ZDH13_DANRE
ID ZDH13_DANRE Reviewed; 645 AA.
AC A0A0R4IQZ2; Q5PRB8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Putative palmitoyltransferase ZDHHC13 {ECO:0000305};
DE AltName: Full=DHHC domain-containing protein 13 {ECO:0000303|PubMed:26056731};
DE Short=DHHC-13 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 13 {ECO:0000303|PubMed:27235108};
GN Name=zdhhc13 {ECO:0000303|PubMed:27235108,
GN ECO:0000312|ZFIN:ZDB-GENE-041212-79};
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=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2004) 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: Putative palmitoyltransferase that could catalyze the
CC addition of palmitate onto various protein substrates.
CC {ECO:0000250|UniProtKB:Q9CWU2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at shield stage (6 hpf) and then
CC decreases after 7.5 hpf but is still detected at 24 hpf.
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 AKR/ZDHHC17 subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the DHHC palmitoyltransferase family,
CC lacks the conserved active site cysteine residue at position 479 and
CC may lack catalytic activity. {ECO:0000305}.
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DR EMBL; CU041375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086723; AAH86723.1; -; mRNA.
DR RefSeq; NP_001008650.2; NM_001008650.3.
DR AlphaFoldDB; A0A0R4IQZ2; -.
DR SMR; A0A0R4IQZ2; -.
DR STRING; 7955.ENSDARP00000094138; -.
DR PaxDb; A0A0R4IQZ2; -.
DR Ensembl; ENSDART00000173777; ENSDARP00000142710; ENSDARG00000101144.
DR GeneID; 494107; -.
DR KEGG; dre:494107; -.
DR CTD; 54503; -.
DR ZFIN; ZDB-GENE-041212-79; zdhhc13.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; A0A0R4IQZ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 7.
DR Bgee; ENSDARG00000101144; Expressed in cleaving embryo and 29 other tissues.
DR ExpressionAtlas; A0A0R4IQZ2; baseline.
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:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0060803; P:BMP signaling pathway involved in mesodermal cell fate specification; IMP:ZFIN.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IMP:ZFIN.
DR GO; GO:0042665; P:regulation of ectodermal cell fate specification; IMP:ZFIN.
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; IPR030290; ZDHHC13.
DR PANTHER; PTHR24161:SF16; PTHR24161:SF16; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasmic vesicle; Golgi apparatus; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..645
FT /note="Putative palmitoyltransferase ZDHHC13"
FT /id="PRO_0000451060"
FT TOPO_DOM 1..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..394
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..542
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 543..563
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 564..645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 104..133
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 138..167
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 171..200
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 204..234
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 239..268
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT DOMAIN 449..499
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 176
FT /note="L -> F (in Ref. 2; AAH86723)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="P -> L (in Ref. 2; AAH86723)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="E -> G (in Ref. 2; AAH86723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 71440 MW; AAA4626328FCCF74 CRC64;
MDWSEGDGSH SHGHMGDSCH GHGGGHSHGH GHSHGGSGFG GFMPAGFHGQ LVPGPMDPTQ
QPRKSSHPED SSSWDIIKAT QFGALERCKE LVEAGYDVRQ PDKENVTLLH WAAINNRADI
VKYYISKGAV IDQLGGDLNS TPLHWAIRQG HLSMVIQLMR YGADPSLADG EGYRGLHLAV
LFQNMPIAAY LMAKGQEVDL PDLNGQTPLM LAAQKIIGPE PTNFLIKCNA SVNAVDKVNR
NSPLHCAVLA GNVDSVHILL EAGASVDMQN DNGHTAIDLA QQVHSPLLIH MLSVVKTERI
KANSACLKLL NRYKVCLQSV FSVVVVGAFG AILDMRTESW LLKGILLACI MAVINLASRQ
LATVAVRSLI PSTGLIASVF WMVVTWVLWF LPDEPSAAVQ MLFTVNITAV LYYYIRSCRT
DPGHVKATEE EKKKNIVVLA EAGCLDPRIF CTSCMMRKPM RANHCFSCNA CVAKQDHHSI
WINGCIGARN HPFFVLFLVA LNFLCIWMFY GSITYWSRHC PLHYSEEGIW GALTALMGCS
PWLLYVFCFV FFHTTWASIL LVLQLYQIAF LGLTTSERAN LMHRQRKLPQ AVSLRQNPFN
HGVVKNLVNF FQWRFCGLCK PMVLDWTQQH PMGLGRDMFS SPDAV
