ZDH8B_DANRE
ID ZDH8B_DANRE Reviewed; 751 AA.
AC A2CEX1; Q7ZU06; Q8AYN4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Palmitoyltransferase ZDHHC8B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9ULC8};
DE AltName: Full=Zinc finger DHHC domain-containing protein 8B {ECO:0000312|ZFIN:ZDB-GENE-030407-3};
GN Name=zdhhc8b {ECO:0000312|ZFIN:ZDB-GENE-030407-3};
GN Synonyms=dhhc8 {ECO:0000303|PubMed:26056731},
GN zisp {ECO:0000303|PubMed:14516702};
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 [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=14516702; DOI=10.1016/s0925-4773(03)00133-3;
RA Nagaya M., Inohaya K., Imai Y., Kudo A.;
RT "Expression of zisp, a DHHC zinc finger gene, in somites and lens during
RT zebrafish embryogenesis.";
RL Mech. Dev. 119:S311-S314(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen Y., Huang C.-H.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 catalyzes the addition of palmitate
CC onto various protein substrates and therefore function in several
CC unrelated biological processes. {ECO:0000250|UniProtKB:Q9ULC8}.
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:Q9ULC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC8};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ULC8}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5Y5T5};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: First detected at 2.75 hours post-
CC fertilization/hpf (PubMed:27235108). The expression increases at least
CC till 24 hpf (PubMed:26056731). During the segmentation period expressed
CC in the adaxial cells and the somites in a striping pattern
CC (PubMed:14516702). By 24 hpf, expression in the somites decreases
CC except in the tail region. In addition expression is also detected in
CC lens placode and lens fiber cell from 18 hpf till 48 hpf and then
CC decreases to disappear at 60 hpf (PubMed:14516702).
CC {ECO:0000269|PubMed:14516702, 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 -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AB085761; BAC24796.1; -; mRNA.
DR EMBL; AY871211; AAX68544.1; -; mRNA.
DR EMBL; CR774200; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR790378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049439; AAH49439.1; -; mRNA.
DR RefSeq; NP_840089.2; NM_178304.3.
DR AlphaFoldDB; A2CEX1; -.
DR SMR; A2CEX1; -.
DR STRING; 7955.ENSDARP00000108476; -.
DR PaxDb; A2CEX1; -.
DR Ensembl; ENSDART00000129878; ENSDARP00000108476; ENSDARG00000018508.
DR GeneID; 352941; -.
DR KEGG; dre:352941; -.
DR CTD; 352941; -.
DR ZFIN; ZDB-GENE-030407-3; zdhhc8b.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000158044; -.
DR HOGENOM; CLU_013779_0_0_1; -.
DR InParanoid; A2CEX1; -.
DR OMA; TAEQITM; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; A2CEX1; -.
DR TreeFam; TF354263; -.
DR Reactome; R-DRE-8963896; HDL assembly.
DR PRO; PR:A2CEX1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000018508; Expressed in somite and 37 other tissues.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030291; ZDHHC8.
DR PANTHER; PTHR12349:SF1; PTHR12349:SF1; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Mitochondrion;
KW Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..751
FT /note="Palmitoyltransferase ZDHHC8B"
FT /id="PRO_0000450547"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..41
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..751
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 293..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 171
FT /note="V -> M (in Ref. 4; AAH49439 and 2; AAX68544)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="L -> I (in Ref. 1; BAC24796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 751 AA; 82852 MW; 7F15D1C3F77178BC CRC64;
MPNSVGKRFK PTKYIPVSTA ATLLVGSTTL FFVFTCPWLT KAVSPVVPLY NGIVFLFVLA
NFSMATFMDP GVFPRADEDE DKDDDFRAPL YKNVEIKGIQ VRMKWCATCH FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLSVHM VGVFSFGLLF VLHHLETLSA
LHTTVTLVVM CVTGLFFIPV MGLTGFHMVL VARGRTTNEQ VTGKFRGGVN PFTRGCGGNV
KHVLCSPLAP RYIADPRKKI PVTVTPPFLR PDLSNRHISV KVSDNGIHSN ILRSKSKTSL
NGMDDKSIDA QPPLPPKADR YNQIKSQLTS SEESSLSSKP TNPSTPAMFK YRPSFGTMPK
VHYHATGEKI VMCENGNPSA VLEERSHDYR SEPNLDLPDY RSAPLHRTYQ SSPFQLDSFS
TTSRSFSLKQ GVNRADCTPL GGTKHETITS TPHRGVFSPG TLSGRNSSLS YDSLLTPSVA
PSIGECAAHP GVPSMGFHSP YLPTKMCHVR GPELQRHAGP PSYSPVHIGA MYGRQSPLSR
ERERDPSPVR YDNLSKTIMA SIQERKEFEE REKLMHRHVQ GYANDSGVFD TAYGLPHGYP
DGPRGPASRE PTPPVCASRD NLMGYPPRTP VLRSSASSLV RAPRTSTTSL HTDGGGMNRT
AELQYRSPVH QSHQSPTSVP RSPSYAHQKV AFISALERAD SPHLGTREDI GQGKVNGQLK
GQYGTPSGTP SRHTSVKKVT GVGGTTYEIS V
