ERFB_DEBHA
ID ERFB_DEBHA Reviewed; 371 AA.
AC Q6BHT4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 88.
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=DEHA2G15972g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382139; CAG90733.2; -; Genomic_DNA.
DR RefSeq; XP_462237.2; XM_462237.1.
DR AlphaFoldDB; Q6BHT4; -.
DR SMR; Q6BHT4; -.
DR STRING; 4959.XP_462237.2; -.
DR EnsemblFungi; CAG90733; CAG90733; DEHA2G15972g.
DR GeneID; 2905161; -.
DR KEGG; dha:DEHA2G15972g; -.
DR VEuPathDB; FungiDB:DEHA2G15972g; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_047581_1_0_1; -.
DR InParanoid; Q6BHT4; -.
DR OMA; KNLYINW; -.
DR OrthoDB; 1264614at2759; -.
DR Proteomes; UP000000599; Chromosome G.
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-EC.
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..371
FT /note="Palmitoyltransferase ERF2"
FT /id="PRO_0000212941"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..106
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..274
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 181..231
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 211
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 371 AA; 43141 MW; 1DF571158B778855 CRC64;
MSRRERYSVE PIPNDANEFQ DNVSFIHKFI TNWLITDPSL RNPGSEKNVK AKNYQVQKHE
NVQFIYLCGG RLRSVKQKPI NVVTGISILI PGILFWIFEA KWIWFHVNPS IVILFSYFWL
ITVSFFIKAS MSDPGMLPRN IHVPYSISNA NTSPKASPPD EYFNIISLPY NAEDHTGVGL
KYCATCHIWR SPRASHCSVC NSCIISHDHH CVFLNNCIGY RNYKYFLWFL LFAVLGCILM
SVISFIHVFY YRLGMETSVS TFRSSISKYP VSFLLCIYSL LALVYPFPLL IFHIFLTSYN
LTTREYFNNV RGVKNSQNHF TNHFDTHSIF KNLYINWLGR ARGFSLVRQT DSYQIGDLRF
EKLDPLQSFS S
