ERFB_YARLI
ID ERFB_YARLI Reviewed; 408 AA.
AC Q6C890;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 25-MAY-2022, entry version 81.
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=YALI0D21670g;
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: 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG81316.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382130; CAG81316.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_503122.1; XM_503122.1.
DR AlphaFoldDB; Q6C890; -.
DR SMR; Q6C890; -.
DR STRING; 4952.CAG81316; -.
DR GeneID; 2911083; -.
DR KEGG; yli:YALI0D21670g; -.
DR InParanoid; Q6C890; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Palmitoyltransferase ERF2"
FT /id="PRO_0000212947"
FT TOPO_DOM 1..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..125
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..296
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 209..259
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 408 AA; 45571 MW; EF02F9B1C80FA236 CRC64;
MDFYTPPTTA GPPTRGSPES VPTTAASTFP LRKRTRAHLR ARDKSDGPAP SSRGTSDRLW
SWVFLKQPLS LPEHNYQAHL GNNVFLIGGR FLSARQKPLN IAVLCVILIL GGLYYGFVAP
WTWNHISPAI PAVFTYIFLL CVASFLRASF SDPGILPRNI HLTDRIADGS IPNEYSVEPG
IDAFDPRKNT TSLSCFKQPE SSENLVYLKY CSTCKIWRPP RASHCSDCDN CVDFHDHHCI
WLNNCVGRKN YRYFVAFVMT GGLCGLYIVG NSIAHVICYK RHMHMTIAES LRHRPMPLVM
IFLGFLGAGY PLALVGFHLW IASRGESTHE FVSMNPVTKH VVDGHVGVTL SKCKVMGSHD
GFKRFSDAVL AVVCARLCAH VSPHSNPVTK QTTPQGVQKS TFRHWKRF
