ID ZDH12_ARATH Reviewed; 338 AA. AC B3DN87; Q9LER6; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 1. DT 02-SEP-2026, entry version 102. DE RecName: Full=Probable protein S-acyltransferase 1; DE EC=2.3.1.225; DE AltName: Full=Probable palmitoyltransferase At3g56920; DE AltName: Full=Zinc finger DHHC domain-containing protein At3g56920; GN Name=PAT01; OrderedLocusNames=At3g56920; ORFNames=T8M16_250; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130713; DOI=10.1038/35048706; RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P., RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."; RL Nature 408:820-822(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.; RT "Arabidopsis ORF clones."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENE FAMILY, AND FUNCTION. RA Hemsley P.A., Taylor L., Grierson C.S.; RT "S-acylation: dynamic control of plant development and sigalling by lipid RT modification of proteins."; RL (In) Proceedings of the 18th international conference on Arabidopsis RL research, abstract#139, Beijing (2007). RN [6] RP SUBCELLULAR LOCATION, GENE FAMILY, AND NOMENCLATURE. RX PubMed=22968831; DOI=10.1104/pp.112.203968; RA Batistic O.; RT "Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S- RT acyltransferase protein family."; RL Plant Physiol. 160:1597-1612(2012). CC -!- FUNCTION: Palmitoyl acyltransferase. {ECO:0000250, ECO:0000269|Ref.5}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteinyl-[protein] + hexadecanoyl-CoA = S-hexadecanoyl-L- CC cysteinyl-[protein] + CoA; 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; CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAC00755.1; Type=Erroneous gene model prediction; Evidence={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; AL390921; CAC00755.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002686; AEE79586.1; -; Genomic_DNA. DR EMBL; OZ408685; CAO7044742.1; -; Genomic_DNA. DR EMBL; BT032875; ACD89065.1; -; mRNA. DR PIR; T51280; T51280. DR RefSeq; NP_191251.2; NM_115551.3. DR AlphaFoldDB; B3DN87; -. DR SMR; B3DN87; -. DR FunCoup; B3DN87; 1624. DR iPTMnet; B3DN87; -. DR PaxDb; 3702-B3DN87; -. DR ProteomicsDB; 242931; -. DR GeneID; 824859; -. DR KEGG; ath:AT3G56920; -. DR Araport; AT3G56920; -. DR TAIR; AT3G56920; -. DR eggNOG; KOG1311; Eukaryota. DR HOGENOM; CLU_018741_7_1_1; -. DR InParanoid; B3DN87; -. DR OMA; ISHRHPF; -. DR PhylomeDB; B3DN87; -. DR BRENDA; 2.3.1.225; 399. DR PRO; PR:B3DN87; -. DR Proteomes; UP000006548; Chromosome 3. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central. DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR InterPro; IPR039859; PFA4/ZDH16/20/ERF2-like. DR PANTHER; PTHR22883:SF284; PROTEIN S-ACYLTRANSFERASE 1-RELATED; 1. DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF01529; DHHC; 1. DR PROSITE; PS50216; DHHC; 1. PE 2: Evidence at transcript level; KW Acyltransferase; Endosome; Lipoprotein; Membrane; Palmitate; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..338 FT /note="Probable protein S-acyltransferase 1" FT /id="PRO_0000363598" FT TRANSMEM 32..52 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 68..88 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 186..206 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 142..192 FT /note="DHHC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067" FT REGION 319..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..338 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 172 FT /note="S-palmitoyl cysteine intermediate" FT /evidence="ECO:0000250" SQ SEQUENCE 338 AA; 38669 MW; 7002A20BC3B9D646 CRC64; MSSQNLERQR IYQVWPAKNK FYCGGRLVFG PDASSLLLTT CMIGGPAIAF SIRMAYLISH RHPFFHSLTL IGAILLTFMA FTFLFLTSSR DPGIIPRNKQ VSEAEIPDVT TQSTEWVTSK LGSVKLPRTK DVMVNGFTVK VKFCDTCQLY RPPRAFHCSI CNNCVQRFDH HCPWVGQCIA LRNYPFFVCF LSCSTLLCIY VFVFSWVSML KVHGEFYVVL ADDLILGVLG LYCFVSVWFV GGLTVFHFYL ICTNQTTCEN FRYHYDKKEN PYRKGILENF KELFFAKIPP PLINFRDWSP EEEDDVEVGS IASELVRAFG PKDTKMSSGK SDSEARER //