DHC3A_DANRE
ID DHC3A_DANRE Reviewed; 316 AA.
AC F1RE57; Q6DH92;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Palmitoyltransferase ZDHHC3-A {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000305|PubMed:28167757};
DE AltName: Full=Acyltransferase ZDHHC3A {ECO:0000305|PubMed:28167757};
DE EC=2.3.1.- {ECO:0000305|PubMed:28167757};
DE AltName: Full=Zinc finger DHHC domain-containing protein 3 {ECO:0000305|PubMed:27235108};
GN Name=zdhhc3a;
GN Synonyms=dhhc3 {ECO:0000303|PubMed:26056731},
GN zdhhc3 {ECO:0000303|PubMed:27235108};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=28167757; DOI=10.1073/pnas.1612254114;
RA Greaves J., Munro K.R., Davidson S.C., Riviere M., Wojno J., Smith T.K.,
RA Tomkinson N.C., Chamberlain L.H.;
RT "Molecular basis of fatty acid selectivity in the zDHHC family of S-
RT acyltransferases revealed by click chemistry.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1365-E1374(2017).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates and regulates
CC their association with membranes (Probable). 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 (Probable). {ECO:0000305|PubMed:28167757}.
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:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:28167757};
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:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000305|PubMed:28167757};
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:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000305|PubMed:28167757};
CC -!- SUBUNIT: Monomer. Homooligomers. The monomeric form has a higher
CC catalytic activity. Forms heterooligomers with zdhhc7.
CC {ECO:0000250|UniProtKB:Q8R173}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8R173}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression is detected early during development at the sphere stage but
CC decreases after 7.5 hpf. {ECO:0000269|PubMed:26056731,
CC ECO:0000269|PubMed:27235108}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8R173}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR925805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC076087; AAH76087.1; -; mRNA.
DR RefSeq; NP_001002725.1; NM_001002725.1.
DR AlphaFoldDB; F1RE57; -.
DR SMR; F1RE57; -.
DR STRING; 7955.ENSDARP00000025104; -.
DR PaxDb; F1RE57; -.
DR Ensembl; ENSDART00000017017; ENSDARP00000025104; ENSDARG00000010981.
DR GeneID; 436998; -.
DR KEGG; dre:436998; -.
DR CTD; 436998; -.
DR ZFIN; ZDB-GENE-040718-484; zdhhc3a.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000155721; -.
DR InParanoid; F1RE57; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; F1RE57; -.
DR TreeFam; TF319798; -.
DR PRO; PR:F1RE57; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000010981; Expressed in mature ovarian follicle and 23 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IC:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IC:UniProtKB.
DR GO; GO:0016417; F:S-acyltransferase activity; IDA:ZFIN.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..316
FT /note="Palmitoyltransferase ZDHHC3-A"
FT /id="PRO_0000449531"
FT TOPO_DOM 1..45
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..70
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..212
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 124..175
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 155
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT LIPID 144
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8R173"
FT CONFLICT 32
FT /note="S -> N (in Ref. 2; AAH76087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 316 AA; 35892 MW; 103F2BED563EE62F CRC64;
MRSPVPRFRD VERQASGLQP PQCLPSCHER QSSMWFIKDA CGIVCAIITW FLVFFAEFVV
LFVMLIPSKN LTYSLVNGTL FNSLAFLALA SHFRAMCTDP GAVPKGNATK EYIESLQLKP
GQVVYKCPKC CSIKPDRAHH CSVCKRCIRK MDHHCPWVNN CVGENNQKYF VLFTMYICLI
SLHSLVMVVF HFLNCFEDDW TKCSTFSPPA TVILLILLCF EGLLFLIFTS VMFGTQVHSI
CTDETGIEKL KREDPTWEKT QCWEGMKSAF GGPLSVTWFS PFTDLSCQKD DSSPVPMFPQ
GEIIEEDVIE IPLEPH
