ID ZDH20_HUMAN Reviewed; 365 AA. AC Q5W0Z9; A8MTV9; C9JG20; I6L9D4; Q2TB82; Q6NVU8; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 02-OCT-2024, entry version 158. DE RecName: Full=Palmitoyltransferase ZDHHC20 {ECO:0000305|PubMed:27153536}; DE EC=2.3.1.225 {ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245}; DE AltName: Full=Acyltransferase ZDHHC20 {ECO:0000305|PubMed:29326245}; DE EC=2.3.1.- {ECO:0000305|PubMed:29326245}; DE AltName: Full=DHHC domain-containing cysteine-rich protein 20 {ECO:0000303|PubMed:27153536}; DE Short=DHHC20 {ECO:0000303|PubMed:27153536}; DE AltName: Full=Zinc finger DHHC domain-containing protein 20 {ECO:0000312|HGNC:HGNC:20749}; GN Name=ZDHHC20 {ECO:0000312|HGNC:HGNC:20749}; 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 GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [2] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Ovary, and Testis; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-330, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=27153536; DOI=10.1016/j.molcel.2016.04.003; RA Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., RA Witze E.S.; RT "Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on RT EGFR Signaling."; RL Mol. Cell 62:385-396(2016). RN [9] RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND CATALYTIC RP ACTIVITY. RX PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016; RA Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B., RA Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M., RA Trono D., D'Angelo G., van der Goot F.G.; RT "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances RT infectivity."; RL Dev. Cell 56:1-18(2021). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=33219126; DOI=10.1074/jbc.ra120.015701; RA Malgapo M.I.P., Safadi J.M., Linder M.E.; RT "Metallo-beta-Lactamase Domain-Containing Protein 2 (MBLAC2) is S- RT palmitoylated and exhibits acyl-CoA hydrolase activity."; RL J. Biol. Chem. 296:100106-100118(2021). RN [11] {ECO:0007744|PDB:6BML, ECO:0007744|PDB:6BMM, ECO:0007744|PDB:6BMN} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 5-299 IN COMPLEX WITH PALMITATE; RP SUBSTRATE ANALOG AND ZINC, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, RP MUTAGENESIS OF ILE-22; SER-29; ASP-153; HIS-154; CYS-156; TRP-158; PHE-171; RP PHE-174; TYR-181; LEU-227; 240-THR-THR-241; GLU-243; ASN-266; TRP-267 AND RP PHE-271, ACTIVE SITE, SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION. RX PubMed=29326245; DOI=10.1126/science.aao6326; RA Rana M.S., Kumar P., Lee C.J., Verardi R., Rajashankar K.R., Banerjee A.; RT "Fatty acyl recognition and transfer by an integral membrane S- RT acyltransferase."; RL Science 359:0-0(2018). CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of CC palmitate onto various protein substrates (PubMed:27153536, CC PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys CC residues in the cytoplasmic C-terminus of EGFR, and modulates the CC duration of EGFR signaling by modulating palmitoylation-dependent EGFR CC internalization and degradation (PubMed:27153536). Has a preference for CC acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize CC acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245). May CC palmitoylate CALHM1 subunit of gustatory voltage-gated ion channels and CC modulate channel gating and kinetics. {ECO:0000250|UniProtKB:Q5Y5T1, CC ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245, CC ECO:0000269|PubMed:33219126}. CC -!- FUNCTION: (Microbial infection) Dominant palmitoyltransferase CC responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike CC protein. Through a sequential action with ZDHHC9, rapidly and CC efficiently palmitoylates spike protein following its synthesis in the CC endoplasmic reticulum (ER). In the infected cell, promotes spike CC biogenesis by protecting it from premature ER degradation, increases CC half-life and controls the lipid organization of its immediate membrane CC environment. Once the virus has formed, spike palmitoylation controls CC fusion with the target cell. {ECO:0000269|PubMed:34599882}. 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:29326245, CC ECO:0000269|PubMed:33219126, ECO:0000269|PubMed:34599882}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684; CC Evidence={ECO:0000305|PubMed:29326245}; 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:0000269|PubMed:29326245}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; CC Evidence={ECO:0000305|PubMed:29326245}; 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:0000269|PubMed:29326245}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; CC Evidence={ECO:0000305|PubMed:29326245}; CC -!- INTERACTION: CC Q5W0Z9-4; P07339: CTSD; NbExp=3; IntAct=EBI-25840130, EBI-2115097; CC Q5W0Z9-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25840130, EBI-396669; CC Q5W0Z9-4; O76024: WFS1; NbExp=3; IntAct=EBI-25840130, EBI-720609; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein CC {ECO:0000269|PubMed:29326245}. Cell membrane CC {ECO:0000269|PubMed:27153536}; Multi-pass membrane protein CC {ECO:0000269|PubMed:29326245}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment CC membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q5W0Z9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5W0Z9-2; Sequence=VSP_016276, VSP_016277; CC Name=3; CC IsoId=Q5W0Z9-3; Sequence=VSP_040481, VSP_040482; CC Name=4; CC IsoId=Q5W0Z9-4; Sequence=VSP_056002; CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity. CC {ECO:0000269|PubMed:29326245}. CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:29326245}. CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL136219; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08309.1; -; Genomic_DNA. DR EMBL; BC034944; AAH34944.1; -; mRNA. DR EMBL; BC050367; AAH50367.2; -; mRNA. DR EMBL; BC067898; AAH67898.1; -; mRNA. DR EMBL; BC110517; AAI10518.1; -; mRNA. DR CCDS; CCDS45017.1; -. [Q5W0Z9-3] DR CCDS; CCDS81758.1; -. [Q5W0Z9-1] DR RefSeq; NP_001273567.1; NM_001286638.1. DR RefSeq; NP_001316988.1; NM_001330059.1. [Q5W0Z9-1] DR RefSeq; NP_694983.2; NM_153251.3. [Q5W0Z9-3] DR PDB; 6BML; X-ray; 2.95 A; A/B=5-299. DR PDB; 6BMM; X-ray; 2.35 A; A/B=7-299. DR PDB; 6BMN; X-ray; 2.25 A; A/B=5-299. DR PDB; 7KHM; X-ray; 2.88 A; A/B=2-316. DR PDBsum; 6BML; -. DR PDBsum; 6BMM; -. DR PDBsum; 6BMN; -. DR PDBsum; 7KHM; -. DR AlphaFoldDB; Q5W0Z9; -. DR SMR; Q5W0Z9; -. DR BioGRID; 128991; 40. DR IntAct; Q5W0Z9; 22. DR MINT; Q5W0Z9; -. DR STRING; 9606.ENSP00000383433; -. DR BindingDB; Q5W0Z9; -. DR ChEMBL; CHEMBL5169156; -. DR TCDB; 8.A.114.1.6; the huntington-interacting protein 14 (hip14) family. DR iPTMnet; Q5W0Z9; -. DR PhosphoSitePlus; Q5W0Z9; -. DR SwissPalm; Q5W0Z9; -. DR BioMuta; ZDHHC20; -. DR DMDM; 74748004; -. DR jPOST; Q5W0Z9; -. DR MassIVE; Q5W0Z9; -. DR PaxDb; 9606-ENSP00000371905; -. DR PeptideAtlas; Q5W0Z9; -. DR ProteomicsDB; 61482; -. DR ProteomicsDB; 65788; -. [Q5W0Z9-1] DR ProteomicsDB; 65789; -. [Q5W0Z9-2] DR ProteomicsDB; 65790; -. [Q5W0Z9-3] DR Pumba; Q5W0Z9; -. DR Antibodypedia; 4929; 217 antibodies from 24 providers. DR DNASU; 253832; -. DR Ensembl; ENST00000320220.13; ENSP00000313583.9; ENSG00000180776.17. [Q5W0Z9-4] DR Ensembl; ENST00000382466.7; ENSP00000371905.3; ENSG00000180776.17. [Q5W0Z9-3] DR Ensembl; ENST00000400590.8; ENSP00000383433.3; ENSG00000180776.17. [Q5W0Z9-1] DR Ensembl; ENST00000415724.2; ENSP00000401232.1; ENSG00000180776.17. [Q5W0Z9-1] DR GeneID; 253832; -. DR KEGG; hsa:253832; -. DR MANE-Select; ENST00000400590.8; ENSP00000383433.3; NM_001330059.2; NP_001316988.1. DR UCSC; uc001uoa.4; human. [Q5W0Z9-1] DR AGR; HGNC:20749; -. DR CTD; 253832; -. DR DisGeNET; 253832; -. DR GeneCards; ZDHHC20; -. DR HGNC; HGNC:20749; ZDHHC20. DR HPA; ENSG00000180776; Low tissue specificity. DR MIM; 617972; gene. DR neXtProt; NX_Q5W0Z9; -. DR OpenTargets; ENSG00000180776; -. DR PharmGKB; PA134880838; -. DR VEuPathDB; HostDB:ENSG00000180776; -. DR eggNOG; KOG1315; Eukaryota. DR GeneTree; ENSGT00940000153716; -. DR InParanoid; Q5W0Z9; -. DR OMA; AFHNYKF; -. DR OrthoDB; 6683at2759; -. DR PhylomeDB; Q5W0Z9; -. DR TreeFam; TF316044; -. DR PathwayCommons; Q5W0Z9; -. DR Reactome; R-HSA-9694548; Maturation of spike protein. DR SignaLink; Q5W0Z9; -. DR BioGRID-ORCS; 253832; 19 hits in 1154 CRISPR screens. DR ChiTaRS; ZDHHC20; human. DR GenomeRNAi; 253832; -. DR Pharos; Q5W0Z9; Tbio. DR PRO; PR:Q5W0Z9; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q5W0Z9; protein. DR Bgee; ENSG00000180776; Expressed in upper arm skin and 191 other cell types or tissues. DR ExpressionAtlas; Q5W0Z9; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:UniProt. 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:0000139; C:Golgi membrane; IMP:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB. DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB. DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB. DR GO; GO:0044794; P:positive regulation by host of viral process; IDA:UniProtKB. DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB. DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central. DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1. DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1. DR Pfam; PF01529; DHHC; 1. DR PROSITE; PS50216; DHHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Alternative splicing; Cell membrane; KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Host-virus interaction; KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; KW Proteomics identification; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1..365 FT /note="Palmitoyltransferase ZDHHC20" FT /id="PRO_0000212906" FT TOPO_DOM 1..14 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29326245" FT TRANSMEM 15..35 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:29326245" FT TOPO_DOM 36..53 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:29326245" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:29326245" FT TOPO_DOM 75..169 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29326245" FT TRANSMEM 170..190 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:29326245" FT TOPO_DOM 191..207 FT /note="Lumenal" FT /evidence="ECO:0000269|PubMed:29326245" FT TRANSMEM 208..231 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:29326245" FT TOPO_DOM 232..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:29326245" 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:0000269|PubMed:29326245" FT BINDING 128 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 135 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:29326245" FT BINDING 140..143 FT /ligand="substrate" FT /evidence="ECO:0000305|PubMed:29326245" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:29326245, FT ECO:0007744|PDB:6BMN" FT SITE 29 FT /note="Important for selectivity toward medium-length fatty FT acids" FT /evidence="ECO:0000269|PubMed:29326245" FT SITE 181 FT /note="Important for selectivity toward medium-length fatty FT acids" FT /evidence="ECO:0000269|PubMed:29326245" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT VAR_SEQ 124..130 FT /note="TIRYCEK -> SLMQSTK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016276" FT VAR_SEQ 131..365 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_016277" FT VAR_SEQ 315..365 FT /note="SSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN FT -> RSKLQR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056002" FT VAR_SEQ 315 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040481" FT VAR_SEQ 355..365 FT /note="TNNHVTVAIEN -> V (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_040482" FT MUTAGEN 22 FT /note="I->W: Strongly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 29 FT /note="S->F: Strongly reduced catalytic activity. Enhances FT activity with acyl-CoA with C12 and C14 fatty acid chains." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 153 FT /note="D->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 154 FT /note="H->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 156 FT /note="C->S: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 158 FT /note="W->A: Strongly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 171 FT /note="F->A: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 174 FT /note="F->A: Strongly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 181 FT /note="Y->A: Moderately reduced catalytic activity. FT Enhances activity with acyl-CoA with C18 and C20 fatty acid FT chains." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 227 FT /note="L->W: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 240..241 FT /note="TT->AA: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 243 FT /note="E->A: Mildly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 266 FT /note="N->A: Strongly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 267 FT /note="Missing: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT MUTAGEN 271 FT /note="F->A: Mildly reduced catalytic activity." FT /evidence="ECO:0000269|PubMed:29326245" FT HELIX 7..14 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 17..34 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 35..42 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 48..74 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 90..96 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 100..111 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 112..115 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 129..132 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 140..142 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 143..146 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 147..149 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 161..164 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 168..197 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 204..237 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 241..245 FT /evidence="ECO:0007829|PDB:6BMN" FT TURN 256..259 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 263..271 FT /evidence="ECO:0007829|PDB:6BMN" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:6BMN" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:6BMN" SQ SEQUENCE 365 AA; 42278 MW; 179D8882138E4F53 CRC64; MAPWTLWRCC QRVVGWVPVL FITFVVVWSY YAYVVELCVF TIFGNEENGK TVVYLVAFHL FFVMFVWSYW MTIFTSPASP SKEFYLSNSE KERYEKEFSQ ERQQEILRRA ARALPIYTTS ASKTIRYCEK CQLIKPDRAH HCSACDSCIL KMDHHCPWVN NCVGFSNYKF FLLFLLYSLL YCLFVAATVL EYFIKFWTNE LTDTRAKFHV LFLFFVSAMF FISVLSLFSY HCWLVGKNRT TIESFRAPTF SYGPDGNGFS LGCSKNWRQV FGDEKKYWLL PIFSSLGDGC SFPTRLVGMD PEQASVTNQN EYARSSGSNQ PFPIKPLSES KNRLLDSESQ WLENGAEEGI VKSGTNNHVT VAIEN //