ZDHC4_DANRE
ID ZDHC4_DANRE Reviewed; 345 AA.
AC F1QAM1; Q7T323;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
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:0000305|PubMed:27235108};
GN Name=zdhhc4 {ECO:0000303|PubMed:27235108};
GN Synonyms=dhhc4 {ECO:0000303|PubMed:26056731};
GN ORFNames=zgc:64155 {ECO:0000312|EMBL:AAH53285.2};
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=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2003) 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).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto protein substrates. {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 -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at 6 hpf and is stable from 7.5 hpf to
CC 24 hpf. {ECO:0000269|PubMed:26056731, ECO:0000269|PubMed:27235108}.
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:0000255|RuleBase:RU079119}.
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DR EMBL; CT009714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053285; AAH53285.2; -; mRNA.
DR RefSeq; NP_956343.2; NM_200049.2.
DR AlphaFoldDB; F1QAM1; -.
DR STRING; 7955.ENSDARP00000112009; -.
DR PaxDb; F1QAM1; -.
DR Ensembl; ENSDART00000122858; ENSDARP00000112009; ENSDARG00000045159.
DR Ensembl; ENSDART00000193262; ENSDARP00000150172; ENSDARG00000045159.
DR GeneID; 561817; -.
DR KEGG; dre:561817; -.
DR CTD; 55146; -.
DR ZFIN; ZDB-GENE-030131-9031; zdhhc4.
DR eggNOG; KOG1312; Eukaryota.
DR GeneTree; ENSGT00920000149163; -.
DR InParanoid; F1QAM1; -.
DR OMA; QHCPLVA; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; F1QAM1; -.
DR TreeFam; TF330931; -.
DR PRO; PR:F1QAM1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000045159; Expressed in early embryo and 21 other tissues.
DR ExpressionAtlas; F1QAM1; baseline and differential.
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: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..345
FT /note="Palmitoyltransferase ZDHHC4"
FT /id="PRO_0000450100"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..100
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..257
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 151..201
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOTIF 342..345
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NPG8"
FT ACT_SITE 181
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 46
FT /note="C -> W (in Ref. 2; AAH53285)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> I (in Ref. 2; AAH53285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39888 MW; AF602450C3A561B5 CRC64;
MDFLTLFGIY VAVVLTCIAL VCKYSGHQQT PLGQLVGAFT RIVSPCIPQW LQSICYRTMH
RLFHQRNNFF LYLHLLLEVV VYGEFTYEVF GFCLDMGSSS LSLCVPYILL ALKSCLFYLC
CSRDPGTLTK SNLSAHLKIY QYDEKLFQQG MKCSTCQLIK PARSKHCRVC NRCVQRFDHH
CVWVNNCIGA QNTRYFMLYL LSVCAMAGNI AVLTTDMLLQ TVLRTGLLHA HYIDEQGIQQ
PAGPLFIIQH LFLTFPRIVF MLGFLVFVFF LLAGYCLFHF YLVLVNQTSN EWFKAKGHNC
QHCHPYSGHN CRTSYNPFRG FYHRGILKNI GEIFWPLRPV QKKEN
