ID W9Z1T2_9EURO Unreviewed; 432 AA.
AC W9Z1T2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 08-NOV-2023, entry version 45.
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=A1O1_05394 {ECO:0000313|EMBL:EXJ88464.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ88464.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ88464.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ88464.1,
RC ECO:0000313|Proteomes:UP000019484};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia coronata CBS 617.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ88464.1}.
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DR EMBL; AMWN01000004; EXJ88464.1; -; Genomic_DNA.
DR RefSeq; XP_007724470.1; XM_007726280.1.
DR AlphaFoldDB; W9Z1T2; -.
DR STRING; 1182541.W9Z1T2; -.
DR GeneID; 19160269; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_1_1; -.
DR OrthoDB; 6683at2759; -.
DR Proteomes; UP000019484; 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; PTHR22883:SF23; PALMITOYLTRANSFERASE ZDHHC6; 1.
DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03199}; Endoplasmic reticulum {ECO:0000256|HAMAP-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:UP000019484};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 180..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT DOMAIN 91..219
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 379..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199"
SQ SEQUENCE 432 AA; 49698 MW; 17F31DA2DF465592 CRC64;
MDPSTVSKFA LPAVVSLIAF LSYSSQYLFK KIEPGPLSQR EFLQFNALVA GIWVSYFRAC
TTDPGHVPAN WNPEHVGVAD TALPVVKTLA RQRYCRKCSA FKPPRAHHCK VCKRCIPKMD
HHCPWTVNCV SHFTFPHFIR FLFYAVSAMT YLEYFLYLRA EVIWQNRNLP SYLGPSLSQL
VHLFILIIVN SLTLFLVSIT FVRTVWGLGG NVTTIESWEI ERHEQLLRRA RVLGGYLDGP
DGIRIKLTRQ EFPYDIGIWN NIVQGMGTAN ILAWFWPFAA TPRTNGLVFE TNGFEDPGTS
WPPPDPDRMP RLNRAAELQD AFVHDRTKLS AEQEIAAFKE RQQADFQRRP DHYGVQRRKP
FHERFQEDNF VPVMDDYMPQ DDSSGEEGWQ DSGGNRLKDY GVDEDVEFYD EDNLPIAELL
RRKEGRAVTT EA
//