ZD23B_DANRE
ID ZD23B_DANRE Reviewed; 428 AA.
AC F1QX91; Q6AXL7;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Palmitoyltransferase ZDHHC23-B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IYP9};
DE AltName: Full=Zinc finger DHHC domain-containing protein 23-B {ECO:0000305};
GN Name=zdhhc23b {ECO:0000312|ZFIN:ZDB-GENE-040808-13};
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 (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates and be involved in a variety
CC of cellular processes. {ECO:0000250|UniProtKB:Q8IYP9}.
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:Q8IYP9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8IYP9};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IYP9}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q8IYP9}; Multi-pass membrane protein
CC {ECO:0000255}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH79487.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CU929332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079487; AAH79487.1; ALT_INIT; mRNA.
DR RefSeq; NP_001003757.1; NM_001003757.1.
DR AlphaFoldDB; F1QX91; -.
DR STRING; 7955.ENSDARP00000014201; -.
DR PaxDb; F1QX91; -.
DR Ensembl; ENSDART00000010126; ENSDARP00000014201; ENSDARG00000003899.
DR GeneID; 445301; -.
DR KEGG; dre:445301; -.
DR CTD; 445301; -.
DR ZFIN; ZDB-GENE-040808-13; zdhhc23b.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156558; -.
DR HOGENOM; CLU_055455_0_0_1; -.
DR InParanoid; F1QX91; -.
DR OMA; ARSHYWG; -.
DR OrthoDB; 1261879at2759; -.
DR TreeFam; TF354316; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000003899; Expressed in ovary and 22 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..428
FT /note="Palmitoyltransferase ZDHHC23-B"
FT /id="PRO_0000451131"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..105
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..160
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..350
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 250..300
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 280
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 261
FT /note="Q -> R (in Ref. 2; AAH79487)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="Y -> F (in Ref. 2; AAH79487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 428 AA; 48309 MW; A79877FAB6FC25BD CRC64;
MSIMKKRSSR AADPDELLCC CEYIDRHGSR SHMVACCCDC EDLDEACDRW MNKEPQNPDS
VSRALATIND RLRVPWISGA RQIDVSLIPP LILLPVFLHI AALHYLLGII MLTAMPITVL
WYYFFTHRKK GRTLFFLGLA LFSLFYMFYL FLTQVVPRGE VTELQLAVVT AGVALTVIFL
MLTKRGPGLV RPRPSETHST VTYHSTPPDV DGVYLNGARH QVVIGSRVAS SEHTGEPGTE
EEEEGVQKRN WCAVCKVVRP QRAGHCRICG VCVLRLDHHC VWINSCVGLA NHRTFLLTLL
FFLLTSIYGI SLVLASVCPD QRVLTALFYC PDVYSQYSSA LCFTCAWYSS IVTGGLLHLL
LLQILNISLN VTEREARLAL REKSAQRRLW GLIVHTGHYS RGFWSNWTEF LTMTEDTQPA
GHKTEDLV
