ZDH17_MOUSE
ID ZDH17_MOUSE Reviewed; 632 AA.
AC Q80TN5; Q8BJ08; Q8BYQ2; Q8BYQ6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Palmitoyltransferase ZDHHC17 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:25253725};
DE AltName: Full=Acyltransferase ZDHHC17 {ECO:0000305|PubMed:28167757};
DE EC=2.3.1.- {ECO:0000305|PubMed:28167757};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 17 {ECO:0000305|PubMed:15603741};
DE Short=DHHC-17 {ECO:0000303|PubMed:15603741};
DE AltName: Full=Huntingtin-interacting protein 14 {ECO:0000303|PubMed:15489887};
DE AltName: Full=Zinc finger DHHC domain-containing protein 17 {ECO:0000312|MGI:MGI:2445110};
GN Name=Zdhhc17 {ECO:0000312|MGI:MGI:2445110};
GN Synonyms=Hip14 {ECO:0000303|PubMed:12393793, ECO:0000303|PubMed:27911442},
GN Kiaa0946 {ECO:0000312|EMBL:BAC65688.1};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-632 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-418 (ISOFORMS 1/2).
RC TISSUE=Eye;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=12393793; DOI=10.1093/hmg/11.23.2815;
RA Singaraja R.R., Hadano S., Metzler M., Givan S., Wellington C.L., Warby S.,
RA Yanai A., Gutekunst C.-A., Leavitt B.R., Yi H., Fichter K., Gan L.,
RA McGutcheon K., Chopra V., Michel J., Hersch S.M., Ikeda J.E., Hayden M.R.;
RT "HIP14, a novel ankyrin domain-containing protein, links huntingtin to
RT intracellular trafficking and endocytosis.";
RL Hum. Mol. Genet. 11:2815-2828(2002).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
RX PubMed=15489887; DOI=10.1038/sj.onc.1208171;
RA Ducker C.E., Stettler E.M., French K.J., Upson J.J., Smith C.D.;
RT "Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl
RT acyltransferase.";
RL Oncogene 23:9230-9237(2004).
RN [7]
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 [8]
RP INDUCTION.
RX PubMed=18794299; DOI=10.1074/jbc.m801469200;
RA Goytain A., Hines R.M., Quamme G.A.;
RT "Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions,
RT palmitoyl acyltransferase and Mg2+ transport.";
RL J. Biol. Chem. 283:33365-33374(2008).
RN [9]
RP INTERACTION WITH SPRED1 AND SPRED3.
RX PubMed=24705354; DOI=10.1093/hmg/ddu137;
RA Butland S.L., Sanders S.S., Schmidt M.E., Riechers S.P., Lin D.T.,
RA Martin D.D., Vaid K., Graham R.K., Singaraja R.R., Wanker E.E.,
RA Conibear E., Hayden M.R.;
RT "The palmitoyl acyltransferase HIP14 shares a high proportion of
RT interactors with huntingtin: implications for a role in the pathogenesis of
RT Huntington's disease.";
RL Hum. Mol. Genet. 23:4142-4160(2014).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH DNAJC5 AND SNAP25,
RP MUTAGENESIS OF HIS-465 AND CYS-467, REGION, AND SUBCELLULAR LOCATION.
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 [11]
RP INTERACTION WITH CLIP3; DNAJC5; HTT; MAP6; SNAP23 AND SNAP25.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [12]
RP FUNCTION, INTERACTION WITH NTRK1, AND DEVELOPMENTAL STAGE.
RX PubMed=26232532; DOI=10.1016/j.mcn.2015.07.005;
RA Shi W., Wang F., Gao M., Yang Y., Du Z., Wang C., Yao Y., He K., Chen X.,
RA Hao A.;
RT "ZDHHC17 promotes axon outgrowth by regulating TrkA-tubulin complex
RT formation.";
RL Mol. Cell. Neurosci. 68:194-202(2015).
RN [13]
RP FUNCTION.
RX PubMed=27911442; DOI=10.1038/cdd.2016.139;
RA Skotte N.H., Sanders S.S., Singaraja R.R., Ehrnhoefer D.E., Vaid K.,
RA Qiu X., Kannan S., Verma C., Hayden M.R.;
RT "Palmitoylation of caspase-6 by HIP14 regulates its activation.";
RL Cell Death Differ. 24:433-444(2017).
RN [14]
RP INTERACTION WITH SPRED2.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
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: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and is involved in a variety of
CC cellular processes (PubMed:15489887, PubMed:15603741, PubMed:25253725,
CC PubMed:27911442). Has no stringent fatty acid selectivity and in
CC addition to palmitate can also transfer onto target proteins myristate
CC from tetradecanoyl-CoA and stearate from octadecanoyl-CoA
CC (PubMed:28167757). Palmitoyltransferase specific for a subset of
CC neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT
CC (PubMed:15489887, PubMed:15603741, PubMed:25253725). Also palmitoylates
CC neuronal protein GPM6A as well as SPRED1 and SPRED3 (By similarity).
CC Could also play a role in axonogenesis through the regulation of NTRK1
CC and the downstream ERK1/ERK2 signaling cascade (PubMed:26232532). May
CC be involved in the sorting or targeting of critical proteins involved
CC in the initiating events of endocytosis at the plasma membrane (By
CC similarity). May play a role in Mg(2+) transport (By similarity). Could
CC also palmitoylate DNAJC5 and regulate its localization to the Golgi
CC membrane (PubMed:18596047). Palmitoylates CASP6, thereby preventing its
CC dimerization and subsequent activation (PubMed:27911442).
CC {ECO:0000250|UniProtKB:Q8IUH5, ECO:0000269|PubMed:18596047,
CC ECO:0000269|PubMed:26232532, ECO:0000269|PubMed:27911442,
CC ECO:0000305|PubMed:28167757}.
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:15489887,
CC ECO:0000269|PubMed:15603741, ECO:0000269|PubMed:25253725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:15489887, ECO:0000305|PubMed:15603741,
CC ECO:0000305|PubMed:25253725};
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: Interacts (via ANK repeats) with numerous proteins (via the
CC consensus sequence motif [VIAP]-[VIT]-x-x-Q-P) (By similarity).
CC Interacts (via ANK repeats) with CLIP3 (PubMed:26198635). Interacts
CC (via ANK repeats) with HTT (PubMed:26198635). Interacts (via ANK
CC repeats) with DNAJC5 (via C-terminus) (PubMed:25253725,
CC PubMed:26198635). Interacts (via ANK repeats) with MAP6
CC (PubMed:26198635). Interacts (via ANK repeats) with SNAP23
CC (PubMed:26198635). Interacts (via ANK repeats) with SNAP25
CC (PubMed:25253725, PubMed:26198635). Interacts (via ANK repeats) with
CC EVL (By similarity). Interacts with SPRED1 and SPRED3
CC (PubMed:24705354). Interacts with GPM6A and OPTN (By similarity). May
CC interact (via ANK repeats) with SPRED2 (PubMed:28882895). May interact
CC with NTRK1; may regulate its localization and function
CC (PubMed:26232532). {ECO:0000250|UniProtKB:Q8IUH5,
CC ECO:0000269|PubMed:24705354, ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:26232532,
CC ECO:0000269|PubMed:28882895}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:25253725}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi
CC and in post-Golgi membrane vesicles. {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80TN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TN5-2; Sequence=VSP_010026, VSP_010027;
CC -!- TISSUE SPECIFICITY: Expressed in liver, testis, kidney, heart, pancreas
CC and brain. Highest expression was seen in the brain. Localized
CC predominantly in the perinuclear regions of neurons from the cortex,
CC striatum and hippocampus. Colocalized with HTT in the medium spiny
CC neurons of the striatum and the spiny neurons that project into the
CC globus pallidus. {ECO:0000269|PubMed:12393793}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in neurons during their
CC differentiation. {ECO:0000269|PubMed:26232532}.
CC -!- INDUCTION: Up-regulated by low extracellular Mg(2+).
CC {ECO:0000269|PubMed:18794299}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. Autopalmitoylation has a regulatory role in
CC ZDHHC17-mediated Mg(2+) transport. {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH58772.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC30090.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC30097.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC32912.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC65688.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122406; BAC65688.1; ALT_INIT; mRNA.
DR EMBL; AK038670; BAC30090.2; ALT_INIT; mRNA.
DR EMBL; AK038681; BAC30097.2; ALT_INIT; mRNA.
DR EMBL; AK046891; BAC32912.1; ALT_INIT; mRNA.
DR EMBL; BC058772; AAH58772.1; ALT_SEQ; mRNA.
DR CCDS; CCDS56748.1; -. [Q80TN5-1]
DR RefSeq; NP_766142.2; NM_172554.2. [Q80TN5-1]
DR AlphaFoldDB; Q80TN5; -.
DR SMR; Q80TN5; -.
DR BioGRID; 235798; 2.
DR STRING; 10090.ENSMUSP00000043279; -.
DR iPTMnet; Q80TN5; -.
DR PhosphoSitePlus; Q80TN5; -.
DR SwissPalm; Q80TN5; -.
DR MaxQB; Q80TN5; -.
DR PaxDb; Q80TN5; -.
DR PeptideAtlas; Q80TN5; -.
DR PRIDE; Q80TN5; -.
DR ProteomicsDB; 275138; -. [Q80TN5-1]
DR ProteomicsDB; 275139; -. [Q80TN5-2]
DR Antibodypedia; 8807; 201 antibodies from 35 providers.
DR DNASU; 320150; -.
DR Ensembl; ENSMUST00000041723; ENSMUSP00000043279; ENSMUSG00000035798. [Q80TN5-1]
DR GeneID; 320150; -.
DR KEGG; mmu:320150; -.
DR UCSC; uc007gzw.2; mouse. [Q80TN5-2]
DR UCSC; uc033fsq.1; mouse. [Q80TN5-1]
DR CTD; 23390; -.
DR MGI; MGI:2445110; Zdhhc17.
DR VEuPathDB; HostDB:ENSMUSG00000035798; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; Q80TN5; -.
DR OMA; PWMAGIF; -.
DR PhylomeDB; Q80TN5; -.
DR TreeFam; TF317342; -.
DR BioGRID-ORCS; 320150; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Zdhhc17; mouse.
DR PRO; PR:Q80TN5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q80TN5; protein.
DR Bgee; ENSMUSG00000035798; Expressed in retinal neural layer and 223 other tissues.
DR ExpressionAtlas; Q80TN5; baseline and differential.
DR Genevisible; Q80TN5; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IC:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IC:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISO:MGI.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030289; ZDHHC17.
DR PANTHER; PTHR24161:SF18; PTHR24161:SF18; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; ANK repeat; Cell membrane;
KW Cell projection; Cytoplasmic vesicle; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Repeat; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Tumor suppressor.
FT CHAIN 1..632
FT /note="Palmitoyltransferase ZDHHC17"
FT /id="PRO_0000212901"
FT TOPO_DOM 1..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..381
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..529
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 51..86
FT /note="ANK 1"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT REPEAT 89..118
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 123..152
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 156..185
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 189..219
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 224..253
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 257..286
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT DOMAIN 437..487
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 11..305
FT /note="Necessary and sufficient for interaction with DNAJC5
FT and SNAP25"
FT /evidence="ECO:0000269|PubMed:25253725"
FT ACT_SITE 467
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT VAR_SEQ 423..429
FT /note="TIVELAE -> VVMYPAN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010026"
FT VAR_SEQ 430..632
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_010027"
FT MUTAGEN 465
FT /note="H->Q: Loss of palmitoyltransferase activity toward
FT DNAJC5 and SNAP25."
FT /evidence="ECO:0000269|PubMed:25253725"
FT MUTAGEN 467
FT /note="C->A: No effect on interaction with DNAJC5 and
FT SNAP25."
FT /evidence="ECO:0000269|PubMed:25253725"
FT CONFLICT 288
FT /note="N -> K (in Ref. 1; BAC32912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 632 AA; 72621 MW; 323EFD47790750DC CRC64;
MQREEGFNTK MADGPDEYET ETGCVPLLHP EEIKPQSHYN HGYGEPLGRK THIDDYSTWD
IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG
GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG
QDVDMMDQNG MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV
ISLLLEAGGN VDAQNVKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE
FRQKVMLGTP FLVIWLVGFI ADLDIDSWLI KGLMYGGVWA TVQFLSKSFF DHSMHSALPL
GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY NFGKSWKSDP GIIKATEEQK
KKTIVELAET GSLDLSIFCS TCLIRKPVRS KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR
YFMGYLFFLL FMICWMIYGC VSYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF
HFLWVAVLLM CQLYQITCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF
RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV
