PFA3_CANAL
ID PFA3_CANAL Reviewed; 377 AA.
AC Q5ADN9; A0A1D8PKN0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Palmitoyltransferase PFA3;
DE EC=2.3.1.225;
DE AltName: Full=Protein fatty acyltransferase 3;
GN Name=PFA3; OrderedLocusNames=CAALFM_C306990WA;
GN ORFNames=CaO19.14094, CaO19.6802;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 (By 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: Vacuole membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017625; AOW28702.1; -; Genomic_DNA.
DR RefSeq; XP_719897.2; XM_714804.2.
DR AlphaFoldDB; Q5ADN9; -.
DR SMR; Q5ADN9; -.
DR STRING; 237561.Q5ADN9; -.
DR GeneID; 3638521; -.
DR KEGG; cal:CAALFM_C306990WA; -.
DR CGD; CAL0000175769; orf19.14094.
DR VEuPathDB; FungiDB:C3_06990W_A; -.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_0_0_1; -.
DR InParanoid; Q5ADN9; -.
DR OMA; DFPTRSD; -.
DR OrthoDB; 1491968at2759; -.
DR PRO; PR:Q5ADN9; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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: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:0006612; P:protein targeting to membrane; IBA:GO_Central.
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; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..377
FT /note="Palmitoyltransferase PFA3"
FT /id="PRO_0000212951"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..62
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..222
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 138..188
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 168
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 377 AA; 43798 MW; 8E8CDCEFC2D605F5 CRC64;
MATNNNNNNG NPILRSLETS CCFLATLFPK VFCTLVLTWS LYVLLFIIPN YIKSSLNSTI
LNIIGITLYV LCIISYYKII LIGPGSPLDY PELRINDLNR MINENPYNNN NNDEEPGDLP
PESMIIHTMK VNGNQGYRYC TKCSVWKPDR SHHCSSSGKC ILKMDHYCPW FSTCIGFHNY
KFFIQFLSYV AIYCWFLFII SGKILYNFIT EGLFEDEILS LNLVAVLILS FAFAIAVSVF
AMFSIYLCCK NLTTIEFQEK RWNYRGQAND ERFNYEFDNN GKRKKINTNI FDLGIMENWK
SVMGPNWITW ILPITVTVTA NTKSMISQDE FNNGVNFKVN EEIYAKYLHN AELQQQLNQQ
LSSYKDRLRR ERQANIV
