PFA4_CANAL
ID PFA4_CANAL Reviewed; 446 AA.
AC Q5AGV7; A0A1D8PQV4; Q3MPJ2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
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};
GN OrderedLocusNames=CAALFM_C701480WA;
GN ORFNames=CaJ7.0163, CaO19.13934, CaO19.6581;
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=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [2]
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 [3]
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 [4]
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: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000255|HAMAP-Rule:MF_03199}.
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}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|HAMAP-Rule:MF_03199}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
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DR EMBL; AP006852; BAE44668.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30515.1; -; Genomic_DNA.
DR RefSeq; XP_721417.1; XM_716324.1.
DR AlphaFoldDB; Q5AGV7; -.
DR SMR; Q5AGV7; -.
DR STRING; 237561.Q5AGV7; -.
DR PRIDE; Q5AGV7; -.
DR GeneID; 3636956; -.
DR KEGG; cal:CAALFM_C701480WA; -.
DR CGD; CAL0000201029; orf19.13934.
DR VEuPathDB; FungiDB:C7_01480W_A; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_0_1; -.
DR InParanoid; Q5AGV7; -.
DR OMA; DQLNLPW; -.
DR OrthoDB; 1491968at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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: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 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 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..446
FT /note="Palmitoyltransferase PFA4"
FT /id="PRO_0000212962"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 30..40
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 62..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 183..201
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 223..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT DOMAIN 114..164
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 144
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ SEQUENCE 446 AA; 52757 MW; 3081431C4134E7F5 CRC64;
MAVQLKWPIL GVIIPCIIIF SLSYGSHYFI LRHHLTMKQQ LIYEFYVTMI WISYLLAIYT
NPGRVPKNYK PSLASSTRIE QTEDDSDGLG LESREDETLI REEPISGDRC EWIRYCKKCN
NYKPPRSHHC KICQQCVLQM DHHCPWTLNC VGNNNLPHFM RFLGWIIWGT GYLMIQLIKL
IINYYENSNM PHYLFNKTEL VAIIAITPLN FFVFASILVL FIRCLINICK GMTQIEIWEW
ERLELQWSSK RLWRLIRFNY GRLHKGKPFP ELNTWTNTTN NVNYNDNDDD GDEDVELINL
ATNNNEDSTI VPQNFTIDDL IFPYNLGIWK NLVNALGYPY MWLIPFGKPK SNGYQPQISQ
DYKQDDQLNL PWPPDGIRQK EIEINVLQQQ GYQRDREEED EEELRSIRNY QELRRRLDPR
LNVQRSDFIN DMGEGLTDFG VDEDSD
