ZDH15_RAT
ID ZDH15_RAT Reviewed; 337 AA.
AC Q2TGJ4;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Palmitoyltransferase ZDHHC15 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000305|PubMed:31189538};
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;
DE Short=DHHC-15;
GN Name=Zdhhc15 {ECO:0000312|RGD:1562075};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen Y., Ye T.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, ACTIVE SITE, AND MUTAGENESIS OF CYS-159.
RX PubMed=31189538; DOI=10.1242/jcs.230052;
RA Shah B.S., Shimell J.J., Bamji S.X.;
RT "Regulation of dendrite morphology and excitatory synapse formation by
RT zDHHC15.";
RL J. Cell Sci. 132:0-0(2019).
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). Palmitoylates IGF2R and SORT1,
CC promoting their partitioning to an endosomal membrane subdomain where
CC they can interact with the retromer cargo-selective complex (By
CC similarity). Thereby, regulates retrograde transport from endosomes to
CC the Golgi apparatus of these lysosomal sorting receptors and plays a
CC role in trafficking of lysosomal proteins (By similarity). In the
CC nervous system, catalyzes the palmitoylation of DLG4/PSD95 and
CC regulates its synaptic clustering and function in synaptogenesis
CC (PubMed:31189538). Could be involved in the differentiation of
CC dopaminergic neurons and the development of the diencephalon (By
CC similarity). Could also catalyze the palmitoylation of GAP43 (By
CC similarity). Could also palmitoylate DNAJC5 and regulate its
CC localization to the Golgi membrane (By similarity). Could also
CC palmitoylate FYN as shown in vitro (By similarity).
CC {ECO:0000250|UniProtKB:F1QXD3, ECO:0000250|UniProtKB:Q8BGJ0,
CC ECO:0000250|UniProtKB:Q96MV8, ECO:0000269|PubMed:31189538}.
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:0000305|PubMed:31189538};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:31189538};
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:0000269|PubMed:31189538}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density
CC {ECO:0000269|PubMed:31189538}.
CC -!- TISSUE SPECIFICITY: In brain, expressed in both excitatory and
CC inhibitory neurons but not expressed by glial cells.
CC {ECO:0000269|PubMed:31189538}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early stages of
CC development at E17 and postnatal day 10 (P10) but significantly reduced
CC in the adult brain. {ECO:0000269|PubMed:31189538}.
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; AY886531; AAX73393.1; -; mRNA.
DR RefSeq; NP_001034190.1; NM_001039101.1.
DR RefSeq; XP_006257207.1; XM_006257145.3.
DR AlphaFoldDB; Q2TGJ4; -.
DR SMR; Q2TGJ4; -.
DR STRING; 10116.ENSRNOP00000003714; -.
DR PaxDb; Q2TGJ4; -.
DR PRIDE; Q2TGJ4; -.
DR Ensembl; ENSRNOT00000003714; ENSRNOP00000003714; ENSRNOG00000002751.
DR GeneID; 317235; -.
DR KEGG; rno:317235; -.
DR UCSC; RGD:1562075; rat.
DR CTD; 158866; -.
DR RGD; 1562075; Zdhhc15.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000158214; -.
DR HOGENOM; CLU_027721_1_1_1; -.
DR InParanoid; Q2TGJ4; -.
DR OMA; AICVLKM; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q2TGJ4; -.
DR TreeFam; TF316044; -.
DR PRO; PR:Q2TGJ4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000002751; Expressed in liver and 16 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:RGD.
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:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0062237; P:protein localization to postsynapse; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISO:RGD.
DR GO; GO:0140450; P:protein targeting to Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IMP:UniProtKB.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISO:RGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Synapse; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..337
FT /note="Palmitoyltransferase ZDHHC15"
FT /id="PRO_0000232504"
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..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:F1QXD3"
FT DOMAIN 129..179
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 293..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067,
FT ECO:0000305|PubMed:31189538"
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"
FT MUTAGEN 159
FT /note="C->S: Loss of function in dendrite development."
FT /evidence="ECO:0000269|PubMed:31189538"
SQ SEQUENCE 337 AA; 39308 MW; 1FAB27E6F863BA05 CRC64;
MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVTVLS PAEKVIYLIL
YHAIFVFFAW TYWKSIFTLP QQPNQKFHLS YTDKERYKNE ERPEVQKQML VDMAKKLPVY
TRTGNGAVRF CDRCHLIKPD RCHHCSVCAM CVLKMDHHCP WVNNCIGFSN YKFFLQFLAY
SVLYCLYIAT TVFSYFIKYW RGELPSVRSK FHVLFLLFVA CMFFVSLVIL FGYHCWLVSR
NKTTLEAFCT PVFTSGPEKN GFNLGFIKNI QQVFGDNKKF WLIPIGSSPG DGHSFPMRSM
NESQNPLLAN EEPWEDNEDE SQDYPEGLSS LAVESET
