SWF1_YEAST
ID SWF1_YEAST Reviewed; 336 AA.
AC Q04629; D6VSB2; Q03889;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Palmitoyltransferase SWF1;
DE EC=2.3.1.225;
DE AltName: Full=Spore wall formation protein 1;
GN Name=SWF1; Synonyms=PSL10; OrderedLocusNames=YDR126W;
GN ORFNames=YD9302.01, YD9727.21;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-164, AND SUBCELLULAR LOCATION.
RX PubMed=15973437; DOI=10.1038/sj.emboj.7600724;
RA Valdez-Taubas J., Pelham H.R.B.;
RT "Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its
RT ubiquitination and degradation.";
RL EMBO J. 24:2524-2532(2005).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs.
CC Palmitoylates the SNAREs SNC1, SNC2, SYN8 and TLG1, at cysteine
CC residues close to the cytoplasmic end of their transmembrane domain.
CC May have a role in the cellular quality control of transmembrane
CC domain-containing proteins. {ECO:0000269|PubMed:15973437}.
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
CC {ECO:0000269|PubMed:15973437}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15973437}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. SWF1
CC subfamily. {ECO:0000305}.
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DR EMBL; Z48758; CAA88679.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88207.1; -; Genomic_DNA.
DR EMBL; AY557692; AAS56018.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11972.1; -; Genomic_DNA.
DR PIR; S52691; S52691.
DR RefSeq; NP_010411.1; NM_001180434.1.
DR AlphaFoldDB; Q04629; -.
DR BioGRID; 32182; 483.
DR DIP; DIP-8105N; -.
DR IntAct; Q04629; 2.
DR MINT; Q04629; -.
DR STRING; 4932.YDR126W; -.
DR MaxQB; Q04629; -.
DR PaxDb; Q04629; -.
DR EnsemblFungi; YDR126W_mRNA; YDR126W; YDR126W.
DR GeneID; 851704; -.
DR KEGG; sce:YDR126W; -.
DR SGD; S000002533; SWF1.
DR VEuPathDB; FungiDB:YDR126W; -.
DR eggNOG; KOG1312; Eukaryota.
DR GeneTree; ENSGT00940000164006; -.
DR HOGENOM; CLU_042181_2_0_1; -.
DR InParanoid; Q04629; -.
DR OMA; STNAYDH; -.
DR BioCyc; YEAST:G3O-29726-MON; -.
DR BRENDA; 2.3.1.225; 984.
DR PRO; PR:Q04629; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04629; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0032432; C:actin filament bundle; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
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:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:SGD.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IGI:SGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Palmitoyltransferase SWF1"
FT /id="PRO_0000212994"
FT TOPO_DOM 1..2
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..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..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..216
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 134..184
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MUTAGEN 164
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15973437"
SQ SEQUENCE 336 AA; 39312 MW; 1F61B9809383A94C CRC64;
MSWNLLFVLL IGFVVLILLS PVFKSTWPFS TFYRNVFQPF LVDDQKYRWK LHLVPLFYTS
IYLYLVYTYH MRVESTIKNE LFLLERILIV PIIILPPVAL GILAMVSRAE DSKDHKSGST
EEYPYDYLLY YPAIKCSTCR IVKPARSKHC SICNRCVLVA DHHCIWINNC IGKGNYLQFY
LFLISNIFSM CYAFLRLWYI SLNSTSTLPR AVLTLTILCG CFTIICAIFT YLQLAIVKEG
MTTNEQDKWY TIQEYMREGK LVRSLDDDCP SWFFKCTEQK DDAAEPLQDQ HVTFYSTNAY
DHKHYNLTHY ITIKDASEIP NIYDKGTFLA NLTDLI
