ZDH17_DANRE
ID ZDH17_DANRE Reviewed; 620 AA.
AC A5WVX9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Palmitoyltransferase ZDHHC17 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IUH5};
DE AltName: Full=Acyltransferase ZDHHC17 {ECO:0000250|UniProtKB:Q80TN5};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q80TN5};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 17 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 17 {ECO:0000303|PubMed:26232532};
GN Name=zdhhc17 {ECO:0000303|PubMed:26232532,
GN ECO:0000312|ZFIN:ZDB-GENE-070424-194};
GN Synonyms=dhhc17 {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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26232532; DOI=10.1016/j.mcn.2015.07.005;
RA Shi W., Wang F., Gao M., Yang Y., Du Z., Wang C., Yao Y., He K., Chen X.,
RA Hao A.;
RT "ZDHHC17 promotes axon outgrowth by regulating TrkA-tubulin complex
RT formation.";
RL Mol. Cell. Neurosci. 68:194-202(2015).
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 catalyzes the addition of palmitate
CC onto various protein substrates and is involved in a variety of
CC cellular processes. Has no stringent fatty acid selectivity and in
CC addition to palmitate can also transfer onto target proteins myristate
CC from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By
CC similarity). Plays a role in axonogenesis (PubMed:26232532).
CC {ECO:0000250|UniProtKB:Q80TN5, ECO:0000250|UniProtKB:Q8IUH5,
CC ECO:0000269|PubMed:26232532}.
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:Q8IUH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at 2.75 hpf and then decreases after
CC 18 hpf but is still detected at 24 hpf (PubMed:26056731,
CC PubMed:27235108). Highly expressed in the developing central nervous
CC system from the presumptive telencephalon to the caudal tip of the
CC spinal cord (PubMed:26232532). {ECO:0000269|PubMed:26056731,
CC ECO:0000269|PubMed:26232532, ECO:0000269|PubMed:27235108}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein does not
CC apparently affect embryo development (PubMed:26232532). However, the
CC motility of morphants is markedly reduced from 3 days post-
CC fertilization onwards (PubMed:26232532). This is associated with a
CC significant defect in the axonal outgrowth of spinal motor neurons
CC without affecting neuron generation (PubMed:26232532).
CC {ECO:0000269|PubMed:26232532}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR EMBL; CT573050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001121854.1; NM_001128382.1.
DR AlphaFoldDB; A5WVX9; -.
DR SMR; A5WVX9; -.
DR STRING; 7955.ENSDARP00000094148; -.
DR PaxDb; A5WVX9; -.
DR PeptideAtlas; A5WVX9; -.
DR Ensembl; ENSDART00000103371; ENSDARP00000094148; ENSDARG00000070441.
DR GeneID; 100148543; -.
DR KEGG; dre:100148543; -.
DR CTD; 23390; -.
DR ZFIN; ZDB-GENE-070424-194; zdhhc17.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; A5WVX9; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; A5WVX9; -.
DR TreeFam; TF317342; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 4.
DR Bgee; ENSDARG00000070441; Expressed in mature ovarian follicle and 21 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0007409; P:axonogenesis; IMP:ZFIN.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030289; ZDHHC17.
DR PANTHER; PTHR24161:SF18; PTHR24161:SF18; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; ANK repeat; Cell membrane; Cell projection;
KW Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Synapse; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..620
FT /note="Palmitoyltransferase ZDHHC17"
FT /id="PRO_0000451101"
FT TOPO_DOM 1..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..369
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..504
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 505..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 77..106
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 111..140
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..173
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 177..207
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 212..241
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 245..274
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT DOMAIN 425..475
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 455
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5,
FT ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 620 AA; 71349 MW; 2CB23E404522566F CRC64;
MADALVGYEK EAGCVPILHP EEIKPQSHYN HGYNESRKSH VDDYSTWDIV KATQYGIFER
CRELVEAGYD VRQPDKENVT LLHWAAINNR VDLVKYYISK GAIVDQLGGD LNSTPLHWAT
RQGHLSMVVQ LMKYGADPSL IDGEGCSCVH LAAQFGHTSI VAYLIAKGQD VDMMDQNGMT
PLMWAAYRTH SVDPTRLLLT FNVSVNLGDK YHKNTALHWA VLAGNTTVIS LLLEANANVD
AQNIKGETPL DLAKQRKNVW MINHLQEARQ AKGYDSPSYL KRLKMDKEFR QKVMLGTPFL
VIWLVGFIAD LDIDSWLIKG VMYAVMWLVV QFLSKSFFDH SMHSALPLGI YLATKFWMYI
TWFYWFWNDL PFVTIHLPFL LNSLALFYNF GKSWKSDPGI IKASEEQKKK TIVELAETGS
LDLSIFCSTC LIRKPIRSKH CAVCNRCIAK FDHHCPWVGN CVGSGNHRYF MGYLFFLLCM
ICWMMYGCIC YWRIHCATSY TKDGFWIYIT QIATCSPWMF WMFLNSVFHF MWVAVLIMCQ
LYQIAVLGIT TNERMNARRY KHFKVTATSI ESPFNHGCMR NLIDFFELRC CGLLRPVPID
WTSQYTIEYD QTSGSGYQLV
