ZDHC6_BOVIN
ID ZDHC6_BOVIN Reviewed; 413 AA.
AC Q2HJ95;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Palmitoyltransferase ZDHHC6 {ECO:0000250|UniProtKB:Q9H6R6};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9H6R6};
DE AltName: Full=Stearoyltransferase ZDHHC6 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9H6R6};
DE AltName: Full=Zinc finger DHHC domain-containing protein 6 {ECO:0000250|UniProtKB:Q9H6R6};
DE Short=DHHC-6 {ECO:0000250|UniProtKB:Q9H6R6};
GN Name=ZDHHC6 {ECO:0000250|UniProtKB:Q9H6R6};
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].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endoplasmic reticulum palmitoyl acyltransferase that mediates
CC palmitoylation of proteins such as AMFR, CALX, ITPR1 and TFRC (By
CC similarity). Palmitoylates calnexin (CALX), which is required for its
CC association with the ribosome-translocon complex and efficient folding
CC of glycosylated proteins (By similarity). Mediates palmitoylation of
CC AMFR, promoting AMFR distribution to the peripheral endoplasmic
CC reticulum (By similarity). Together with SELENOK, palmitoylates ITPR1
CC in immune cells, leading to regulate ITPR1 stability and function (By
CC similarity). Stearoyltransferase that mediates stearoylation of TFRC to
CC inhibit TFRC-mediated activation of the JNK pathway and mitochondrial
CC fragmentation (By similarity). {ECO:0000250|UniProtKB:Q9H6R6}.
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:Q9H6R6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9H6R6};
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:Q9H6R6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q9H6R6};
CC -!- SUBUNIT: Homooligomerizes. Interacts with SELENOK.
CC {ECO:0000250|UniProtKB:Q9H6R6}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H6R6}; Multi-pass membrane protein
CC {ECO:0000255}. Note=When not palmitoylated, accumulates to dot-like
CC structures in the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q9H6R6}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum
CC localization. {ECO:0000250|UniProtKB:Q9H6R6}.
CC -!- PTM: Palmitoylated at 3 different sites by ZDHHC16. The combination of
CC the different palmitoylation events strongly affects the quaternary
CC assembly of ZDHHC6, its localization, stability and function.
CC Palmitoylation at Cys-328 accelerates the turnover of ZDHHC6.
CC Depalmitoylated by LYPLA2. {ECO:0000250|UniProtKB:Q9H6R6}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC113243; AAI13244.1; -; mRNA.
DR RefSeq; NP_001039632.1; NM_001046167.1.
DR AlphaFoldDB; Q2HJ95; -.
DR SMR; Q2HJ95; -.
DR STRING; 9913.ENSBTAP00000008828; -.
DR PaxDb; Q2HJ95; -.
DR PRIDE; Q2HJ95; -.
DR Ensembl; ENSBTAT00000008828; ENSBTAP00000008828; ENSBTAG00000006713.
DR GeneID; 514158; -.
DR KEGG; bta:514158; -.
DR CTD; 64429; -.
DR VEuPathDB; HostDB:ENSBTAG00000006713; -.
DR VGNC; VGNC:37144; ZDHHC6.
DR eggNOG; KOG1314; Eukaryota.
DR GeneTree; ENSGT00940000155642; -.
DR HOGENOM; CLU_044394_1_0_1; -.
DR InParanoid; Q2HJ95; -.
DR OMA; FIYPYDL; -.
DR OrthoDB; 1491968at2759; -.
DR TreeFam; TF320809; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000006713; Expressed in oocyte and 105 other tissues.
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; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:Ensembl.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0140438; P:protein stearoylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; SH3 domain; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..413
FT /note="Palmitoyltransferase ZDHHC6"
FT /id="PRO_0000269227"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..57
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 165..194
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 99..149
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT DOMAIN 313..398
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT MOTIF 410..413
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R6"
FT ACT_SITE 129
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT LIPID 328
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R6"
FT LIPID 329
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R6"
FT LIPID 343
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R6"
SQ SEQUENCE 413 AA; 47531 MW; 76DD8EDA86EE57BE CRC64;
MGTFCSVVKF ENLQELKRLC HWGPIIALGV IAICSAMAMI DSVLWYWPLH TTGGSVNFIM
LINWTVMILY NYFNAMFVGP GFVPLGWKPE NSQDSVYLQY CKVCQAYKAP RSHHCRKCNR
CVMKMDHHCP WINNCCGYQN HASFTLFLLL APLGCIHAAF IFVMTMYTQL YNRLSFGWNT
VKIDMSAARR DPLPIIPFGL AAFAATLFAL GLALGTTIAV GMLFFIQMKI ILRNKTSIES
WIEEKAKDRI QYYQLDEVFV FPYDMGSRWK NFKQVFTWSG VPEGDGLDWP IREGCHQYSL
TIEQLKQKAD KRVRSVRYKV IEDYSGTCCP LNRGIKTFFT SPCTEEPRIR LQKGEFILAT
RGLRYWLYGD KILDDSVLEG VSRIRGWFPR NCVEKCPCDA ETDQAPEGEK KNR
