ZDH15_XENLA
ID ZDH15_XENLA Reviewed; 338 AA.
AC Q5FWL7;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Palmitoyltransferase ZDHHC15;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:F1QXD3};
DE AltName: Full=Acyltransferase ZDHHC15 {ECO:0000250|UniProtKB:Q8BGJ0};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q8BGJ0};
DE AltName: Full=Zinc finger DHHC domain-containing protein 15 homolog;
DE Short=DHHC-15;
GN Name=zdhhc15;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates (By similarity). Has no stringent fatty
CC acid selectivity and in addition to palmitate can also transfer onto
CC target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). May thereby regulate target proteins
CC association and localization to membranes (By similarity). In the
CC nervous system, probably catalyzes the palmitoylation of synaptic
CC proteins and is involved in the differentiation of dopaminergic neurons
CC and the development of the diencephalon (By similarity).
CC {ECO:0000250|UniProtKB:F1QXD3, ECO:0000250|UniProtKB:Q8BGJ0,
CC ECO:0000250|UniProtKB:Q96MV8}.
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:0000250|UniProtKB:F1QXD3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:F1QXD3}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q2TGJ4}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8BGJ0}.
CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000250|UniProtKB:F1QXD3}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC089290; AAH89290.1; -; mRNA.
DR RefSeq; NP_001089258.1; NM_001095789.1.
DR AlphaFoldDB; Q5FWL7; -.
DR SMR; Q5FWL7; -.
DR DNASU; 734305; -.
DR GeneID; 734305; -.
DR KEGG; xla:734305; -.
DR CTD; 734305; -.
DR Xenbase; XB-GENE-948860; zdhhc15.L.
DR OrthoDB; 1491968at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 734305; Expressed in blastula and 18 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0140450; P:protein targeting to Golgi apparatus; ISS:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Synapse; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..338
FT /note="Palmitoyltransferase ZDHHC15"
FT /id="PRO_0000212895"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TOPO_DOM 42..56
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TOPO_DOM 78..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TOPO_DOM 194..210
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TRANSMEM 211..234
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT TOPO_DOM 235..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT DOMAIN 129..179
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 159
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
SQ SEQUENCE 338 AA; 39440 MW; 3C10219B0C59015B CRC64;
MLAGCRVALP RGLRCCQRVL SWVPVVIISL VVLWSYYAYV WELCLVTVTN PAEKAAYLLI
FHTVFLLFIW TYWKAIFTPP KQPTKKFLLP YAEKERYDNE ERPEAQKQIV AEFARKLPVY
TRTGSGATRF CDTCQMVKPD RCHHCSVCGM CVLKMDHHCP WVNNCIGYSN YKFFLLFLAY
AMLYCLYIGC TVFQYFILYW TDTLSNGRAK FHVLFLLFVA LMFFISLMFL FGYHCWLVSL
NRTTLEAFST PVFQSGPDKN GFHLGIRRNL EQVFGKERKL WLIPVFTSLG DGFTYPMRMA
CESRNPLLAA ENQWEDDLTD EESQAYCETS HITVHIEK
