ZDHC5_RAT
ID ZDHC5_RAT Reviewed; 715 AA.
AC Q2THW7;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
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.
RN [2]
RP INTERACTION WITH SSTR5.
RX PubMed=21820437; DOI=10.1016/j.febslet.2011.07.028;
RA Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H.,
RA Hennemann H., Kreienkamp H.J.;
RT "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5
RT palmitoyltransferase.";
RL FEBS Lett. 585:2665-2670(2011).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-425; SER-554 AND
RP SER-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP PALMITOYLATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31547976; DOI=10.1016/j.bpj.2019.08.018;
RA Chen J.J., Marsden A.N., Scott C.A., Akimzhanov A.M., Boehning D.;
RT "DHHC5 Mediates beta-Adrenergic Signaling in Cardiomyocytes by Targeting
RT Galpha Proteins.";
RL Biophys. J. 118:826-835(2020).
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 (PubMed:31547976). Plays an important role in the regulation of synapse
CC efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby
CC increasing synaptic delivery and surface stabilization of alpha-amino-
CC 3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs). Under
CC basal 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 ECO:0000269|PubMed:31547976}.
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:0000269|PubMed:31547976};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated (By similarity). Palmitoylation of the C-
CC terminal tail regulates stimulation-dependent plasma membrane motility
CC (PubMed:31547976). {ECO:0000250|UniProtKB:Q9C0B5,
CC ECO:0000269|PubMed:31547976}.
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 -!- 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; AY871203; AAX68536.1; -; mRNA.
DR RefSeq; NP_001034427.1; NM_001039338.1.
DR RefSeq; XP_017447385.1; XM_017591896.1.
DR RefSeq; XP_017447386.1; XM_017591897.1.
DR RefSeq; XP_017447387.1; XM_017591898.1.
DR AlphaFoldDB; Q2THW7; -.
DR STRING; 10116.ENSRNOP00000009708; -.
DR iPTMnet; Q2THW7; -.
DR PhosphoSitePlus; Q2THW7; -.
DR PaxDb; Q2THW7; -.
DR PRIDE; Q2THW7; -.
DR Ensembl; ENSRNOT00000009708; ENSRNOP00000009708; ENSRNOG00000006832.
DR GeneID; 362156; -.
DR KEGG; rno:362156; -.
DR UCSC; RGD:1589737; rat.
DR CTD; 25921; -.
DR RGD; 1589737; Zdhhc5.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_0_0_1; -.
DR InParanoid; Q2THW7; -.
DR OMA; LAPRYMG; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q2THW7; -.
DR TreeFam; TF354263; -.
DR BRENDA; 2.3.1.225; 5301.
DR PRO; PR:Q2THW7; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006832; Expressed in esophagus and 18 other tissues.
DR Genevisible; Q2THW7; RN.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0018345; P:protein palmitoylation; ISO:RGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein 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_0000418364"
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..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..715
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..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..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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; 77430 MW; C142840D11C0E494 CRC64;
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LDVSPAVPIY NAIMFLFVLA
NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI MGVFGFGLLY VLCHIEELSG
VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
EITESQSADA EPPPPPKPDL SRYTGLRTHL SLATNEDSSL LGKDSPPTPT MYKYRPGYSS
SSTSAAMPHS SSAKLSRGDS LKEPTSIADS SRHPSYRSEP SLEPESFRSP TFGKSFHFDP
LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
DFESVQAGPE PDPPLGYTSP FLSARLAQQR EAERHPRLLP TGPPHREPSP VRYDNLSRHI
VASLQEREKL LRQSPPLAGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLSKTPL
GRPAVPRFGK PDGLRGRGLG SPEPGTTAPY LGRSMSYSSQ KAPSGVSETE EVALQPLLTP
KDEVQLKTTY SKSNGQPKSI GSASPGPGQP PLSSPTRGGV KKVSGVGGTT YEISV
