PFA3_YEAST
ID PFA3_YEAST Reviewed; 336 AA.
AC P42836; D6W0M1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Palmitoyltransferase PFA3;
DE EC=2.3.1.225 {ECO:0000269|PubMed:16186255};
DE AltName: Full=Protein fatty acyltransferase 3;
GN Name=PFA3; OrderedLocusNames=YNL326C; ORFNames=N0325;
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].
RC STRAIN=S288c / FY1676;
RX PubMed=7645347; DOI=10.1002/yea.320110606;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 15.4 kb fragment of yeast chromosome XIV
RT identifies the RPD3, PAS8 and KRE1 loci, five new open reading frames.";
RL Yeast 11:567-572(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-134, AND SUBCELLULAR
RP LOCATION.
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 [7]
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 specific for VAC8. Palmitoylates VAC8 at
CC one or more of its N-terminal cysteine residues, which is required for
CC its proper membrane localization. {ECO:0000269|PubMed:16186255}.
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:0000269|PubMed:16186255};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16186255}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16186255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC -!- PTM: Autopalmitoylated. {ECO:0000269|PubMed:16186255}.
CC -!- MISCELLANEOUS: Present with 2133 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC subfamily. {ECO:0000305}.
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DR EMBL; Z46259; CAA86372.1; -; Genomic_DNA.
DR EMBL; Z71602; CAA96258.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10237.1; -; Genomic_DNA.
DR PIR; S55863; S55863.
DR RefSeq; NP_014073.1; NM_001183164.1.
DR AlphaFoldDB; P42836; -.
DR SMR; P42836; -.
DR BioGRID; 35515; 11.
DR DIP; DIP-4833N; -.
DR IntAct; P42836; 2.
DR MINT; P42836; -.
DR STRING; 4932.YNL326C; -.
DR iPTMnet; P42836; -.
DR PaxDb; P42836; -.
DR PRIDE; P42836; -.
DR DNASU; 855390; -.
DR EnsemblFungi; YNL326C_mRNA; YNL326C; YNL326C.
DR GeneID; 855390; -.
DR KEGG; sce:YNL326C; -.
DR SGD; S000005270; PFA3.
DR VEuPathDB; FungiDB:YNL326C; -.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_0_0_1; -.
DR InParanoid; P42836; -.
DR OMA; DFPTRSD; -.
DR BioCyc; YEAST:G3O-33310-MON; -.
DR BRENDA; 2.3.1.225; 984.
DR PRO; PR:P42836; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42836; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
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:0005774; C:vacuolar membrane; IDA:UniProtKB.
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 GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:SGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..336
FT /note="Palmitoyltransferase PFA3"
FT /id="PRO_0000212959"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..37
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..188
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MUTAGEN 134
FT /note="C->S: Abolishes autopalmitoylation and VAC8
FT palmitoylation."
FT /evidence="ECO:0000269|PubMed:16186255"
SQ SEQUENCE 336 AA; 39184 MW; D36BF37DEC5D3983 CRC64;
MNDRLSLTSL FPRCLTTCLY IWTAYITLTR IHQIPRWFLA LTIVPTLAVA LYTYYKVIAR
GPGSPLDFPD LLVHDLKAAE NGLELPPEYM SKRCLTLKHD GRFRVCQVCH VWKPDRCHHC
SSCDVCILKM DHHCPWFAEC TGFRNQKFFI QFLMYTTLYA FLVLIYTCYE LGTWFNSGSF
NRELIDFHLL GVALLAVAVF ISVLAFTCFS IYQVCKNQTT IEVHGMRRYR RDLEILNDSY
GTNEHLENIF DLGSSMANWQ DIMGTSWLEW ILPIETFKYK KSKHTKDEKG LYFNVRPQVQ
DRLLSSRCLE DQLLRRVTPR PSLEADRASV EIIDAN
