SWF1_KLULA
ID SWF1_KLULA Reviewed; 324 AA.
AC Q6CJC5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Palmitoyltransferase SWF1;
DE EC=2.3.1.225;
GN Name=SWF1; OrderedLocusNames=KLLA0F19690g;
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: 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; CR382126; CAG98672.1; -; Genomic_DNA.
DR RefSeq; XP_455964.1; XM_455964.1.
DR AlphaFoldDB; Q6CJC5; -.
DR SMR; Q6CJC5; -.
DR STRING; 28985.XP_455964.1; -.
DR EnsemblFungi; CAG98672; CAG98672; KLLA0_F19690g.
DR GeneID; 2895524; -.
DR KEGG; kla:KLLA0_F19690g; -.
DR eggNOG; KOG1312; Eukaryota.
DR HOGENOM; CLU_042181_2_0_1; -.
DR InParanoid; Q6CJC5; -.
DR OMA; STNAYDH; -.
DR Proteomes; UP000000598; Chromosome F.
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..324
FT /note="Palmitoyltransferase SWF1"
FT /id="PRO_0000212990"
FT TOPO_DOM 1
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..84
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..203
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 127..177
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 324 AA; 38289 MW; 55FE8F87BC0AB769 CRC64;
MFLLFLLFVV SQVGLLVFSP KFKDLILFRW YYQHIYYPLF TDYTRYRWKY WLVPGFYACI
LIFCVHLFYN KLNDTVNPYL YSLEKAFIPI TIAFTSLTGV ASVFVKPLGL QAGPQFQPDY
IIFHPSAVCQ TCKTIKVPRS KHCPICERCI PLHDHHCIWI NNCVGYGNYE YFYSFLLSNC
LLLTYASLRL LTLFRITAFK KDKFFLSLFL LTTAFSLIAI VFTYYQLKLV NDGMTNNEQD
KWYLVQEYMR NGNLVKDMDG VLYYRSMSTD AQTAEPIFYS TNLYDHSKYH LINPAKILSH
EEIINLYDRG SFLDNLKERI HLLD
