ID A0A0D2BAP7_9EURO Unreviewed; 424 AA.
AC A0A0D2BAP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=PV08_05714 {ECO:0000313|EMBL:KIW15665.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW15665.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW15665.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW15665.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs.
CC Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic
CC end of their transmembrane domain. May have a role in the cellular
CC quality control of transmembrane domain-containing proteins.
CC {ECO:0000256|ARBA:ARBA00043903}.
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|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. 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|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. SWF1
CC subfamily. {ECO:0000256|ARBA:ARBA00038463}.
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DR EMBL; KN847495; KIW15665.1; -; Genomic_DNA.
DR RefSeq; XP_016235881.1; XM_016380054.1.
DR AlphaFoldDB; A0A0D2BAP7; -.
DR STRING; 91928.A0A0D2BAP7; -.
DR GeneID; 27332797; -.
DR VEuPathDB; FungiDB:PV08_05714; -.
DR HOGENOM; CLU_042181_2_1_1; -.
DR OrthoDB; 5480099at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR22883:SF286; PALMITOYLTRANSFERASE ZDHHC4; 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,
KW ECO:0000256|RuleBase:RU079119};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 197..222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 153..305
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 368..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 48646 MW; 89C00B6E70DD0ABD CRC64;
MGLIRTIALV VLTISFIVFI ALFGRLPAFR RTPIAFLHQL LWRHIPNGFI AVDERLTGRR
ISRSLARTGN YLMNEKHPLV LIFFLGLQVI GEAMFVPAAW DRLATSQKIV IPCLIAGPMV
FLYLSATTSS NVTPENHAEC IRAYPYDFAL FHPGYFCSTC RFAKPARSKH CPICKACVQK
QDHHCIWINN CVGRNNYLWF NLLIVATAVL LAYGARLGYV LLDARLQERL VPAALTRGSA
TAKRWSTALT WGEYWQCWAW AISVEWRIGS IMMLTILSFP LATAFLVYHV YLVWAGMTTN
ESAKWSDWKE DILDDLVYRA RIAELRETYP KLPDDVEPRD EDIKSPWPRG ARAKWWLVRM
VDGRQPTLRK NRENGKGVGE RGAEDEGNEV PDERWTKVHS LREVDNVYDL GFWSNLKDSI
LNRD
//
