ZDH18_MOUSE
ID ZDH18_MOUSE Reviewed; 380 AA.
AC Q5Y5T2; A2A9F0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Palmitoyltransferase ZDHHC18 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000305|PubMed:15603741};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 18 {ECO:0000303|PubMed:15603741};
DE Short=DHHC-18 {ECO:0000303|PubMed:15603741};
DE AltName: Full=Zinc finger DHHC domain-containing protein 18 {ECO:0000312|MGI:MGI:3527792};
GN Name=Zdhhc18 {ECO:0000312|MGI:MGI:3527792};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-380.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-227.
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 [MRNA] OF 128-380, FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:15603741).
CC Palmitoylates HRAS and LCK (PubMed:15603741). May also have a
CC palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling (By similarity). {ECO:0000250|UniProtKB:Q9NUE0,
CC ECO:0000269|PubMed:15603741}.
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:0000305|PubMed:15603741};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:15603741};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NUE0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:15603741}.
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; AL627228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX537327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BF582271; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CJ065144; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY668950; AAU89704.1; -; mRNA.
DR CCDS; CCDS38906.1; -.
DR RefSeq; NP_001017968.2; NM_001017968.2.
DR AlphaFoldDB; Q5Y5T2; -.
DR SMR; Q5Y5T2; -.
DR STRING; 10090.ENSMUSP00000081260; -.
DR iPTMnet; Q5Y5T2; -.
DR PhosphoSitePlus; Q5Y5T2; -.
DR SwissPalm; Q5Y5T2; -.
DR EPD; Q5Y5T2; -.
DR MaxQB; Q5Y5T2; -.
DR PaxDb; Q5Y5T2; -.
DR PeptideAtlas; Q5Y5T2; -.
DR PRIDE; Q5Y5T2; -.
DR ProteomicsDB; 302050; -.
DR Antibodypedia; 46760; 97 antibodies from 24 providers.
DR DNASU; 503610; -.
DR Ensembl; ENSMUST00000084238; ENSMUSP00000081260; ENSMUSG00000037553.
DR GeneID; 503610; -.
DR KEGG; mmu:503610; -.
DR UCSC; uc008vde.1; mouse.
DR CTD; 84243; -.
DR MGI; MGI:3527792; Zdhhc18.
DR VEuPathDB; HostDB:ENSMUSG00000037553; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156585; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; Q5Y5T2; -.
DR OMA; HLTIFIP; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q5Y5T2; -.
DR TreeFam; TF312923; -.
DR BioGRID-ORCS; 503610; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Zdhhc18; mouse.
DR PRO; PR:Q5Y5T2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q5Y5T2; protein.
DR Bgee; ENSMUSG00000037553; Expressed in granulocyte and 214 other tissues.
DR Genevisible; Q5Y5T2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS: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:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0018345; P:protein palmitoylation; ISO:MGI.
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; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..380
FT /note="Palmitoyltransferase ZDHHC18"
FT /id="PRO_0000212903"
FT TOPO_DOM 1..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..111
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..269
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 184..234
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
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:19144319"
SQ SEQUENCE 380 AA; 41148 MW; 91311320F4AE505C CRC64;
MKDCEYQQIS PGAAPPPASP GARRPGPAAP PAPSPGPAPG APRWSGSGSG SGSLGRRPRR
KWEVFPGRNR FYCGGRLMLA GHGGVFALTL LLILSTTILF FVFDCPYLAR TLTLAIPIIA
AILFFFVMSC LLQTSFTDPG ILPRATICEA AALEKQIDNT GSSTYRPPPR TREVMINGQT
VKLKYCFTCK MFRPPRTSHC SVCDNCVERF DHHCPWVGNC VGRRNYRFFY AFILSLSFLT
AFIFACVVTH LTLLSQGSNF LSALKKTPAS VLELVICFFS IWSILGLSGF HTYLVASNLT
TNEDIKGSWS SKRGGEASVN PYSHKSIITN CCAVLCGPLP PSLIDRRGFV QSDTALPSPI
RSDDPACGAK PDASMVGGHP
