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   27-MAR-2024, entry version 168.
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; 13.
DR   DIP; DIP-4833N; -.
DR   IntAct; P42836; 2.
DR   MINT; P42836; -.
DR   STRING; 4932.YNL326C; -.
DR   iPTMnet; P42836; -.
DR   PaxDb; 4932-YNL326C; -.
DR   PeptideAtlas; P42836; -.
DR   DNASU; 855390; -.
DR   EnsemblFungi; YNL326C_mRNA; YNL326C; YNL326C.
DR   GeneID; 855390; -.
DR   KEGG; sce:YNL326C; -.
DR   AGR; SGD:S000005270; -.
DR   SGD; S000005270; PFA3.
DR   VEuPathDB; FungiDB:YNL326C; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_027721_0_0_1; -.
DR   InParanoid; P42836; -.
DR   OMA; CFVVMHI; -.
DR   OrthoDB; 6683at2759; -.
DR   BioCyc; YEAST:G3O-33310-MONOMER; -.
DR   BRENDA; 2.3.1.225; 984.
DR   BioGRID-ORCS; 855390; 2 hits in 10 CRISPR screens.
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: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: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   PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR   PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
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
//