ZDHC4_RAT
ID ZDHC4_RAT Reviewed; 343 AA.
AC Q5FVR1; Q2TGK2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Palmitoyltransferase ZDHHC4 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9NPG8};
DE AltName: Full=Zinc finger DHHC domain-containing protein 4 {ECO:0000312|RGD:1308389};
DE Short=DHHC-4;
GN Name=Zdhhc4 {ECO:0000312|RGD:1308389};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto protein substrates including the D(2) dopamine receptor
CC DRD2. {ECO:0000250|UniProtKB:Q9NPG8}.
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:Q9NPG8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9NPG8};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NPG8}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NPG8};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9NPG8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum
CC localization. {ECO:0000250|UniProtKB:Q9NPG8}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY886523; AAX73385.1; -; mRNA.
DR EMBL; BC089831; AAH89831.1; -; mRNA.
DR RefSeq; NP_001013141.1; NM_001013123.1.
DR AlphaFoldDB; Q5FVR1; -.
DR STRING; 10116.ENSRNOP00000001447; -.
DR PhosphoSitePlus; Q5FVR1; -.
DR PaxDb; Q5FVR1; -.
DR GeneID; 304291; -.
DR KEGG; rno:304291; -.
DR CTD; 55146; -.
DR RGD; 1308389; Zdhhc4.
DR eggNOG; KOG1312; Eukaryota.
DR InParanoid; Q5FVR1; -.
DR PhylomeDB; Q5FVR1; -.
DR PRO; PR:Q5FVR1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cell membrane; Endoplasmic reticulum; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Palmitoyltransferase ZDHHC4"
FT /id="PRO_0000212867"
FT TOPO_DOM 1..2
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..95
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..255
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 149..199
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOTIF 340..343
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NPG8"
FT ACT_SITE 179
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 343 AA; 39397 MW; 429AF110422B217E CRC64;
MDFLVLFSFY LAFLLICVIM ICIFTKSQRL KAVVLGGAQV CARVTPQCFQ RAVQTLLHQL
FHTRHPAFLA LHLLLQGLVY AEYTYEVFSY CRELEFSLPC LLLPYVLLSV NLVFFTLTCS
TNPGTITKTN VLLLLQVYEF DEVMFPKNSR CSTCDLRKPA RSKHCRVCDR CVHRFDHHCV
WVNNCIGAWN TGYFLIYLLT LTASAATIAI LSAAFLLRLV AVSNLYQETY LDDLGRFQAV
DTGFLIQHLF LAFPRIIFLL GFVIVLSLLL AGYLCFALYL AATNQTTNEW YRGDWAWCQH
WPLVAWSPSA EPQIHQNIYS HGLWSNLQEV FIPATPSYKK KKR
