ZDH20_BOVIN
ID ZDH20_BOVIN Reviewed; 365 AA.
AC Q0VC89;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Palmitoyltransferase ZDHHC20 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Acyltransferase ZDHHC20 {ECO:0000250|UniProtKB:Q5W0Z9};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=Zinc finger DHHC domain-containing protein 20 {ECO:0000250|UniProtKB:Q5W0Z9};
GN Name=ZDHHC20 {ECO:0000250|UniProtKB:Q5W0Z9};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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 in the cytoplasmic C-terminus of EGFR, and modulates the
CC duration of EGFR signaling by modulating palmitoylation-dependent EGFR
CC internalization and degradation. Has a preference for acyl-CoA with C16
CC fatty acid chains. Can also utilize acyl-CoA with C14 and C18 fatty
CC 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 -!- PTM: Autopalmitoylated (in vitro). {ECO:0000250|UniProtKB:Q5W0Z9}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC120294; AAI20295.1; -; mRNA.
DR RefSeq; NP_001069856.1; NM_001076388.2.
DR RefSeq; XP_005213858.1; XM_005213801.1.
DR RefSeq; XP_005213859.1; XM_005213802.1.
DR AlphaFoldDB; Q0VC89; -.
DR SMR; Q0VC89; -.
DR STRING; 9913.ENSBTAP00000008119; -.
DR PaxDb; Q0VC89; -.
DR PRIDE; Q0VC89; -.
DR Ensembl; ENSBTAT00000078233; ENSBTAP00000059434; ENSBTAG00000006177.
DR GeneID; 615659; -.
DR KEGG; bta:615659; -.
DR CTD; 253832; -.
DR VEuPathDB; HostDB:ENSBTAG00000006177; -.
DR VGNC; VGNC:37136; ZDHHC20.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; Q0VC89; -.
DR OMA; QPDSNKC; -.
DR OrthoDB; 1491968at2759; -.
DR TreeFam; TF316044; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000006177; Expressed in monocyte and 110 other tissues.
DR ExpressionAtlas; Q0VC89; 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:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
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: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:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
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..365
FT /note="Palmitoyltransferase ZDHHC20"
FT /id="PRO_0000269230"
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..53
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 75..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 191..207
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 208..231
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 232..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT DOMAIN 126..176
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 301..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 140..143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT SITE 29
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT SITE 181
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
SQ SEQUENCE 365 AA; 41907 MW; B6C65283C2308463 CRC64;
MAPCTLWRCC QRTVGWVPVL FITFVVVWSY YAYVVELCVF TLSGNGENGK AVVYLVAFHL
FFVMFVWSYW MTIFTSPASP SKEFCLSNSE KERYEKEFSQ ERQQEILRRA ARDLPIYTTS
ASKTVRYCER CQLIKPDRAH HCSACDMCIL KMDHHCPWVN NCVGFSNYKF FLLFLFYSLL
YCLFVATTVL QYFIKFWTNE LTDTRAKFHV LFLFFVSTMF FISVLSLLSY HCWLVGKNRT
TIESFRAPMF SYGTDGNGFS LGCSKNWRQV FGDEKKYWLL PVFSSQGDGC SFPTRLVGTD
PEQASVSNQS ESARSIGSNQ PFPIKPLSES KNRLLDSDPQ WLESGSEEGV GGSGTNNHVT
VAIEN
