ID M9MFZ6_PSEA3 Unreviewed; 568 AA.
AC M9MFZ6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199};
DE Short=PAT {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN ORFNames=PANT_22c00103 {ECO:0000313|EMBL:GAC76593.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC76593.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
CC -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000256|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:0000256|ARBA:ARBA00001870,
CC ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03199}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03199}.
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DR EMBL; DF196788; GAC76593.1; -; Genomic_DNA.
DR AlphaFoldDB; M9MFZ6; -.
DR OrthoDB; 6683at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF19; S-ACYLTRANSFERASE; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_03199};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 86..112
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 118..142
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 281..307
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT DOMAIN 194..321
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..538
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 226
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199"
SQ SEQUENCE 568 AA; 64115 MW; 619A1AE186DA1F2A CRC64;
MSAASPRAGP PLGRADRRQD ADDDDYPSSE SDAEIDVHAP PAESQRLLAA DEDANATQDR
AGPSIPAQAA RAHGRKRQTP LKWTEIIWVS CTLSLIAVLG YSSQLCIMLP YYNKTPSFSA
QALAAVLVPF NLGLLGIFYN YYLCVTTDPG SVPHGYQPEW SALEPVASPH HHASPHADSG
EMEPSLELKQ AIYRPRYCKT CSAYKPPRSH HCKTCERCVL RMDHHCPWLA NCVGHHNYAH
FLRFLFCVDV TCAYHLCMVS ARVLDRFNAY TYWREPSTRE LIWLVVNYAL CLPVLLLVGV
FSAYHFYCTA INQTTIESWE KDRTATMIRR GRIRRIKYPY HLGVARNVRC VLGDNVLTWC
LPGQAAGGDG LKFPVAPGLG KWSSGVRAWV RSSRSWHWHV QTSQQDEVHL SPLPHKQVDD
ETYVDPDLEA SVLHRLRWEN WHRQAMRHRS AQYRWPPKDP AKTIHHTAPP AVYEQSSGWY
GEPAAPHLFP PGASSNSPFT YGDGFNPALR PSNQTYTQSE VESDVESDVE SDVEPDVDDD
HADQLRRRVA VRRGSEGYEV RPVAQWSI
//
