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Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Huntingtin yeast partner H) (Huntingtin-interacting protein 14) (HIP-14) (Huntingtin-interacting protein 3) (HIP-3) (Huntingtin-interacting protein H) (Putative MAPK-activating protein PM11) (Putative NF-kappa-B-activating protein 205) (Zinc finger DHHC domain-containing protein 17) (DHHC-17)

 ZDH17_HUMAN             Reviewed;         632 AA.
Q8IUH5; B4DR39; O75407; Q7Z2I0; Q86W89; Q86YK0; Q9P088; Q9UPZ8;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=Palmitoyltransferase ZDHHC17 {ECO:0000305};
EC=2.3.1.225 {ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603740};
AltName: Full=Huntingtin yeast partner H {ECO:0000303|PubMed:9700202};
AltName: Full=Huntingtin-interacting protein 14 {ECO:0000303|PubMed:15489887};
Short=HIP-14 {ECO:0000303|PubMed:15489887};
AltName: Full=Huntingtin-interacting protein 3 {ECO:0000312|EMBL:BAC22089.1};
Short=HIP-3 {ECO:0000312|EMBL:BAC22089.1};
AltName: Full=Huntingtin-interacting protein H {ECO:0000303|PubMed:9700202};
AltName: Full=Putative MAPK-activating protein PM11 {ECO:0000305|PubMed:12761501};
AltName: Full=Putative NF-kappa-B-activating protein 205 {ECO:0000305|PubMed:12761501};
AltName: Full=Zinc finger DHHC domain-containing protein 17 {ECO:0000312|HGNC:HGNC:18412};
Short=DHHC-17 {ECO:0000303|PubMed:15603740};
Name=ZDHHC17 {ECO:0000312|HGNC:HGNC:18412};
Synonyms=HIP14 {ECO:0000303|PubMed:12393793},
HIP3 {ECO:0000312|EMBL:BAC22089.1}, HYPH {ECO:0000303|PubMed:9700202},
KIAA0946 {ECO:0000312|EMBL:BAA76790.1};
ORFNames=HSPC294 {ECO:0000312|EMBL:AAC26848.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HTT, TISSUE
SPECIFICITY, AND FUNCTION.
TISSUE=Brain;
PubMed=12393793; DOI=10.1093/hmg/11.23.2815;
Singaraja R.R., Hadano S., Metzler M., Givan S., Wellington C.L.,
Warby S., Yanai A., Gutekunst C.-A., Leavitt B.R., Yi H., Fichter K.,
Gan L., McGutcheon K., Chopra V., Michel J., Hersch S.M., Ikeda J.E.,
Hayden M.R.;
"HIP14, a novel ankyrin domain-containing protein, links huntingtin to
intracellular trafficking and endocytosis.";
Hum. Mol. Genet. 11:2815-2828(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Bone marrow, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-182, AND INTERACTION WITH HTT.
TISSUE=Testis;
PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
MacDonald M.E.;
"Huntingtin interacts with a family of WW domain proteins.";
Hum. Mol. Genet. 7:1463-1474(1998).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-203 (ISOFORM 3).
TISSUE=Umbilical cord blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, CATALYTIC ACTIVITY, DHHC DOMAIN, SUBCELLULAR LOCATION, AND
AUTOPALMITOYLATION.
PubMed=15603740; DOI=10.1016/j.neuron.2004.11.027;
Huang K., Yanai A., Kang R., Arstikaitis P., Singaraja R.R.,
Metzler M., Mullard A., Haigh B., Gauthier-Campbell C.,
Gutekunst C.-A., Hayden M.R., El-Husseini A.;
"Huntingtin-interacting protein HIP14 is a palmitoyl transferase
involved in palmitoylation and trafficking of multiple neuronal
proteins.";
Neuron 44:977-986(2004).
[9]
FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-467.
PubMed=15489887; DOI=10.1038/sj.onc.1208171;
Ducker C.E., Stettler E.M., French K.J., Upson J.J., Smith C.D.;
"Huntingtin interacting protein 14 is an oncogenic human protein:
palmitoyl acyltransferase.";
Oncogene 23:9230-9237(2004).
[10]
SUBCELLULAR LOCATION.
PubMed=18032660; DOI=10.1523/JNEUROSCI.2464-07.2007;
Stowers R.S., Isacoff E.Y.;
"Drosophila huntingtin-interacting protein 14 is a presynaptic protein
required for photoreceptor synaptic transmission and expression of the
palmitoylated proteins synaptosome-associated protein 25 and cysteine
string protein.";
J. Neurosci. 27:12874-12883(2007).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18794299; DOI=10.1074/jbc.M801469200;
Goytain A., Hines R.M., Quamme G.A.;
"Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual
functions, palmitoyl acyltransferase and Mg2+ transport.";
J. Biol. Chem. 283:33365-33374(2008).
[12]
FUNCTION.
PubMed=19139280; DOI=10.1128/MCB.00754-08;
Ding J., Du K.;
"ClipR-59 interacts with Akt and regulates Akt cellular
compartmentalization.";
Mol. Cell. Biol. 29:1459-1471(2009).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22496366; DOI=10.1074/jbc.M111.332981;
Lach A., Grzybek M., Heger E., Korycka J., Wolny M., Kubiak J.,
Kolondra A., Boguslawska D.M., Augoff K., Majkowski M., Podkalicka J.,
Kaczor J., Stefanko A., Kuliczkowski K., Sikorski A.F.;
"Palmitoylation of MPP1 (membrane-palmitoylated protein 1)/p55 is
crucial for lateral membrane organization in erythroid cells.";
J. Biol. Chem. 287:18974-18984(2012).
[14]
ANKYRIN REPEATS.
PubMed=25547411; DOI=10.1186/s12859-014-0440-9;
Chakrabarty B., Parekh N.;
"Identifying tandem Ankyrin repeats in protein structures.";
BMC Bioinformatics 15:6599-6599(2014).
[15]
INTERACTION WITH CLIP3; HTT AND MAP6.
PubMed=26198635; DOI=10.1074/jbc.M115.657668;
Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
"Identification of a novel sequence motif recognized by the ankyrin
repeat domain of zDHHC17/13 S-acyltransferases.";
J. Biol. Chem. 290:21939-21950(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 51-288, AND ANKYRIN REPEATS.
PubMed=19434754; DOI=10.1002/prot.22452;
Gao T., Collins R.E., Horton J.R., Zhang X., Zhang R., Dhayalan A.,
Tamas R., Jeltsch A., Cheng X.;
"The ankyrin repeat domain of Huntingtin interacting protein 14
contains a surface aromatic cage, a potential site for methyl-lysine
binding.";
Proteins 76:772-777(2009).
-!- FUNCTION: Palmitoyltransferase specific for a subset of neuronal
proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HD
(PubMed:15603740, PubMed:15489887, PubMed:19139280). Palmitoylates
MPP1 in erythrocytes (PubMed:22496366). May be involved in the
sorting or targeting of critical proteins involved in the
initiating events of endocytosis at the plasma membrane
(PubMed:12393793). May play a role in Mg(2+) transport
(PubMed:18794299). {ECO:0000269|PubMed:12393793,
ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603740,
ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19139280,
ECO:0000269|PubMed:22496366}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
[protein]-S-palmitoyl-L-cysteine + CoA.
{ECO:0000269|PubMed:15489887, ECO:0000269|PubMed:15603740}.
-!- SUBUNIT: Interacts (via ANK repeats) with CLIP3 (PubMed:26198635).
Interacts (via ANK repeats) with HTT; this interaction is
inversely correlated to the length of the polyglutamine tract
added to the huntingtin protein in Huntington disease
(PubMed:12393793, PubMed:9700202, PubMed:26198635). Interacts (via
ANK repeats) with DNAJC5 (via C-terminus) (By similarity).
Interacts (via ANK repeats) with MAP6 (PubMed:26198635). Interacts
(via ANK repeats) with SNAP23 (By similarity). Interacts (via ANK
repeats) with SNAP25 (By similarity).
{ECO:0000250|UniProtKB:Q80TN5, ECO:0000269|PubMed:12393793,
ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:9700202}.
-!- INTERACTION:
Self; NbExp=6; IntAct=EBI-524753, EBI-524753;
Q7Z783:-; NbExp=3; IntAct=EBI-524753, EBI-9088990;
Q7Z5R6:APBB1IP; NbExp=2; IntAct=EBI-524753, EBI-2818084;
Q9NP61:ARFGAP3; NbExp=2; IntAct=EBI-524753, EBI-2875816;
P15336:ATF2; NbExp=3; IntAct=EBI-524753, EBI-1170906;
Q9UQB8-3:BAIAP2; NbExp=3; IntAct=EBI-524753, EBI-9091996;
Q9UQB8-6:BAIAP2; NbExp=2; IntAct=EBI-524753, EBI-9092016;
P17655:CAPN2; NbExp=2; IntAct=EBI-524753, EBI-1028956;
Q96GN5-2:CDCA7L; NbExp=2; IntAct=EBI-524753, EBI-9091443;
P48730-2:CSNK1D; NbExp=3; IntAct=EBI-524753, EBI-9087876;
P68104:EEF1A1; NbExp=2; IntAct=EBI-524753, EBI-352162;
P60228:EIF3E; NbExp=2; IntAct=EBI-524753, EBI-347740;
Q9UI08-2:EVL; NbExp=2; IntAct=EBI-524753, EBI-6448852;
Q9UHY8:FEZ2; NbExp=4; IntAct=EBI-524753, EBI-396453;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-524753, EBI-618309;
Q9H4A5:GOLPH3L; NbExp=2; IntAct=EBI-524753, EBI-4403434;
P51674:GPM6A; NbExp=5; IntAct=EBI-524753, EBI-7187133;
P49840:GSK3A; NbExp=3; IntAct=EBI-524753, EBI-1044067;
P42858:HTT; NbExp=12; IntAct=EBI-524753, EBI-466029;
Q8IY31-3:IFT20; NbExp=3; IntAct=EBI-524753, EBI-9091197;
Q9NWB7:IFT57; NbExp=2; IntAct=EBI-524753, EBI-725672;
O60259:KLK8; NbExp=3; IntAct=EBI-524753, EBI-3915857;
Q14847-2:LASP1; NbExp=3; IntAct=EBI-524753, EBI-9088686;
Q96CV9-2:OPTN; NbExp=2; IntAct=EBI-524753, EBI-9091423;
Q08499-8:PDE4D; NbExp=2; IntAct=EBI-524753, EBI-9090666;
O15530-4:PDPK1; NbExp=3; IntAct=EBI-524753, EBI-9087775;
P27986-2:PIK3R1; NbExp=2; IntAct=EBI-524753, EBI-9090282;
Q9UF11-4:PLEKHB1; NbExp=4; IntAct=EBI-524753, EBI-9089825;
Q16537:PPP2R5E; NbExp=2; IntAct=EBI-524753, EBI-968374;
Q96DA2:RAB39B; NbExp=3; IntAct=EBI-524753, EBI-9089467;
Q15047-2:SETDB1; NbExp=3; IntAct=EBI-524753, EBI-9090795;
Q8IVB4:SLC9A9; NbExp=2; IntAct=EBI-524753, EBI-9092184;
O00161:SNAP23; NbExp=4; IntAct=EBI-524753, EBI-745000;
P60880:SNAP25; NbExp=3; IntAct=EBI-524753, EBI-524785;
Q7Z699:SPRED1; NbExp=3; IntAct=EBI-524753, EBI-5235340;
Q7Z698:SPRED2; NbExp=3; IntAct=EBI-524753, EBI-7082156;
O43597:SPRY2; NbExp=3; IntAct=EBI-524753, EBI-742487;
Q9C004:SPRY4; NbExp=2; IntAct=EBI-524753, EBI-354861;
Q8NFA0:USP32; NbExp=2; IntAct=EBI-524753, EBI-2511075;
Q9Y6W5:WASF2; NbExp=2; IntAct=EBI-524753, EBI-4290615;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:15603740, ECO:0000269|PubMed:18794299}; Multi-
pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:18794299}; Multi-pass membrane protein
{ECO:0000255}. Cell junction, synapse, presynaptic cell membrane
{ECO:0000269|PubMed:18032660}; Multi-pass membrane protein
{ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in
Golgi and in post-Golgi membrane vesicles.
{ECO:0000269|PubMed:18794299}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8IUH5-1; Sequence=Displayed;
Name=2;
IsoId=Q8IUH5-2; Sequence=VSP_010021, VSP_010022, VSP_010024,
VSP_010025;
Name=3;
IsoId=Q8IUH5-3; Sequence=VSP_010023;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all brain regions. Expression is
highest in the cortex, cerebellum, occipital lobe and caudate and
lowest in the spinal cord. Expression is also seen in testis,
pancreas, heart and kidney. ZDHHC17 is the only
palmitoyltransferase in erythrocytes.
{ECO:0000269|PubMed:12393793, ECO:0000269|PubMed:22496366}.
-!- DOMAIN: The DHHC domain is required for palmitoyltransferase
activity. {ECO:0000269|PubMed:15603740}.
-!- PTM: Autopalmitoylated (PubMed:15603740, PubMed:18794299).
Autopalmitoylation has a regulatory role in ZDHHC17-mediated
Mg(2+) transport (PubMed:18794299). {ECO:0000269|PubMed:15603740,
ECO:0000269|PubMed:18794299}.
-!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
AKR/ZDHHC17 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28972.1; Type=Frameshift; Positions=183, 191; Evidence={ECO:0000305};
Sequence=AAH30990.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA76790.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAC77366.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC77388.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB024494; BAC22089.1; -; mRNA.
EMBL; AB023163; BAA76790.1; ALT_INIT; mRNA.
EMBL; AB097013; BAC77366.1; ALT_INIT; mRNA.
EMBL; AB097035; BAC77388.1; ALT_INIT; mRNA.
EMBL; AK299089; BAG61151.1; -; mRNA.
EMBL; BC030990; AAH30990.1; ALT_INIT; mRNA.
EMBL; BC050324; AAH50324.1; -; mRNA.
EMBL; AF049612; AAC26848.1; -; mRNA.
EMBL; AF161412; AAF28972.1; ALT_FRAME; mRNA.
CCDS; CCDS44946.1; -. [Q8IUH5-1]
RefSeq; NP_056151.2; NM_015336.2. [Q8IUH5-1]
UniGene; Hs.4014; -.
PDB; 3EU9; X-ray; 1.99 A; A/B/C=51-288.
PDB; 5W7I; X-ray; 2.10 A; A/C=50-284.
PDB; 5W7J; X-ray; 2.20 A; A/C=50-284.
PDBsum; 3EU9; -.
PDBsum; 5W7I; -.
PDBsum; 5W7J; -.
ProteinModelPortal; Q8IUH5; -.
SMR; Q8IUH5; -.
BioGrid; 116965; 250.
IntAct; Q8IUH5; 227.
MINT; MINT-1537511; -.
STRING; 9606.ENSP00000403397; -.
TCDB; 9.B.37.1.1; the huntington-interacting protein 14 (hip14) family.
iPTMnet; Q8IUH5; -.
PhosphoSitePlus; Q8IUH5; -.
SwissPalm; Q8IUH5; -.
BioMuta; ZDHHC17; -.
DMDM; 46395885; -.
EPD; Q8IUH5; -.
MaxQB; Q8IUH5; -.
PaxDb; Q8IUH5; -.
PeptideAtlas; Q8IUH5; -.
PRIDE; Q8IUH5; -.
Ensembl; ENST00000426126; ENSP00000403397; ENSG00000186908. [Q8IUH5-1]
GeneID; 23390; -.
KEGG; hsa:23390; -.
UCSC; uc001syk.2; human. [Q8IUH5-1]
CTD; 23390; -.
DisGeNET; 23390; -.
EuPathDB; HostDB:ENSG00000186908.14; -.
GeneCards; ZDHHC17; -.
HGNC; HGNC:18412; ZDHHC17.
HPA; HPA016807; -.
MIM; 607799; gene.
neXtProt; NX_Q8IUH5; -.
OpenTargets; ENSG00000186908; -.
PharmGKB; PA134991292; -.
eggNOG; KOG0509; Eukaryota.
eggNOG; COG0666; LUCA.
eggNOG; COG5273; LUCA.
GeneTree; ENSGT00530000063074; -.
HOVERGEN; HBG051907; -.
InParanoid; Q8IUH5; -.
KO; K20032; -.
OMA; QAKGYDS; -.
OrthoDB; EOG091G056H; -.
PhylomeDB; Q8IUH5; -.
TreeFam; TF317342; -.
BRENDA; 2.3.1.225; 2681.
ChiTaRS; ZDHHC17; human.
EvolutionaryTrace; Q8IUH5; -.
GeneWiki; ZDHHC17; -.
GenomeRNAi; 23390; -.
PRO; PR:Q8IUH5; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000186908; -.
CleanEx; HS_ZDHHC17; -.
ExpressionAtlas; Q8IUH5; baseline and differential.
Genevisible; Q8IUH5; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0042953; P:lipoprotein transport; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 2.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR001594; Palmitoyltrfase_DHHC.
InterPro; IPR030289; ZDHHC17.
PANTHER; PTHR24161:SF18; PTHR24161:SF18; 1.
Pfam; PF12796; Ank_2; 2.
Pfam; PF01529; DHHC; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
PROSITE; PS50216; DHHC; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Alternative splicing; ANK repeat;
Cell junction; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Golgi apparatus; Lipoprotein; Membrane; Palmitate; Polymorphism;
Reference proteome; Repeat; Synapse; Transferase; Transmembrane;
Transmembrane helix; Tumor suppressor.
CHAIN 1 632 Palmitoyltransferase ZDHHC17.
/FTId=PRO_0000212900.
TOPO_DOM 1 304 Cytoplasmic. {ECO:0000255}.
TRANSMEM 305 325 Helical. {ECO:0000255}.
TRANSMEM 326 346 Helical. {ECO:0000255}.
TOPO_DOM 347 357 Cytoplasmic. {ECO:0000255}.
TRANSMEM 358 378 Helical. {ECO:0000255}.
TOPO_DOM 379 381 Lumenal. {ECO:0000255}.
TRANSMEM 382 402 Helical. {ECO:0000255}.
TOPO_DOM 403 480 Cytoplasmic. {ECO:0000255}.
TRANSMEM 481 501 Helical. {ECO:0000255}.
TOPO_DOM 502 529 Lumenal. {ECO:0000255}.
TRANSMEM 530 550 Helical. {ECO:0000255}.
TOPO_DOM 551 632 Cytoplasmic. {ECO:0000255}.
REPEAT 51 86 ANK 1. {ECO:0000305|PubMed:19434754}.
REPEAT 89 118 ANK 2. {ECO:0000255}.
REPEAT 123 152 ANK 3. {ECO:0000255}.
REPEAT 156 185 ANK 4. {ECO:0000255}.
REPEAT 189 219 ANK 5. {ECO:0000255}.
REPEAT 224 253 ANK 6. {ECO:0000255}.
REPEAT 257 286 ANK 7. {ECO:0000255}.
DOMAIN 437 487 DHHC. {ECO:0000255|PROSITE-
ProRule:PRU00067}.
REGION 11 305 Necessary and sufficient for interaction
with DNAJC5 and SNAP25.
{ECO:0000250|UniProtKB:Q80TN5}.
ACT_SITE 467 467 S-palmitoyl cysteine intermediate.
{ECO:0000305|PubMed:15489887}.
VAR_SEQ 1 50 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010021.
VAR_SEQ 51 66 THIDDYSTWDIVKATQ -> MSTIPKRAVCPFSTQR (in
isoform 2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010022.
VAR_SEQ 204 632 Missing (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_010023.
VAR_SEQ 258 266 GESALDLAK -> AILRCHMAL (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010024.
VAR_SEQ 267 632 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_010025.
VARIANT 383 383 N -> S (in dbSNP:rs33996476).
/FTId=VAR_052978.
MUTAGEN 467 467 C->S: Abolishes palmitoyltransferase
activity. {ECO:0000269|PubMed:15489887}.
CONFLICT 3 3 R -> G (in Ref. 7; AAF28972).
{ECO:0000305}.
CONFLICT 39 39 Y -> F (in Ref. 1; BAC22089).
{ECO:0000305}.
CONFLICT 173 173 V -> VV (in Ref. 1; BAC22089).
{ECO:0000305}.
CONFLICT 182 182 D -> E (in Ref. 7; AAF28972).
{ECO:0000305}.
HELIX 56 58 {ECO:0000244|PDB:3EU9}.
HELIX 61 66 {ECO:0000244|PDB:3EU9}.
HELIX 70 78 {ECO:0000244|PDB:3EU9}.
HELIX 93 99 {ECO:0000244|PDB:3EU9}.
HELIX 103 111 {ECO:0000244|PDB:3EU9}.
TURN 121 124 {ECO:0000244|PDB:3EU9}.
HELIX 127 134 {ECO:0000244|PDB:3EU9}.
HELIX 137 145 {ECO:0000244|PDB:3EU9}.
HELIX 160 166 {ECO:0000244|PDB:3EU9}.
HELIX 170 178 {ECO:0000244|PDB:3EU9}.
HELIX 193 200 {ECO:0000244|PDB:3EU9}.
HELIX 207 212 {ECO:0000244|PDB:3EU9}.
TURN 222 224 {ECO:0000244|PDB:3EU9}.
HELIX 228 235 {ECO:0000244|PDB:3EU9}.
HELIX 238 247 {ECO:0000244|PDB:3EU9}.
HELIX 261 267 {ECO:0000244|PDB:3EU9}.
HELIX 271 280 {ECO:0000244|PDB:3EU9}.
SEQUENCE 632 AA; 72640 MW; 3FD5FD592F2C617F CRC64;
MQREEGFNTK MADGPDEYDT EAGCVPLLHP EEIKPQSHYN HGYGEPLGRK THIDDYSTWD
IVKATQYGIY ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG
GDLNSTPLHW ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG
QDVDMMDQNG MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV
ISLLLEAGAN VDAQNIKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE
FRQKVMLGTP FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF DHSMHSALPL
GIYLATKFWM YVTWFFWFWN DLNFLFIHLP FLANSVALFY NFGKSWKSDP GIIKATEEQK
KKTIVELAET GSLDLSIFCS TCLIRKPVRS KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR
YFMGYLFFLL FMICWMIYGC ISYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF
HFMWVAVLLM CQMYQISCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF
RCCGLFRPVI VDWTRQYTIE YDQISGSGYQ LV


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