ZDH20_MOUSE
ID ZDH20_MOUSE Reviewed; 380 AA.
AC Q5Y5T1; Q3TDL1; Q8VCL6; Q9D3Q8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Palmitoyltransferase ZDHHC20 {ECO:0000305|PubMed:15603741};
DE EC=2.3.1.225 {ECO:0000305|PubMed:15603741};
DE AltName: Full=Acyltransferase ZDHHC20 {ECO:0000250|UniProtKB:Q5W0Z9};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5W0Z9};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 20 {ECO:0000303|PubMed:15603741};
DE Short=DHHC-20 {ECO:0000303|PubMed:15603741};
DE AltName: Full=Zinc finger DHHC domain-containing protein 20 {ECO:0000312|MGI:MGI:1923215};
GN Name=Zdhhc20 {ECO:0000312|MGI:MGI:1923215};
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] (ISOFORM 1), 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Forelimb, Ovary, and Uterus;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:15603741). Catalyzes
CC palmitoylation of Cys residues in the cytoplasmic C-terminus of EGFR,
CC and modulates the duration of EGFR signaling by modulating
CC palmitoylation-dependent EGFR internalization and degradation. Has a
CC preference for acyl-CoA with C16 fatty acid chains. Can also utilize
CC acyl-CoA with C14 and C18 fatty acid chains (By similarity).
CC {ECO:0000250|UniProtKB:Q5W0Z9, ECO:0000305|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 -!- 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:0000250|UniProtKB:Q5W0Z9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q5W0Z9};
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:0000250|UniProtKB:Q5W0Z9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q5W0Z9};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q5W0Z9}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:Q5W0Z9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5Y5T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5Y5T1-2; Sequence=VSP_016278;
CC -!- TISSUE SPECIFICITY: Highest levels in lung.
CC {ECO:0000269|PubMed:15603741}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q5W0Z9}.
CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000250|UniProtKB:Q5W0Z9}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY668951; AAU89705.1; -; mRNA.
DR EMBL; AK017158; BAB30620.1; -; mRNA.
DR EMBL; AK031184; BAC27294.1; -; mRNA.
DR EMBL; AK049270; BAC33648.1; -; mRNA.
DR EMBL; AK140182; BAE24268.1; -; mRNA.
DR EMBL; AK163174; BAE37221.1; -; mRNA.
DR EMBL; AK170139; BAE41590.1; -; mRNA.
DR EMBL; BC019536; AAH19536.1; -; mRNA.
DR CCDS; CCDS27162.1; -. [Q5Y5T1-2]
DR CCDS; CCDS88676.1; -. [Q5Y5T1-1]
DR RefSeq; NP_083768.4; NM_029492.4. [Q5Y5T1-2]
DR AlphaFoldDB; Q5Y5T1; -.
DR SMR; Q5Y5T1; -.
DR STRING; 10090.ENSMUSP00000086900; -.
DR iPTMnet; Q5Y5T1; -.
DR PhosphoSitePlus; Q5Y5T1; -.
DR SwissPalm; Q5Y5T1; -.
DR EPD; Q5Y5T1; -.
DR jPOST; Q5Y5T1; -.
DR MaxQB; Q5Y5T1; -.
DR PaxDb; Q5Y5T1; -.
DR PeptideAtlas; Q5Y5T1; -.
DR PRIDE; Q5Y5T1; -.
DR ProteomicsDB; 302122; -. [Q5Y5T1-1]
DR ProteomicsDB; 302123; -. [Q5Y5T1-2]
DR Antibodypedia; 4929; 196 antibodies from 24 providers.
DR DNASU; 75965; -.
DR Ensembl; ENSMUST00000089473; ENSMUSP00000086900; ENSMUSG00000021969. [Q5Y5T1-2]
DR Ensembl; ENSMUST00000226057; ENSMUSP00000153568; ENSMUSG00000021969. [Q5Y5T1-1]
DR GeneID; 75965; -.
DR KEGG; mmu:75965; -.
DR UCSC; uc007udr.1; mouse. [Q5Y5T1-2]
DR UCSC; uc007uds.1; mouse. [Q5Y5T1-1]
DR CTD; 253832; -.
DR MGI; MGI:1923215; Zdhhc20.
DR VEuPathDB; HostDB:ENSMUSG00000021969; -.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; Q5Y5T1; -.
DR OMA; QPDSNKC; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q5Y5T1; -.
DR TreeFam; TF316044; -.
DR BioGRID-ORCS; 75965; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Zdhhc20; mouse.
DR PRO; PR:Q5Y5T1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q5Y5T1; protein.
DR Bgee; ENSMUSG00000021969; Expressed in seminal vesicle and 238 other tissues.
DR Genevisible; Q5Y5T1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:MGI.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISS: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; Cell membrane; Cytoplasm;
KW Endoplasmic reticulum; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..380
FT /note="Palmitoyltransferase ZDHHC20"
FT /id="PRO_0000212907"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 36..53
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 75..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 191..222
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TRANSMEM 223..246
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT TOPO_DOM 247..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT DOMAIN 126..176
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 156
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 140..143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT SITE 29
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT SITE 181
FT /note="Important for selectivity toward medium-length fatty
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT VAR_SEQ 199..210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016278"
FT CONFLICT 130
FT /note="K -> R (in Ref. 2; BAE41590)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="F -> Y (in Ref. 2; BAB30620)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="T -> I (in Ref. 2; BAE41590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 43976 MW; 3ECD9E424185BF01 CRC64;
MAPWTLWRCC QRVVGWVPVL FITFVVVWSY YAYVVELCVS TISRTGEKGK TVVYLVAFHL
FFVMFVWSYW MTIFTSPASP SKEFYLSNSE KERYEKEFSQ ERQQDILRRA ARDLPIYTTS
ASKAIRYCEK CQLIKPDRAH HCSACDRCVL KMDHHCPWVN NCVGFTNYKF FMLFLLYSLL
YCLFVAATVL EYFIKFWTLC RRKSTENCPK NEPTVLNFPS AKFHVLFLFF VSAMFFVSVL
SLFSYHCWLV GKNRTTIESF RAPMFSYGID GNGFSLGCSK NWRQVFGDEK KYWLVPIFSS
LGDGCSFPAR LVGMDPEQAS VANQSDYVRS IGSNQPFPIK PLSESKNRLL DSESQWLENG
AEEGVTKSGT NNHVTVEIEN
