ZD20B_DANRE
ID ZD20B_DANRE Reviewed; 323 AA.
AC E7F587;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 3.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Palmitoyltransferase ZDHHC20-B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Acyltransferase ZDHHC20-B {ECO:0000250|UniProtKB:Q5W0Z9};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Zinc finger DHHC domain-containing protein 20-B {ECO:0000312|ZFIN:ZDB-GENE-091117-30};
GN Name=zdhhc20b {ECO:0000312|ZFIN:ZDB-GENE-091117-30};
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).
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; CR383672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E7F587; -.
DR SMR; E7F587; -.
DR PaxDb; E7F587; -.
DR Ensembl; ENSDART00000080997; ENSDARP00000075441; ENSDARG00000058178.
DR ZFIN; ZDB-GENE-091117-30; zdhhc20b.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR InParanoid; E7F587; -.
DR OrthoDB; 1491968at2759; -.
DR TreeFam; TF316044; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000058178; Expressed in early embryo and 20 other tissues.
DR ExpressionAtlas; E7F587; baseline.
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 3: Inferred from homology;
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..323
FT /note="Palmitoyltransferase ZDHHC20-B"
FT /id="PRO_0000451128"
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..41
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 63..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 179..195
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 196..219
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 220..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT DOMAIN 114..164
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 144
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 323 AA; 37305 MW; BEF42793BFDB35BC CRC64;
MAPTHVLRCC QRGLAWIPVI FIALVVCWSY YAYVVELCLL VYLVVFHLSF VMFVWSYWKT
IFTKPANPSK EFCLPKSEKE QYEKEQRPET QQEILKKVAT SLPLYTRTGA GAIRYCDRCQ
VIKPDRCHHC SACDMCVLKM DHHCPWVNNC VGFSNYKFFI LFLTYSLVYC LFIAASVLQY
FIKFWTSDLP ESHAKFHVLF LFFVAAMFCI SILSLFTYHL WLVGKNRSTI EAFRAPVFRN
GPDKNGFSLG FSKNIAQVFG DEKKYWLLPV FTSQGDGLSF PTRLVTIDPE QPTECLQPGG
AISSLIIVEY CFCKQAKKKK TDE
