ZDHC1_DANRE
ID ZDHC1_DANRE Reviewed; 578 AA.
AC E7F4Z4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Palmitoyltransferase ZDHHC1 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8WTX9};
DE AltName: Full=DHHC domain-containing protein 1 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 1 {ECO:0000305|PubMed:27235108};
GN Name=zdhhc1 {ECO:0000303|PubMed:27235108};
GN Synonyms=dhhc1 {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 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 [3]
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: May have a palmitoyltransferase activity toward substrates
CC like ncdn, thereby regulating their association with membranes.
CC {ECO:0000250|UniProtKB:Q8R0N9}.
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:Q8R0N9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8R0N9};
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:Q8R0N9};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q8WTX9}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q8WTX9}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression is detected early during development at the 512-cell stage.
CC {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:0000255|RuleBase:RU079119}.
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DR EMBL; CR381641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_691086.3; XM_685994.8.
DR AlphaFoldDB; E7F4Z4; -.
DR STRING; 7955.ENSDARP00000102433; -.
DR PaxDb; E7F4Z4; -.
DR Ensembl; ENSDART00000110552; ENSDARP00000102433; ENSDARG00000077546.
DR Ensembl; ENSDART00000189002; ENSDARP00000146569; ENSDARG00000077546.
DR GeneID; 562614; -.
DR KEGG; dre:562614; -.
DR CTD; 29800; -.
DR ZFIN; ZDB-GENE-130925-1; zdhhc1.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159191; -.
DR HOGENOM; CLU_020283_0_1_1; -.
DR InParanoid; E7F4Z4; -.
DR OMA; CASAKHC; -.
DR OrthoDB; 1216670at2759; -.
DR TreeFam; TF317498; -.
DR PRO; PR:E7F4Z4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000077546; Expressed in mature ovarian follicle and 21 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
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; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..578
FT /note="Palmitoyltransferase ZDHHC1"
FT /id="PRO_0000449457"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..71
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..230
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 121..173
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 278..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 578 AA; 63372 MW; 950631C323005D1C CRC64;
MDVCSKNSNR TAPVSEGGIR RADVPLCSRT NGWSWPPHPF QFLAWLLYLY FAVTGFGVFV
PLLPTHWIPA GYICTGITFV CHLFMHLMAV SIDPADYNVR AKSYKGPMPV FDRTKHAHVI
ENCHCYLCEV DVGPKSKHCS ACNKCVASFD HHCRWLNNCV GSRNYWLFLN SVISALLGIV
LVVVIASYVF IEFFLDPSKL RSDKHFQQVR NESVVWFVFL PVAPVTTAGP AIPALAGVTI
ALGLLSALLL GHLLCFHIYL MWNRLSTYEY IVRQRHRQEA GDSRKPPPEN DSGVPKLNLI
KQQVSYSGTL GYTNPEMEVE DPKAMTSQEG AARYGNGRIR CSSEHMDEEE HLPSVLTEQK
ASPHPHKHAQ KKKRKVRKLA AEVNGDISID TSTAKGLQKT SAEKESSVAA ATVSSSLGQR
LPFPAFPLRA SLPPLAPVQA AGPPAEYHSD SAESLEEIPV AMARLGSAAL AGAQIPTTTA
TASSSYSSML QCALPSSAAG HAAPSPQPRT KRKTAARTVS EQRFEMLYHN PSMFMTRESG
EPAIPPEESP RAAKRKQTGK KRNTEDAKPS SRVGTSLA
