ZDH24_DANRE
ID ZDH24_DANRE Reviewed; 295 AA.
AC F1QGD2; A7YYE7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable palmitoyltransferase ZDHHC24;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q6UX98};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 24 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 24 {ECO:0000303|PubMed:27235108, ECO:0000312|ZFIN:ZDB-GENE-040718-8};
GN Name=zdhhc24 {ECO:0000303|PubMed:27235108,
GN ECO:0000312|ZFIN:ZDB-GENE-040718-8};
GN Synonyms=dhhc24 {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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2007) 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: Probable palmitoyltransferase that could catalyze the
CC addition of palmitate onto various protein substrates. {ECO:0000305}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at 2.75 hpf and remains constant until
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 -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; FP016208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC152631; AAI52632.1; -; mRNA.
DR AlphaFoldDB; F1QGD2; -.
DR SMR; F1QGD2; -.
DR STRING; 7955.ENSDARP00000097146; -.
DR PaxDb; F1QGD2; -.
DR Ensembl; ENSDART00000168546; ENSDARP00000132373; ENSDARG00000105134.
DR Ensembl; ENSDART00000189778; ENSDARP00000153443; ENSDARG00000105134.
DR ZFIN; ZDB-GENE-040718-8; zdhhc24.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000164006; -.
DR HOGENOM; CLU_027721_5_2_1; -.
DR OMA; RMHLTWL; -.
DR PhylomeDB; F1QGD2; -.
DR TreeFam; TF319523; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000105134; Expressed in early embryo and 23 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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: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; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Probable palmitoyltransferase ZDHHC24"
FT /id="PRO_0000451132"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..60
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..176
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..295
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 102..152
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 132
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 52
FT /note="T -> S (in Ref. 2; AAI52632)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="S -> P (in Ref. 2; AAI52632)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="V -> I (in Ref. 2; AAI52632)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33721 MW; A89FB24B75B39BF9 CRC64;
MTSFMSRVWC KVESTGRQLP IVLNAVLVFS ITAEVSYLVL VEAPFEPEQK KTDWSTIWTG
LHLFAQYFML GNITWNASLF VKTNPSIRGV FLGGDTLGQG WRYCYNCETH TPPRCSHCYD
CNVCVLRRDH HCVFFGQCVG FHNYRYFLTC LLFMWAGLLY AVVMNAEVFI FILKEGVTFH
SVMLLLVPWI MLVSGQVTTR AFAFAFIADT CVVGFLLVAA FLFFHVALML RGQTTREWYS
TRRPYSLGTM ANIRECLGKN WYFCWLCPLI PSPLPGDGIN FKVTASLEPK KQAVH
