; CAG59647; CAG59647; CAGL0G08217g.
DR GeneID; 2888209; -.
DR KEGG; cgr:CAGL0G08217g; -.
DR CGD; CAL0130306; CAGL0G08217g.
DR VEuPathDB; FungiDB:CAGL0G08217g; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_047581_0_0_1; -.
DR InParanoid; Q6FSS4; -.
DR Proteomes; UP000002428; Chromosome G.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0031211; C:endoplasmic reticulum palmitoyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IEA:EnsemblFungi.
DR GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
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..326
FT /note="Palmitoyltransferase ERF2"
FT /id="PRO_0000212940"
FT TOPO_DOM 1..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..90
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..241
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 158..208
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 188
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 326 AA; 37644 MW; 6352F4C324610E04 CRC64;
MKGNPSTHEV IGTMSTRRFY RWLITIDGDT EINYRNYEEL PSRSNYIFFF GGRLRAVKTA
RPFSLVVLFL ILSPMVLFSV FEAHRLWHTR YGYKALVVLF YYAWAWSLLS FTKTATSDPG
VLPRNIHMHK DTPQEYFNNV TLPYGAGGSA GNASVTLKYC HTCKIWRPPR ASHCSVCECC
VLTHDHHCIW VNNCVGQRNY RYFLAFLLSS TLACALLIAN CALHLHRALH EGIRVSHRPL
PVAVLLCVYA AVLCVYPVIL LGYHVAMSGT QQTTREYLRS IGFRNPVMHR IRRRRDNPYA
EHGFLRNMLD LMAEPRGPRS CNYRYR
