ZDHC2_DANRE
ID ZDHC2_DANRE Reviewed; 361 AA.
AC Q5BLG4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Palmitoyltransferase ZDHHC2 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9UIJ5};
DE AltName: Full=Acyltransferase ZDHHC2 {ECO:0000250|UniProtKB:P59267};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P59267};
DE AltName: Full=DHHC domain-containing protein 2 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 2 {ECO:0000305|PubMed:27235108};
GN Name=zdhhc2 {ECO:0000303|PubMed:27235108};
GN Synonyms=dhhc2 {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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2005) 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: 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). {ECO:0000250|UniProtKB:P59267,
CC ECO:0000250|UniProtKB:Q9UIJ5}.
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:Q9UIJ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9UIJ5};
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:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:P59267};
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:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC -!- SUBUNIT: Monomer. Homodimer. The monomeric form has a higher catalytic
CC activity. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UIJ5};
CC Multi-pass membrane protein {ECO:0000255}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q9JKR5}. Postsynaptic recycling endosome
CC membrane {ECO:0000250|UniProtKB:P59267}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Translocates to postsynaptic
CC density when synaptic activity decreases.
CC {ECO:0000250|UniProtKB:Q9JKR5}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression is detected early during development at the 512-cell stage
CC but decreases after 7.5 hpf. {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 -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CR384105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090450; AAH90450.1; -; mRNA.
DR EMBL; BC164809; AAI64809.1; -; mRNA.
DR RefSeq; NP_001013510.1; NM_001013492.1.
DR AlphaFoldDB; Q5BLG4; -.
DR SMR; Q5BLG4; -.
DR STRING; 7955.ENSDARP00000019867; -.
DR PaxDb; Q5BLG4; -.
DR Ensembl; ENSDART00000011480; ENSDARP00000019867; ENSDARG00000034757.
DR GeneID; 541365; -.
DR KEGG; dre:541365; -.
DR CTD; 51201; -.
DR ZFIN; ZDB-GENE-050320-58; zdhhc2.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; Q5BLG4; -.
DR OMA; DFPTRSD; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q5BLG4; -.
DR TreeFam; TF316044; -.
DR Reactome; R-DRE-5683826; Surfactant metabolism.
DR PRO; PR:Q5BLG4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000034757; Expressed in cardiac ventricle and 10 other tissues.
DR ExpressionAtlas; Q5BLG4; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISS:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; 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; Cell membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Synapse; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Palmitoyltransferase ZDHHC2"
FT /id="PRO_0000449926"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..50
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 124..174
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 296..361
FT /note="Mediates localization to plasma membrane and
FT recycling endosomes"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT REGION 299..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 333..334
FT /note="Non-canonical dileucine endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT MOTIF 352..355
FT /note="NPxY-like endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT COMPBIAS 339..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 361 AA; 41921 MW; 44EB85A4F00D4289 CRC64;
MAPSGSRSFD CWRVLYWIPV LFISLIVAWS YYAYVVQLCI ETIENMGEKT VYLLIYHLLF
LMFVWSYWQT IYSKPMNPLK EFHLSHVDKE LLEREDRRES QQEILRRIAK DLPIYTRTMS
GAIRYCDRCL LLKPDRCHHC SACDMCILKM DHHCPWVNNC VGFANYKFFM LFLAYSLLYC
LFVTATDMQY FIQFWTNGLP DTQAKFHIMF LFFAASTFSV SLAFLFAYHC WLVCKNRSTL
EAFRAPAFQH GTDKNGFSLG AYKNFRQVFG DEKKYWLLPI FSSLGDGCSF PTCLVNPDPE
QPSIPPGRNP SVKSAGESHP FPPKPLRESQ SRLLNNGQTD GSEDRDKRGT SNPALTIEKE
T
