ZDHC4_BOVIN
ID ZDHC4_BOVIN Reviewed; 343 AA.
AC Q58DT3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
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:0000250|UniProtKB:Q9NPG8};
DE Short=DHHC-4;
GN Name=ZDHHC4 {ECO:0000250|UniProtKB:Q9NPG8};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; BT021514; AAX46361.1; -; mRNA.
DR RefSeq; NP_001030369.1; NM_001035292.1.
DR AlphaFoldDB; Q58DT3; -.
DR STRING; 9913.ENSBTAP00000012560; -.
DR PaxDb; Q58DT3; -.
DR PRIDE; Q58DT3; -.
DR GeneID; 514338; -.
DR KEGG; bta:514338; -.
DR CTD; 55146; -.
DR eggNOG; KOG1312; Eukaryota.
DR InParanoid; Q58DT3; -.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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_0000212864"
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..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..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; 39710 MW; 6FF48DFEAE05A22F CRC64;
MDFLVLFLLY LALVLLGFVM ICIGSKTHYL QGLISRGAQV FSYIIPECLQ RAMLSVLHYL
FHTRNYTFVV LHLILQGMVY TEYTWEIFGL CQQLEFSLYY LFLPYLLLIV NLLFFTLSCV
TNPGTITKAN ELLFLQVYEF DGVMFPKNVR CPTCDLRKPA RSKHCSVCNR CVHRFDHHCV
WVNNCIGAWN TRYFLSYLFT LTASAATMAV VSTVFLVRLV VMSDVYLQTY VDDLGHLQVV
DTVFLVQYLF LTFPRIVFLV GFVVVLSFLL GGYLCFCLYL AATNQTTNEW YKGDRAWCQH
CPHVARPPAA EPQAYRNIHS HGLWSNLREI FLPATACYER KEK
