ZDH11_ARATH
ID ZDH11_ARATH Reviewed; 340 AA.
AC Q7XA86; Q8LAV8; Q9SD10;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Protein S-acyltransferase 10;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At3g51390;
DE AltName: Full=Zinc finger DHHC domain-containing protein At3g51390;
GN Name=PAT10; OrderedLocusNames=At3g51390; ORFNames=F26O13.30;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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 FUNCTION, 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).
RN [7]
RP FUNCTION, MUTAGENESIS OF CYS-192, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY SALT.
RX PubMed=23482856; DOI=10.1105/tpc.112.108829;
RA Zhou L.Z., Li S., Feng Q.N., Zhang Y.L., Zhao X., Zeng Y.L., Wang H.,
RA Jiang L., Zhang Y.;
RT "Protein S-acyl transferase10 is critical for development and salt
RT tolerance in Arabidopsis.";
RL Plant Cell 25:1093-1107(2013).
CC -!- FUNCTION: S-acyltransferase involved in protein lipid modification.
CC Catalyzes the palmitoylation of proteins peripheral or integral to the
CC tonoplast. Required for the tonoplast localization of CBL2, CBL3 and
CC CBL6, but not for the plasma membrane localization of CBL9, for the
CC endosome localization of RABF1 or for the endomembrane localization of
CC RABF2B. {ECO:0000269|PubMed:22968831, ECO:0000269|PubMed:23482856,
CC ECO:0000269|Ref.5}.
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;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Transient expression results in
CC mistargeting of PAT10 to the Golgi apparatus, while the non-functional
CC mutant is also localized in Golgi apparatus membranes.
CC {ECO:0000269|PubMed:22968831, ECO:0000269|PubMed:23482856}.
CC -!- TISSUE SPECIFICITY: Expressed in mature embryos, embryo sacs,
CC cotyledons, whole seedlings, hydathodes, guard cells, sites of lateral
CC root initiation, root tips and phloem, but not in xylem.
CC {ECO:0000269|PubMed:23482856}.
CC -!- DEVELOPMENTAL STAGE: Expressed in tapetal layer of developing anthers
CC and then expression gradually increases in developing microspores and
CC in mature pollen. {ECO:0000269|PubMed:23482856}.
CC -!- INDUCTION: Not regulated by salt stresses.
CC {ECO:0000269|PubMed:23482856}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Pleiotropic growth defects, including smaller
CC leaves, dwarfism, and sterility. Hypersensitivity to salt stress and
CC compromised pollen tube growth. {ECO:0000269|PubMed:23482856}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB63003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL133452; CAB63003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78787.1; -; Genomic_DNA.
DR EMBL; BT010141; AAQ22610.1; -; mRNA.
DR EMBL; AY087575; AAM65117.1; -; mRNA.
DR PIR; T45770; T45770.
DR RefSeq; NP_566950.1; NM_114998.5.
DR AlphaFoldDB; Q7XA86; -.
DR SMR; Q7XA86; -.
DR BioGRID; 9620; 1.
DR IntAct; Q7XA86; 1.
DR STRING; 3702.AT3G51390.1; -.
DR iPTMnet; Q7XA86; -.
DR SwissPalm; Q7XA86; -.
DR PaxDb; Q7XA86; -.
DR PRIDE; Q7XA86; -.
DR ProteomicsDB; 242975; -.
DR EnsemblPlants; AT3G51390.1; AT3G51390.1; AT3G51390.
DR GeneID; 824302; -.
DR Gramene; AT3G51390.1; AT3G51390.1; AT3G51390.
DR KEGG; ath:AT3G51390; -.
DR Araport; AT3G51390; -.
DR TAIR; locus:2081795; AT3G51390.
DR eggNOG; ENOG502QT5K; Eukaryota.
DR HOGENOM; CLU_031257_0_0_1; -.
DR InParanoid; Q7XA86; -.
DR OrthoDB; 1440636at2759; -.
DR PhylomeDB; Q7XA86; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q7XA86; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7XA86; baseline and differential.
DR Genevisible; Q7XA86; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; 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; IBA:GO_Central.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT CHAIN 1..340
FT /note="Protein S-acyltransferase 10"
FT /id="PRO_0000363597"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 162..212
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 192
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT MUTAGEN 192
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:23482856"
FT CONFLICT 140
FT /note="R -> K (in Ref. 4; AAM65117)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="G -> V (in Ref. 4; AAM65117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 39228 MW; 029BA53613D8F4E7 CRC64;
MGVCCPFLQP WDRARDQCLL NLPCLSDPVR RSSLLLKLAL VALHLVFIGF LFLFDAEFIE
KTKRDPWYMG CYILLFSATL LQYFVTSGSS PGYVVDAMRD VCEASAMYRN PSTTSIQHAS
RKSESVVVNV EGGSASCPRR PPTPWGKLVL DLYPPGTSIR NLTCGYCHVE QPPRTKHCHD
CDRCVLQFDH HCVWLGTCIG QKNHSKFWWY ICEETTLCIW TLIMYVDYLS NVAKPWWKNA
IIILLLVILA ISLIFVLLLL IFHSYLILTN QSTYELVRRR RIPYMRNIPG RVHPFSRGIR
RNLYNVCCGN YNLDSLPTAF ELEDRSRPYT CIDMLKCRCC
