ZDHC6_DANRE
ID ZDHC6_DANRE Reviewed; 412 AA.
AC E7F6D7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Palmitoyltransferase ZDHHC6 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9H6R6};
DE AltName: Full=DHHC domain-containing protein 6 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Stearoyltransferase ZDHHC6 {ECO:0000250|UniProtKB:Q9H6R6};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q9H6R6};
DE AltName: Full=Zinc finger DHHC domain-containing protein 6 {ECO:0000305|PubMed:27235108};
GN Name=zdhhc6 {ECO:0000303|PubMed:27235108,
GN ECO:0000312|ZFIN:ZDB-GENE-030131-3189};
GN Synonyms=dhhc6 {ECO:0000303|PubMed:26056731};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DEVELOPMENTAL STAGE.
RX PubMed=26056731; DOI=10.1016/j.ntt.2015.06.001;
RA Wang C., Chen X., Shi W., Wang F., Du Z., Li X., Yao Y., Liu T., Shao T.,
RA Li G., Hao A.;
RT "2-Bromopalmitate impairs neural stem/progenitor cell proliferation,
RT promotes cell apoptosis and induces malformation in zebrafish embryonic
RT brain.";
RL Neurotoxicol. Teratol. 50:53-63(2015).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=27235108; DOI=10.1016/j.bbrc.2016.05.074;
RA Du Z., Chen X., Li X., He K., Ji S., Shi W., Hao A.;
RT "Protein palmitoylation activate zygotic gene expression during the
RT maternal-to-zygotic transition.";
RL Biochem. Biophys. Res. Commun. 475:194-201(2016).
CC -!- FUNCTION: Endoplasmic reticulum palmitoyl acyltransferase that probably
CC catalyzes the addition of palmitate onto various protein substrates and
CC is involved in a variety of cellular processes (By similarity). Could
CC also function as a stearoyltransferase (By similarity).
CC {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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9H6R6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at 6 hpf and increases from 7.5 hpf to
CC 24 hpf. {ECO:0000269|PubMed:26056731, ECO:0000269|PubMed:27235108}.
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 -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CU459185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001191086.1; NM_001204157.1.
DR RefSeq; XP_005156380.1; XM_005156323.3.
DR AlphaFoldDB; E7F6D7; -.
DR STRING; 7955.ENSDARP00000127320; -.
DR PaxDb; E7F6D7; -.
DR Ensembl; ENSDART00000153179; ENSDARP00000127320; ENSDARG00000075721.
DR GeneID; 324468; -.
DR KEGG; dre:324468; -.
DR CTD; 64429; -.
DR ZFIN; ZDB-GENE-030131-3189; zdhhc6.
DR eggNOG; KOG1314; Eukaryota.
DR GeneTree; ENSGT00940000155642; -.
DR HOGENOM; CLU_044394_1_0_1; -.
DR InParanoid; E7F6D7; -.
DR OMA; FIYPYDL; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; E7F6D7; -.
DR TreeFam; TF320809; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000075721; Expressed in intestine and 27 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
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 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..412
FT /note="Palmitoyltransferase ZDHHC6"
FT /id="PRO_0000451039"
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..205
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..412
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 409..412
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q9H6R6"
FT ACT_SITE 129
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
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 412 AA; 47805 MW; 1F052D08FB0A3946 CRC64;
MNILSAIIVF ENLHEVKRLF HWGPIIALTV IGVCSSMAIL DSIIWYWPLD TTGGSINFIM
LINWTVLILY NYFNAMFVGP GYIPLEWKPE KQQDIMYLQF CRLCQGYKAP RSHHCRKCNR
CVMKMDHHCP WINNCCGHLN HAYFTSFLLL APLGCIHAAL IFIMTMYTQL YDRISFGWSS
VKIDMSAARH IHHPIMPFSI AAFAATLFAL GLALGTTIAV GMLFFIQMKV ILRNRTSIEA
WIEEKAKDRI QYYQTGEDFI FPYDLGSRWE NFKQVFTWSG APMGDGIEWP VHEKCDQYTL
TIEQLKQKHD KRQRSVEYRV VEEYNGACCP LGKGLNTFFR TPCTEEPRIK LTKGETIFAT
RGTKWWMYGD KVLNEEQAKA GVRIRGWFPR RCVEKCLYDS ANNSTSEEKK EQ
