SWF1_CANGA
ID SWF1_CANGA Reviewed; 330 AA.
AC Q6FXC6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Palmitoyltransferase SWF1;
DE EC=2.3.1.225;
GN Name=SWF1; OrderedLocusNames=CAGL0B01991g;
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: Palmitoyltransferase that targets several endosomal SNAREs.
CC Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic
CC end of their transmembrane domain. May have a role in the cellular
CC quality control of transmembrane domain-containing proteins (By
CC 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: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass 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. SWF1
CC subfamily. {ECO:0000305}.
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DR EMBL; CR380948; CAG57956.1; -; Genomic_DNA.
DR RefSeq; XP_445056.1; XM_445056.1.
DR AlphaFoldDB; Q6FXC6; -.
DR STRING; 5478.XP_445056.1; -.
DR EnsemblFungi; CAG57956; CAG57956; CAGL0B01991g.
DR GeneID; 2886685; -.
DR KEGG; cgr:CAGL0B01991g; -.
DR CGD; CAL0127124; CAGL0B01991g.
DR VEuPathDB; FungiDB:CAGL0B01991g; -.
DR eggNOG; KOG1312; Eukaryota.
DR HOGENOM; CLU_042181_2_0_1; -.
DR InParanoid; Q6FXC6; -.
DR OMA; STNAYDH; -.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR GO; GO:0032432; C:actin filament bundle; IEA:EnsemblFungi.
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 GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR GO; GO:0018345; P:protein palmitoylation; IEA:EnsemblFungi.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:EnsemblFungi.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; 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..330
FT /note="Palmitoyltransferase SWF1"
FT /id="PRO_0000212987"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..86
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..218
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..184
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 330 AA; 38744 MW; 852965A498FB24E2 CRC64;
MLLFLVFILV VSQVVLLLLS PQFRDKFIFR WYYDEVYKPM ILDNSRYRIK FYVVPVFYLS
VYSYMVYIFY SRTFAIISPM LTSIETYVVI PLMLILPLFF GSMSMIIKPD SSNAHQIGSE
KRYPYDNLLY FPQHECRTCK QVKPARSKHC TVCNSCIYLA DHHCVWINNC VGMGNYMYFY
SFLCSNLLLL SYSFIRLIFI QFNKSAYNTT PTGEKSLLIL SILCGSFTVI LAVYCYFVFE
LVNSGMTTNE KDKWQMVHDY INTGDLVRDP EGKYFIKYQN GGNNYEFYST DSYDGTQYTI
VDYFTVKSPA EITNIYDKGN FINNLREFIG
