ID A0EH42_PARTE Unreviewed; 362 AA.
AC A0EH42;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=GSPATT00026957001 {ECO:0000313|EMBL:CAK94633.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK94633.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK94633.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK94633.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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|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.
CC {ECO:0000256|RuleBase:RU079119}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU079119}.
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DR EMBL; CT868678; CAK94633.1; -; Genomic_DNA.
DR RefSeq; XP_001462006.1; XM_001461969.1.
DR AlphaFoldDB; A0EH42; -.
DR STRING; 5888.A0EH42; -.
DR EnsemblProtists; CAK94633; CAK94633; GSPATT00026957001.
DR GeneID; 5047791; -.
DR KEGG; ptm:GSPATT00026957001; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_063994_0_0_1; -.
DR InParanoid; A0EH42; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR22883:SF43; PALMITOYLTRANSFERASE APP; 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}; Membrane {ECO:0000256|RuleBase:RU079119};
KW Reference proteome {ECO:0000313|Proteomes:UP000000600};
KW Transferase {ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 187..314
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 74..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 42889 MW; EBC0DB9C83D7D3A6 CRC64;
MFQFQAIPSN ARTYPIIEQQ NVVQEQKSEN EQELPCEASI DVNQLPEFDI NQIPSFTKTP
DKYPSPIKGQ KAFQDFDSKQ PSTQAFSITS QNEHENIVPN TNNDEQKEAD VQKSEGKKTQ
QKGMSEEKRK NNKIEPQLSI QVHSVQNEYI SEQYSPGMSE RNKITQSTRA VNKVFIEKRF
NFLEYIRYCP ICSIDQLARA KHCQSCNKCV ACYDHHCPWA GNCIGERNRC VYYWFPSILD
SRNLLCLYQR IKFQQTSFQT LQNLEFDHYN PLLKFFSIYF LTNTIFFGFL VTRLLCFQTF
LSFQNLTTWE FYSWNKISYL QELQRKNGSP FSQGWKRNLQ TYCRFNIPQL TIWEYNPERV
YK
//
