ZDHC3_MOUSE
ID ZDHC3_MOUSE Reviewed; 299 AA.
AC Q8R173; Q6EMK3;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Palmitoyltransferase ZDHHC3 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:19001095, ECO:0000269|PubMed:23793055, ECO:0000269|PubMed:26487721};
DE AltName: Full=Acyltransferase ZDHHC3 {ECO:0000305|PubMed:28167757};
DE EC=2.3.1.- {ECO:0000305|PubMed:28167757};
DE AltName: Full=GABA-A receptor-associated membrane protein 1 {ECO:0000312|EMBL:AAO27359.1};
DE AltName: Full=Golgi-specific DHHC zinc finger protein {ECO:0000303|PubMed:12163046};
DE AltName: Full=Zinc finger DHHC domain-containing protein 3 {ECO:0000312|MGI:MGI:1926134};
DE Short=DHHC-3 {ECO:0000303|PubMed:15603741};
GN Name=Zdhhc3 {ECO:0000312|MGI:MGI:1926134};
GN Synonyms=Godz {ECO:0000303|PubMed:12163046},
GN Gramp1 {ECO:0000312|EMBL:AAO27359.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=12163046; DOI=10.1016/s0006-291x(02)00900-2;
RA Uemura T., Mori H., Mishina M.;
RT "Isolation and characterization of Golgi apparatus-specific GODZ with the
RT DHHC zinc finger domain.";
RL Biochem. Biophys. Res. Commun. 296:492-496(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AUTOPALMITOYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=15229235; DOI=10.1523/jneurosci.1037-04.2004;
RA Keller C.A., Yuan X., Panzanelli P., Martin M.L., Alldred M.,
RA Sassoe-Pognetto M., Luescher B.;
RT "The gamma2 subunit of GABA(A) receptors is a substrate for palmitoylation
RT by GODZ.";
RL J. Neurosci. 24:5881-5891(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT "Identification of PSD-95 palmitoylating enzymes.";
RL Neuron 44:987-996(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AUTOPALMITOYLATION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF CYS-157, AND ACTIVE SITE.
RX PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA Hayashi T., Rumbaugh G., Huganir R.L.;
RT "Differential regulation of AMPA receptor subunit trafficking by
RT palmitoylation of two distinct sites.";
RL Neuron 47:709-723(2005).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=17151279; DOI=10.1523/jneurosci.4214-06.2006;
RA Fang C., Deng L., Keller C.A., Fukata M., Fukata Y., Chen G., Luescher B.;
RT "GODZ-mediated palmitoylation of GABA(A) receptors is required for normal
RT assembly and function of GABAergic inhibitory synapses.";
RL J. Neurosci. 26:12758-12768(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18596047; DOI=10.1074/jbc.m802140200;
RA Greaves J., Salaun C., Fukata Y., Fukata M., Chamberlain L.H.;
RT "Palmitoylation and membrane interactions of the neuroprotective chaperone
RT cysteine-string protein.";
RL J. Biol. Chem. 283:25014-25026(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-157, AND ACTIVE SITE.
RX PubMed=19001095; DOI=10.1128/mcb.01144-08;
RA Tsutsumi R., Fukata Y., Noritake J., Iwanaga T., Perez F., Fukata M.;
RT "Identification of G protein alpha subunit-palmitoylating enzyme.";
RL Mol. Cell. Biol. 29:435-447(2009).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF VAL-61.
RX PubMed=19955568; DOI=10.1074/jbc.m109.069849;
RA Hines R.M., Kang R., Goytain A., Quamme G.A.;
RT "Golgi-specific DHHC zinc finger protein GODZ mediates membrane Ca2+
RT transport.";
RL J. Biol. Chem. 285:4621-4628(2010).
RN [11]
RP FUNCTION.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF CYS-157, AND ACTIVE
RP SITE.
RX PubMed=23793055; DOI=10.1074/jbc.m113.458794;
RA Lai J., Linder M.E.;
RT "Oligomerization of DHHC protein S-acyltransferases.";
RL J. Biol. Chem. 288:22862-22870(2013).
RN [13]
RP FUNCTION, AND AUTOPALMITOYLATION.
RX PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA Chamberlain L.H.;
RT "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT differences in substrate affinity and S-acylation activity.";
RL Mol. Biol. Cell 25:3870-3883(2014).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY,
RP PALMITOYLATION AT CYS-146, ACTIVE SITE, AND MUTAGENESIS OF CYS-129;
RP CYS-132; CYS-133 AND CYS-146.
RX PubMed=26487721; DOI=10.1074/jbc.m115.691147;
RA Gottlieb C.D., Zhang S., Linder M.E.;
RT "The Cysteine-rich Domain of the DHHC3 Palmitoyltransferase Is
RT Palmitoylated and Contains Tightly Bound Zinc.";
RL J. Biol. Chem. 290:29259-29269(2015).
RN [15]
RP FUNCTION.
RX PubMed=27613864; DOI=10.1074/jbc.m116.742767;
RA Murphy J., Kolandaivelu S.;
RT "Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates
RT Protein Stability and Localization.";
RL J. Biol. Chem. 291:23036-23046(2016).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27875292; DOI=10.1074/jbc.m116.732768;
RA Kilpatrick C.L., Murakami S., Feng M., Wu X., Lal R., Chen G., Du K.,
RA Luscher B.;
RT "Dissociation of Golgi-associated DHHC-type Zinc Finger Protein (GODZ)- and
RT Sertoli Cell Gene with a Zinc Finger Domain-beta (SERZ-beta)-mediated
RT Palmitoylation by Loss of Function Analyses in Knock-out Mice.";
RL J. Biol. Chem. 291:27371-27386(2016).
RN [17]
RP FUNCTION, PHOSPHORYLATION AT TYR-18, AUTOPALMITOYLATION, AND MUTAGENESIS OF
RP TYR-18; TYR-295 AND TYR-297.
RX PubMed=27247265; DOI=10.1128/mcb.00144-16;
RA Lievens P.M., Kuznetsova T., Kochlamazashvili G., Cesca F., Gorinski N.,
RA Galil D.A., Cherkas V., Ronkina N., Lafera J., Gaestel M., Ponimaskin E.,
RA Dityatev A.;
RT "ZDHHC3 Tyrosine Phosphorylation Regulates Neural Cell Adhesion Molecule
RT Palmitoylation.";
RL Mol. Cell. Biol. 36:2208-2225(2016).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP CYS-157 AND 182-ILE--LEU-184.
RX PubMed=28167757; DOI=10.1073/pnas.1612254114;
RA Greaves J., Munro K.R., Davidson S.C., Riviere M., Wojno J., Smith T.K.,
RA Tomkinson N.C., Chamberlain L.H.;
RT "Molecular basis of fatty acid selectivity in the zDHHC family of S-
RT acyltransferases revealed by click chemistry.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E1365-E1374(2017).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates (PubMed:15229235,
CC PubMed:15603741, PubMed:16129400, PubMed:19001095, PubMed:23793055,
CC PubMed:25253725, PubMed:26487721). Has no stringent fatty acid
CC selectivity and in addition to palmitate can also transfer onto target
CC proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (Probable). 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 (PubMed:19001095). 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 (PubMed:15229235,
CC PubMed:17151279, PubMed:27875292). Palmitoylates the neuronal protein
CC GAP43 which is also involved in the formation of GABAergic synapses
CC (PubMed:27875292). Palmitoylates NCDN thereby regulating its
CC association with endosome membranes (PubMed:23687301). Probably
CC palmitoylates PRCD and is involved in its proper localization within
CC the photoreceptor (PubMed:27613864). Could mediate the palmitoylation
CC of NCAM1 and regulate neurite outgrowth (PubMed:27247265). Could
CC palmitoylate DNAJC5 and regulate its localization to Golgi membranes
CC (PubMed:18596047). Also constitutively palmitoylates DLG4
CC (PubMed:15603741). May also palmitoylate SNAP25 (PubMed:25253725).
CC Could palmitoylate the glutamate receptors GRIA1 and GRIA2 but this has
CC not been confirmed in vivo (PubMed:16129400, PubMed:27875292). Could
CC also palmitoylate the D(2) dopamine receptor DRD2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NYG2, ECO:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:16129400,
CC ECO:0000269|PubMed:17151279, ECO:0000269|PubMed:18596047,
CC ECO:0000269|PubMed:19001095, ECO:0000269|PubMed:23687301,
CC ECO:0000269|PubMed:23793055, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:26487721, ECO:0000269|PubMed:27247265,
CC ECO:0000269|PubMed:27613864, ECO:0000269|PubMed:27875292,
CC ECO:0000305|PubMed:28167757}.
CC -!- FUNCTION: May also function as a calcium transporter.
CC {ECO:0000269|PubMed:19955568}.
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:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:19001095,
CC ECO:0000269|PubMed:23793055, ECO:0000269|PubMed:26487721};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:15229235};
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:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000305|PubMed:28167757};
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:0000305|PubMed:28167757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000305|PubMed:28167757};
CC -!- SUBUNIT: Monomer (PubMed:23793055). Homooligomers (PubMed:17151279,
CC PubMed:23793055). The monomeric form has a higher catalytic activity
CC (PubMed:23793055). Forms heterooligomers with ZDHHC7 (PubMed:17151279).
CC Interacts with TNFRSF10A (By similarity).
CC {ECO:0000250|UniProtKB:Q9NYG2, ECO:0000269|PubMed:17151279,
CC ECO:0000269|PubMed:23793055}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12163046, ECO:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:18596047}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the Golgi cis
CC cisterna. {ECO:0000269|PubMed:27875292}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain. In
CC the brain, expressed only in neurons (at protein level).
CC {ECO:0000269|PubMed:12163046, ECO:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:15603741}.
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:0000269|PubMed:27247265}.
CC -!- PTM: Autopalmitoylated. {ECO:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:27247265}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable, fertile and
CC do not display overt phenotype (PubMed:27875292). Male show a modest
CC reduction in body weight (PubMed:27875292). Zdhhc3 and Zdhhc7 double
CC knockout mice show a perinatally lethal phenotype (PubMed:27875292).
CC {ECO:0000269|PubMed:27875292}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB088044; BAC02941.1; -; mRNA.
DR EMBL; AY166672; AAO27359.1; -; mRNA.
DR EMBL; AK080541; BAC37939.1; -; mRNA.
DR EMBL; BC025126; AAH25126.1; -; mRNA.
DR EMBL; BC052464; AAH52464.1; -; mRNA.
DR CCDS; CCDS23654.1; -.
DR RefSeq; NP_081193.2; NM_026917.5.
DR AlphaFoldDB; Q8R173; -.
DR SMR; Q8R173; -.
DR IntAct; Q8R173; 1.
DR MINT; Q8R173; -.
DR STRING; 10090.ENSMUSP00000117392; -.
DR SwissLipids; SLP:000001950; -.
DR TCDB; 8.A.114.1.3; the huntington-interacting protein 14 (hip14) family.
DR iPTMnet; Q8R173; -.
DR PhosphoSitePlus; Q8R173; -.
DR SwissPalm; Q8R173; -.
DR EPD; Q8R173; -.
DR MaxQB; Q8R173; -.
DR PaxDb; Q8R173; -.
DR PeptideAtlas; Q8R173; -.
DR PRIDE; Q8R173; -.
DR ProteomicsDB; 302054; -.
DR Antibodypedia; 3251; 147 antibodies from 21 providers.
DR DNASU; 69035; -.
DR Ensembl; ENSMUST00000147563; ENSMUSP00000117392; ENSMUSG00000025786.
DR GeneID; 69035; -.
DR KEGG; mmu:69035; -.
DR UCSC; uc009sfq.2; mouse.
DR CTD; 51304; -.
DR MGI; MGI:1926134; Zdhhc3.
DR VEuPathDB; HostDB:ENSMUSG00000025786; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000155721; -.
DR HOGENOM; CLU_048061_1_1_1; -.
DR InParanoid; Q8R173; -.
DR OMA; CVVMTWL; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q8R173; -.
DR TreeFam; TF319798; -.
DR BRENDA; 2.3.1.225; 3474.
DR BioGRID-ORCS; 69035; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Zdhhc3; mouse.
DR PRO; PR:Q8R173; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8R173; protein.
DR Bgee; ENSMUSG00000025786; Expressed in granulocyte and 261 other tissues.
DR ExpressionAtlas; Q8R173; baseline and differential.
DR Genevisible; Q8R173; MM.
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; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IC:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IC:UniProtKB.
DR GO; GO:0044873; P:lipoprotein localization to membrane; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; IMP:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:1903546; P:protein localization to photoreceptor outer segment; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISS:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein 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_0000212863"
FT TOPO_DOM 1..47
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..72
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..214
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..177
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 ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:19001095,
FT ECO:0000269|PubMed:23793055, ECO:0000269|PubMed:26487721"
FT MOD_RES 18
FT /note="Phosphotyrosine; by FGFR1"
FT /evidence="ECO:0000269|PubMed:27247265"
FT LIPID 146
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:26487721"
FT MUTAGEN 18
FT /note="Y->F: Decreased phosphorylation by FGFR1."
FT /evidence="ECO:0000269|PubMed:27247265"
FT MUTAGEN 61
FT /note="V->R: Loss of function in calcium transport."
FT /evidence="ECO:0000269|PubMed:19955568"
FT MUTAGEN 129
FT /note="C->S: No effect on ZDHHC3 palmitoylation. Changed
FT protein structure. Decreased protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26487721"
FT MUTAGEN 132
FT /note="C->S: No effect on ZDHHC3 palmitoylation. Changed
FT protein structure. Decreased protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26487721"
FT MUTAGEN 133
FT /note="C->S: No effect on ZDHHC3 palmitoylation. No effect
FT on protein-cysteine S-palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26487721"
FT MUTAGEN 146
FT /note="C->S: Decreased ZDHHC3 palmitoylation. Changed
FT protein structure. Decreased protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26487721"
FT MUTAGEN 157
FT /note="C->S: Loss of protein-cysteine S-acyltransferase
FT activity. Loss of ZDHHC3 palmitoylation."
FT /evidence="ECO:0000269|PubMed:16129400,
FT ECO:0000269|PubMed:19001095, ECO:0000269|PubMed:23793055,
FT ECO:0000269|PubMed:28167757"
FT MUTAGEN 182..184
FT /note="ISL->SSV: Increased protein-cysteine S-
FT stearoyltransferase activity."
FT /evidence="ECO:0000305|PubMed:28167757"
FT MUTAGEN 295
FT /note="Y->F: Decreased phosphorylation by SRC and increased
FT autopalmitoylation; when associated with F-297."
FT /evidence="ECO:0000269|PubMed:27247265"
FT MUTAGEN 297
FT /note="Y->F: Decreased phosphorylation by SRC and increased
FT autopalmitoylation; when associated with F-295."
FT /evidence="ECO:0000269|PubMed:27247265"
FT CONFLICT 246
FT /note="E -> G (in Ref. 3; BAC37939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 34041 MW; BA93F65828A3B36C CRC64;
MMLIPTHHFR DIERKPEYLQ PEKCAPPPFP GPAGAMWFIR DGCGIACAIV TWFLVLYAEF
VVLFVMLVPS RDYAYSIING IVFNLLAFLA LASHCRAMLT DPGAVPKGNA TKEFIESLQL
KPGQVVYKCP KCCSIKPDRA HHCSVCKRCI RKMDHHCPWV NNCVGENNQK YFVLFTMYIA
LISLHALIMV GFHFLHCFEE DWTKCSSFSP PTTVILLILL CFEALLFLIF TSVMFGTQVH
SICTDETGIE QLKKEERRWA KKTKWMNMKA VFGHPFSLGW ASPFATPDQG KADPYQYVV
