ZDHC5_CANLF
ID ZDHC5_CANLF Reviewed; 715 AA.
AC Q2THW9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen Y., Huang C.-H.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY871201; AAX68534.1; -; mRNA.
DR RefSeq; NP_001041570.1; NM_001048105.1.
DR RefSeq; XP_005631102.1; XM_005631045.2.
DR AlphaFoldDB; Q2THW9; -.
DR STRING; 9615.ENSCAFP00000011554; -.
DR Ensembl; ENSCAFT00030010279; ENSCAFP00030009005; ENSCAFG00030005614.
DR Ensembl; ENSCAFT00040025881; ENSCAFP00040022510; ENSCAFG00040013996.
DR Ensembl; ENSCAFT00845035969; ENSCAFP00845028149; ENSCAFG00845020408.
DR GeneID; 483490; -.
DR KEGG; cfa:483490; -.
DR CTD; 25921; -.
DR VEuPathDB; HostDB:ENSCAFG00845020408; -.
DR GeneTree; ENSGT00940000156001; -.
DR InParanoid; Q2THW9; -.
DR OrthoDB; 1264614at2759; -.
DR Proteomes; UP000002254; Chromosome 18.
DR Bgee; ENSCAFG00000042658; Expressed in nose and 45 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 2: Evidence at transcript level;
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..715
FT /note="Palmitoyltransferase ZDHHC5"
FT /id="PRO_0000269228"
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..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..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..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 289..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..697
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 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 415
FT /note="Phosphoserine"
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 617
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 697
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 715 AA; 77385 MW; 9BEC02E1EFB501C2 CRC64;
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LCVSPAVPIY NAIVFLFVLA
NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI MGVFGFGLLY VLYHMEELSG
VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRSKSKGSL
EVTESQSADA EPPPPPKPDL SRYTGLRTHL TLAANEDSSL LGKDSPPTPT MYKYRPGYSS
SSTSAAMPHS SSAKLSRGDS LKEPTSIAES SRHPSYRSEP SLEPESFRSP TFGKSFHFDP
LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
DFESVQAGPE PDPPLGYTSP FLSARLAQQR EAERHPRLVP TGPTHREPSP VRYDNLSRHI
VASLQEREKL LRQSPPLPGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLVKTPL
GRPAAPRFGK PDGLRGRGLG SPEPGPTAPY LGRSMSYSSQ KAPAGVSEAE EVALQPLLTP
KDEVQLKTAY SKSNGQPKSI GSASPGPGQQ PLSSPTRGGV KKVSGVGGTT YEISV
