ZD20A_DANRE
ID ZD20A_DANRE Reviewed; 357 AA.
AC F1Q7H8; A4FVK6; Q05AL0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Palmitoyltransferase ZDHHC20-A {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Acyltransferase ZDHHC20-A {ECO:0000250|UniProtKB:Q5W0Z9};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Zinc finger DHHC domain-containing protein 20-A {ECO:0000312|ZFIN:ZDB-GENE-070424-38};
GN Name=zdhhc20a {ECO:0000312|ZFIN:ZDB-GENE-070424-38};
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=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. Catalyzes palmitoylation of
CC Cys residues on protein substrates and has a preference for acyl-CoA
CC with C16 fatty acid chains but may also utilize acyl-CoA with C14 and
CC C18 fatty acid chains. {ECO:0000250|UniProtKB:Q5W0Z9}.
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:Q5W0Z9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q5W0Z9};
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:Q5W0Z9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q5W0Z9};
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:Q5W0Z9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q5W0Z9};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q5W0Z9}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CR376845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR925771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC124427; AAI24428.1; -; mRNA.
DR EMBL; BC134069; AAI34070.1; -; mRNA.
DR RefSeq; NP_001077018.1; NM_001083549.1.
DR AlphaFoldDB; F1Q7H8; -.
DR SMR; F1Q7H8; -.
DR STRING; 7955.ENSDARP00000071840; -.
DR PaxDb; F1Q7H8; -.
DR Ensembl; ENSDART00000077373; ENSDARP00000071840; ENSDARG00000055066.
DR GeneID; 561776; -.
DR KEGG; dre:561776; -.
DR CTD; 561776; -.
DR ZFIN; ZDB-GENE-070424-38; zdhhc20a.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; F1Q7H8; -.
DR PhylomeDB; F1Q7H8; -.
DR TreeFam; TF316044; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000055066; Expressed in retina and 19 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:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
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; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..357
FT /note="Palmitoyltransferase ZDHHC20-A"
FT /id="PRO_0000451127"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 36..50
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 72..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 188..204
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 229..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT DOMAIN 123..173
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 153
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 44
FT /note="N -> S (in Ref. 2; AAI34070)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="A -> G (in Ref. 2; AAI24428)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> H (in Ref. 2; AAI24428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 357 AA; 41414 MW; 7EBA8F36B889B6A9 CRC64;
MAPSHAVRCC QRGLSWIPVI FINLVVCWSY YAYVVELCIY TIPNVNEQVI YLVVFHAFFF
MFMWSYWKTI SSKPTNPSKE FCLPKAEKEL YEKEERPEAQ QDILKRVARE LPIYTFTGSG
AIRYCDRCQL IKPDRCHHCS TCDKCVLKMD HHCPWVNNCV GFSNYKFFVL FLAYSMLYCV
YIAATVLQYF IKFWTNQLPD THAKFHVLFL FFVAAMFFIS ILSLFSYHLW LVGKNRTTIE
AFRAPVFRNG PDKNGFTLGF RKNITQVFGD QKKYWCLPIF SSLGDGYTFP TRLVTVDVEH
GNIEHQTIKC TVDGQTNARP LSESQNHLLC NDEGQKDSSM AAIEVCQPVC VTLENES
