PFA4_YEAST
ID PFA4_YEAST Reviewed; 378 AA.
AC Q12006; D6W264;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000303|PubMed:16751107};
DE EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000305|PubMed:16818716};
DE AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000303|PubMed:26224664};
DE Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000303|PubMed:16751107};
GN OrderedLocusNames=YOL003C {ECO:0000312|SGD:S000005363}; ORFNames=UNE378;
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 [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=12379641; DOI=10.1074/jbc.m209760200;
RA Zhao L., Lobo S., Dong X., Ault A.D., Deschenes R.J.;
RT "Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved
RT in the plasma membrane localization of yeast Ras proteins.";
RL J. Biol. Chem. 277:49352-49359(2002).
RN [6]
RP 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 [7]
RP AUTOPALMITOYLATION.
RX PubMed=16186255; DOI=10.1083/jcb.200507048;
RA Smotrys J.E., Schoenfish M.J., Stutz M.A., Linder M.E.;
RT "The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for
RT Vac8p.";
RL J. Cell Biol. 170:1091-1099(2005).
RN [8]
RP FUNCTION.
RX PubMed=16751107; DOI=10.1016/j.cell.2006.03.042;
RA Roth A.F., Wan J., Bailey A.O., Sun B., Kuchar J.A., Green W.N.,
RA Phinney B.S., Yates J.R. III, Davis N.G.;
RT "Global analysis of protein palmitoylation in yeast.";
RL Cell 125:1003-1013(2006).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-108, AND DISRUPTION PHENOTYPE.
RX PubMed=16818716; DOI=10.1083/jcb.200602049;
RA Lam K.K.Y., Davey M., Sun B., Roth A.F., Davis N.G., Conibear E.;
RT "Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3.";
RL J. Cell Biol. 174:19-25(2006).
RN [10]
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).
RN [11]
RP MUTAGENESIS OF CYS-108.
RX PubMed=26224664; DOI=10.1074/jbc.m115.651356;
RA Gonzalez Montoro A., Chumpen Ramirez S., Valdez Taubas J.;
RT "The canonical DHHC motif is not absolutely required for the activity of
RT the yeast S-acyltransferases Swf1 and Pfa4.";
RL J. Biol. Chem. 290:22448-22459(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28346351; DOI=10.3390/ijms18040702;
RA Gohlke S., Muthukrishnan S., Merzendorfer H.;
RT "In Vitro and In Vivo Studies on the Structural Organization of Chs3 from
RT Saccharomyces cerevisiae.";
RL Int. J. Mol. Sci. 18:0-0(2017).
CC -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. Palmitoylates several amino acid permeases (PubMed:16751107).
CC Palmitoylates chitin synthase CHS3, which is required for its proper
CC export from the ER (PubMed:16818716, PubMed:28346351). Can palmitoylate
CC RAS2 in vitro (PubMed:12379641). {ECO:0000255|HAMAP-Rule:MF_03199,
CC ECO:0000269|PubMed:12379641, ECO:0000269|PubMed:16751107,
CC ECO:0000269|PubMed:16818716, ECO:0000269|PubMed:28346351}.
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:0000255|HAMAP-Rule:MF_03199};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03199, ECO:0000269|PubMed:15973437}; Multi-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03199,
CC ECO:0000269|PubMed:15973437}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- PTM: Autopalmitoylated. {ECO:0000269|PubMed:16186255,
CC ECO:0000269|PubMed:26224664}.
CC -!- DISRUPTION PHENOTYPE: Leads to the retention of non-palmitoylated CHS3
CC in the endoplasmic reticulum and reduced levels of chitin on the cell
CC wall. {ECO:0000269|PubMed:16818716, ECO:0000269|PubMed:28346351}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
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DR EMBL; U43491; AAC49477.1; -; Genomic_DNA.
DR EMBL; Z74745; CAA99002.1; -; Genomic_DNA.
DR EMBL; AY558023; AAS56349.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10780.1; -; Genomic_DNA.
DR PIR; S61981; S61981.
DR RefSeq; NP_014640.1; NM_001183257.1.
DR AlphaFoldDB; Q12006; -.
DR SMR; Q12006; -.
DR BioGRID; 34401; 137.
DR DIP; DIP-4248N; -.
DR IntAct; Q12006; 3.
DR STRING; 4932.YOL003C; -.
DR iPTMnet; Q12006; -.
DR MaxQB; Q12006; -.
DR PaxDb; Q12006; -.
DR PRIDE; Q12006; -.
DR DNASU; 854159; -.
DR EnsemblFungi; YOL003C_mRNA; YOL003C; YOL003C.
DR GeneID; 854159; -.
DR KEGG; sce:YOL003C; -.
DR SGD; S000005363; PFA4.
DR VEuPathDB; FungiDB:YOL003C; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_0_1; -.
DR InParanoid; Q12006; -.
DR OMA; DQLNLPW; -.
DR BioCyc; YEAST:G3O-33420-MON; -.
DR BRENDA; 2.3.1.225; 984.
DR PRO; PR:Q12006; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12006; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA: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:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
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:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
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..378
FT /note="Palmitoyltransferase PFA4"
FT /id="PRO_0000212972"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 31..40
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 62..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 141..164
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000305|PubMed:16847258"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 186..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000269|PubMed:16847258"
FT DOMAIN 78..128
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 108
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199,
FT ECO:0000305|PubMed:26224664"
FT MUTAGEN 108
FT /note="C->A: Causes mislocalization of chitin synthase CHS3
FT (PubMed:16818716). Reduces, but does not abolish catalytic
FT activity. Lacks autopalmitoylation (PubMed:26224664)."
FT /evidence="ECO:0000269|PubMed:16818716,
FT ECO:0000269|PubMed:26224664"
FT MUTAGEN 108
FT /note="C->R: Reduces, but does not abolish catalytic
FT activity. Lacks autopalmitoylation."
FT /evidence="ECO:0000269|PubMed:26224664"
SQ SEQUENCE 378 AA; 44488 MW; 52156A3BF98F5755 CRC64;
MPVKLRWPWL GIAIPTFLIS FIGYGAHYFI LSNFLSVPKQ ITFEFCLSMI WLSYYLAICT
NPGRPLPNYK PPPDIWRNFC KKCQSYKPER SHHCKTCNQC VLMMDHHCPW TMNCVGFANY
PHFLRFLFWI IVTTSVLFCI QAKRIYFIWQ QRHLPGYFFK KSELIFLTIS SPLNSFVLLT
ITILFLRCLF NQILNGRSQI ESWDMDRLES LFNSGRLTQK LIDNTWRIYP ESRSFQNKKD
AEEHLTKKRP RFDELVNFPY DFDLYTNALL YLGPIHLWLW PYGVPTGDGN NFPKNGISKY
EANSSLEDHI LSLPWPPDGG KTNTVFNHGS STIEMRNESG EQLIRTRLPQ NGRHASREKW
YNDWGESLDD FGVDVDME
