ZDHC3_RAT
ID ZDHC3_RAT Reviewed; 299 AA.
AC Q2TGK3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Palmitoyltransferase ZDHHC3 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8R173};
DE AltName: Full=Acyltransferase ZDHHC3 {ECO:0000250|UniProtKB:Q8R173};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q8R173};
DE AltName: Full=Zinc finger DHHC domain-containing protein 3 {ECO:0000312|RGD:1309041};
GN Name=Zdhhc3 {ECO:0000312|RGD:1309041};
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 Huang C.-H., Chen Y., Peng J., Ye T.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19596852; DOI=10.1083/jcb.200903101;
RA Noritake J., Fukata Y., Iwanaga T., Hosomi N., Tsutsumi R., Matsuda N.,
RA Tani H., Iwanari H., Mochizuki Y., Kodama T., Matsuura Y., Bredt D.S.,
RA Hamakubo T., Fukata M.;
RT "Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic
RT targeting of PSD-95.";
RL J. Cell Biol. 186:147-160(2009).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates. Has no stringent
CC fatty acid selectivity and in addition to palmitate can also transfer
CC onto target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). Plays an important role in G protein-
CC coupled receptor signaling pathways involving GNAQ and potentially
CC other heterotrimeric G proteins by regulating their dynamic association
CC with the plasma membrane (By similarity). Palmitoylates ITGA6 and
CC ITGB4, thereby regulating the alpha-6/beta-4 integrin localization,
CC expression and function in cell adhesion to laminin (By similarity).
CC Plays a role in the TRAIL-activated apoptotic signaling pathway most
CC probably through the palmitoylation and localization to the plasma
CC membrane of TNFRSF10A (By similarity). In the brain, by palmitoylating
CC the gamma subunit GABRG2 of GABA(A) receptors and regulating their
CC postsynaptic accumulation, plays a role in synaptic GABAergic
CC inhibitory function and GABAergic innervation. Palmitoylates the
CC neuronal protein GAP43 which is also involved in the formation of
CC GABAergic synapses. Palmitoylates NCDN thereby regulating its
CC association with endosome membranes. Probably palmitoylates PRCD and is
CC involved in its proper localization within the photoreceptor. Could
CC mediate the palmitoylation of NCAM1 and regulate neurite outgrowth.
CC Could palmitoylate DNAJC5 and regulate its localization to Golgi
CC membranes (By similarity). Also constitutively palmitoylates DLG4
CC (PubMed:19596852). May also palmitoylate SNAP25. Could palmitoylate the
CC glutamate receptors GRIA1 and GRIA2 but this has not been confirmed in
CC vivo (By similarity). Could also palmitoylate the D(2) dopamine
CC receptor DRD2. {ECO:0000250|UniProtKB:Q8R173,
CC ECO:0000250|UniProtKB:Q9NYG2, ECO:0000269|PubMed:19596852}.
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:Q8R173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8R173};
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:Q8R173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q8R173};
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:Q8R173};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q8R173};
CC -!- SUBUNIT: Monomer. Homooligomers. The monomeric form has a higher
CC catalytic activity. Forms heterooligomers with ZDHHC7 (By similarity).
CC Interacts with TNFRSF10A (By similarity).
CC {ECO:0000250|UniProtKB:Q8R173, ECO:0000250|UniProtKB:Q9NYG2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:19596852}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the Golgi cis cisterna.
CC {ECO:0000250|UniProtKB:Q8R173}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Phosphorylation by FGFR1 and SRC probably regulates the
CC palmitoyltransferase activity. {ECO:0000250|UniProtKB:Q8R173}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q8R173}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY886522; AAX73384.1; -; mRNA.
DR EMBL; AC133294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473954; EDL76770.1; -; Genomic_DNA.
DR EMBL; BC128697; AAI28698.1; -; mRNA.
DR RefSeq; NP_001034103.1; NM_001039014.1.
DR RefSeq; XP_006244250.1; XM_006244188.3.
DR AlphaFoldDB; Q2TGK3; -.
DR SMR; Q2TGK3; -.
DR STRING; 10116.ENSRNOP00000005817; -.
DR PhosphoSitePlus; Q2TGK3; -.
DR SwissPalm; Q2TGK3; -.
DR PaxDb; Q2TGK3; -.
DR Ensembl; ENSRNOT00000005817; ENSRNOP00000005817; ENSRNOG00000004344.
DR GeneID; 301081; -.
DR KEGG; rno:301081; -.
DR UCSC; RGD:1309041; rat.
DR CTD; 51304; -.
DR RGD; 1309041; Zdhhc3.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000155721; -.
DR HOGENOM; CLU_048061_1_1_1; -.
DR InParanoid; Q2TGK3; -.
DR OMA; CVVMTWL; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q2TGK3; -.
DR TreeFam; TF319798; -.
DR PRO; PR:Q2TGK3; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000004344; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; Q2TGK3; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0016409; F:palmitoyltransferase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISO:RGD.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0044873; P:lipoprotein localization to membrane; ISO:RGD.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISO:RGD.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; ISO:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0018345; P:protein palmitoylation; ISO:RGD.
DR GO; GO:0006605; P:protein targeting; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:RGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..299
FT /note="Palmitoyltransferase ZDHHC3"
FT /id="PRO_0000449923"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..72
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..214
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 128..254
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 157
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 18
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8R173"
FT LIPID 146
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q8R173"
SQ SEQUENCE 299 AA; 34113 MW; FE8BC32B21355031 CRC64;
MMLIPTHHFR DIERKPEYLQ PEKCAPPPFP GPVGTMWFIR DGCGIACAIV TWFLVLYAEF
VVLFVMLIPS RDYAYSIING IVFNLLAFLA LASHCRAMLT DPGAVPKGNA TKEFIESLQL
KPGQVVYKCP KCCSIKPDRA HHCSVCKRCI RKMDHHCPWV NNCVGENNQK YFVLFTMYIA
LISLHALIMV GFHFLHCFEE DWTKCSSFSP PTTVILLILL CFEALLFLIF TSVMFGTQVH
SICTDETGIE QLKKEERRWA KKTKWMNMKA VFGHPFSLGW ASPFATPDQG KADPYQYVV
