ZDHC5_BOVIN
ID ZDHC5_BOVIN Reviewed; 714 AA.
AC E1BLT8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Palmitoyltransferase ZDHHC5;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE AltName: Full=Zinc finger DHHC domain-containing protein 5;
DE Short=DHHC-5;
GN Name=ZDHHC5;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates such as CTNND2, CD36, STAT3 and S1PR1
CC thus plays a role in various biological processes including cell
CC adhesion, fatty acid uptake, bacterial sensing or cardiac functions.
CC Plays an important role in the regulation of synapse efficacy by
CC mediating palmitoylation of delta-catenin/CTNND2, thereby increasing
CC synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-
CC methyl-4-isoxazole propionic acid receptors (AMPARs). Under basal
CC conditions, remains at the synaptic membrane through FYN-mediated
CC phosphorylation that prevents association with endocytic proteins.
CC Neuronal activity enhances the internalization and trafficking of DHHC5
CC from spines to dendritic shafts where it palmitoylates delta-
CC catenin/CTNND2. Regulates cell adhesion at the plasma membrane by
CC palmitoylating GOLGA7B and DSG2. Plays a role in innate immune response
CC by mediating the palmitoylation of NOD1 and NOD2 and their proper
CC recruitment to the bacterial entry site and phagosomes. Participates
CC also in fatty acid uptake by palmitoylating CD36 and thereby targeting
CC it to the plasma membrane. Upon binding of fatty acids to CD36, gets
CC phosphorylated by LYN leading to inactivation and subsequent CD36
CC caveolar endocytosis. {ECO:0000250|UniProtKB:Q9C0B5}.
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:Q8VDZ4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8VDZ4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDZ4};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Phosphorylation regulates association with endocytic proteins and
CC its subcellular localization. Phosphorylation by LYN during fatty acid
CC uptake leads to inactivation of the activity.
CC {ECO:0000250|UniProtKB:Q9C0B5}.
CC -!- PTM: Autopalmitoylated (By similarity). Palmitoylation of the C-
CC terminal tail regulates stimulation-dependent plasma membrane motility
CC (By similarity). {ECO:0000250|UniProtKB:Q2THW7,
CC ECO:0000250|UniProtKB:Q9C0B5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02041769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179692.1; NM_001192763.1.
DR RefSeq; XP_005201016.1; XM_005200959.2.
DR AlphaFoldDB; E1BLT8; -.
DR STRING; 9913.ENSBTAP00000003078; -.
DR PaxDb; E1BLT8; -.
DR PRIDE; E1BLT8; -.
DR Ensembl; ENSBTAT00000003078; ENSBTAP00000003078; ENSBTAG00000002381.
DR GeneID; 533250; -.
DR KEGG; bta:533250; -.
DR CTD; 25921; -.
DR VEuPathDB; HostDB:ENSBTAG00000002381; -.
DR VGNC; VGNC:37143; ZDHHC5.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_0_0_1; -.
DR InParanoid; E1BLT8; -.
DR OMA; LAPRYMG; -.
DR OrthoDB; 1264614at2759; -.
DR TreeFam; TF354263; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000002381; Expressed in retina and 106 other tissues.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0062208; P:positive regulation of pattern recognition receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0018345; P:protein palmitoylation; 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; Immunity; Innate immunity; Lipid transport;
KW Lipoprotein; Membrane; Methylation; Palmitate; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..714
FT /note="Palmitoyltransferase ZDHHC5"
FT /id="PRO_0000418363"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 289..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 91
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 616
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 696
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 714 AA; 76976 MW; F86040EEF7BFE613 CRC64;
MPAESAKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LSVSPAVPVY NAVVFLFVLA
NFSMATFMDP GVFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI TGVFGFGLLY VLYHMEELSG
VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
EVTESQSADA EPPPPPKPDL SRYTGLRTHL SLATNEESSL LGKDSPPTPT MYKYRPGYSS
SSASAAMPHS SSAKLSRGDS LKEPPSIAES SRQPSYRSEP SLEPESFRSP TLGKGFPFDP
LSSGSRSSSL KSAQGTGFEL GPLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
DFESVQAGPE PEPPLGYTSP FLSARLAQQR EAERHPRLAP GGPAPREPSP VRYDNLSRHI
VASLQEREKL LRQSPPPGRE EEPGLGDSGV QCTPGSGHAP RTSSSSDDSK RSPLGKTPLA
RPVAPRFGKP DGLRGRGLAS PEPGLPAPYL GRSVSYSSQK APPGVPETEE VALQPLLTPK
DEVQLKTAYS KSNGQPKSIG SAPPGPGQPP LSSPTRGGVK KVSGVGGTTY EISV
