ZDH18_HUMAN
ID ZDH18_HUMAN Reviewed; 388 AA.
AC Q9NUE0; A6NHY9; B4DQ84; Q5JYH0; Q9H020;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Palmitoyltransferase ZDHHC18 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:23034182, ECO:0000269|PubMed:27481942};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 18 {ECO:0000303|PubMed:16647879};
DE Short=DHHC-18 {ECO:0000303|PubMed:16647879};
DE AltName: Full=Zinc finger DHHC domain-containing protein 18 {ECO:0000312|HGNC:HGNC:20712};
GN Name=ZDHHC18 {ECO:0000312|HGNC:HGNC:20712};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-388 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT "Intracellular localization and tissue-specific distribution of human and
RT yeast DHHC cysteine-rich domain-containing proteins.";
RL Biochim. Biophys. Acta 1761:474-483(2006).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23034182; DOI=10.1091/mbc.e12-05-0336;
RA Ohno Y., Kashio A., Ogata R., Ishitomi A., Yamazaki Y., Kihara A.;
RT "Analysis of substrate specificity of human DHHC protein acyltransferases
RT using a yeast expression system.";
RL Mol. Biol. Cell 23:4543-4551(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27481942; DOI=10.1074/jbc.m116.725762;
RA Adachi N., Hess D.T., McLaughlin P., Stamler J.S.;
RT "S-Palmitoylation of a Novel Site in the beta2-Adrenergic Receptor
RT Associated with a Novel Intracellular Itinerary.";
RL J. Biol. Chem. 291:20232-20246(2016).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:23034182,
CC PubMed:27481942). Palmitoylates HRAS and LCK (By similarity). May also
CC have a palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling (PubMed:27481942). {ECO:0000250|UniProtKB:Q5Y5T2,
CC ECO:0000269|PubMed:23034182, ECO:0000269|PubMed:27481942}.
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:23034182,
CC ECO:0000269|PubMed:27481942};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:27481942};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:16647879}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NUE0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NUE0-2; Sequence=VSP_056000;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16647879}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AK298683; BAG60846.1; -; mRNA.
DR EMBL; AL034380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07788.1; -; Genomic_DNA.
DR EMBL; BC066776; AAH66776.1; -; mRNA.
DR EMBL; AL512765; CAC21682.1; -; mRNA.
DR CCDS; CCDS30650.1; -. [Q9NUE0-1]
DR RefSeq; NP_115659.1; NM_032283.2. [Q9NUE0-1]
DR AlphaFoldDB; Q9NUE0; -.
DR SMR; Q9NUE0; -.
DR BioGRID; 123972; 73.
DR IntAct; Q9NUE0; 22.
DR MINT; Q9NUE0; -.
DR STRING; 9606.ENSP00000363257; -.
DR iPTMnet; Q9NUE0; -.
DR PhosphoSitePlus; Q9NUE0; -.
DR SwissPalm; Q9NUE0; -.
DR BioMuta; ZDHHC18; -.
DR DMDM; 34395910; -.
DR EPD; Q9NUE0; -.
DR jPOST; Q9NUE0; -.
DR MassIVE; Q9NUE0; -.
DR PaxDb; Q9NUE0; -.
DR PeptideAtlas; Q9NUE0; -.
DR PRIDE; Q9NUE0; -.
DR ProteomicsDB; 4855; -.
DR ProteomicsDB; 82667; -. [Q9NUE0-1]
DR Antibodypedia; 46760; 97 antibodies from 24 providers.
DR DNASU; 84243; -.
DR Ensembl; ENST00000374141.6; ENSP00000363256.2; ENSG00000204160.12. [Q9NUE0-2]
DR Ensembl; ENST00000374142.9; ENSP00000363257.3; ENSG00000204160.12. [Q9NUE0-1]
DR GeneID; 84243; -.
DR KEGG; hsa:84243; -.
DR MANE-Select; ENST00000374142.9; ENSP00000363257.3; NM_032283.3; NP_115659.1.
DR UCSC; uc001bnb.4; human. [Q9NUE0-1]
DR CTD; 84243; -.
DR DisGeNET; 84243; -.
DR GeneCards; ZDHHC18; -.
DR HGNC; HGNC:20712; ZDHHC18.
DR HPA; ENSG00000204160; Tissue enhanced (bone).
DR neXtProt; NX_Q9NUE0; -.
DR OpenTargets; ENSG00000204160; -.
DR PharmGKB; PA134968241; -.
DR VEuPathDB; HostDB:ENSG00000204160; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156585; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; Q9NUE0; -.
DR OMA; HLTIFIP; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q9NUE0; -.
DR TreeFam; TF312923; -.
DR PathwayCommons; Q9NUE0; -.
DR SignaLink; Q9NUE0; -.
DR BioGRID-ORCS; 84243; 22 hits in 1084 CRISPR screens.
DR ChiTaRS; ZDHHC18; human.
DR GenomeRNAi; 84243; -.
DR Pharos; Q9NUE0; Tdark.
DR PRO; PR:Q9NUE0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NUE0; protein.
DR Bgee; ENSG00000204160; Expressed in blood and 158 other tissues.
DR ExpressionAtlas; Q9NUE0; baseline and differential.
DR Genevisible; Q9NUE0; HS.
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:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Palmitoyltransferase ZDHHC18"
FT /id="PRO_0000212902"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..119
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..277
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 192..242
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..46
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056000"
SQ SEQUENCE 388 AA; 42031 MW; 446114704C461C6E CRC64;
MKDCEYQQIS PGAAPLPASP GARRPGPAAS PTPGPGPAPP AAPAPPRWSS SGSGSGSGSG
SLGRRPRRKW EVFPGRNRFY CGGRLMLAGH GGVFALTLLL ILTTTGLFFV FDCPYLARKL
TLAIPIIAAI LFFFVMSCLL QTSFTDPGIL PRATVCEAAA LEKQIDNTGS STYRPPPRTR
EVLINGQMVK LKYCFTCKMF RPPRTSHCSV CDNCVERFDH HCPWVGNCVG RRNYRFFYAF
ILSLSFLTAF IFACVVTHLT LRAQGSNFLS TLKETPASVL ELVICFFSIW SILGLSGFHT
YLVASNLTTN EDIKGSWSSK RGGEASVNPY SHKSIITNCC AVLCGPLPPS LIDRRGFVQS
DTVLPSPIRS DEPACRAKPD ASMVGGHP
