ZDHC2_ARATH
ID ZDHC2_ARATH Reviewed; 536 AA.
AC Q3EC11; A2RVQ6; Q9ZQ58;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Probable protein S-acyltransferase 23;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At2g14255;
DE AltName: Full=Zinc finger DHHC domain-containing protein At2g14255;
GN Name=PAT23; OrderedLocusNames=At2g14255; ORFNames=T1O16.20;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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] OF 1-249.
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, GENE
RP 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.4}.
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: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q3EC11-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, flowers and pollen.
CC {ECO:0000269|PubMed:22968831}.
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=AAD20110.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006304; AAD20110.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06292.1; -; Genomic_DNA.
DR EMBL; BT030047; ABN04785.1; -; mRNA.
DR PIR; D84515; D84515.
DR RefSeq; NP_973453.2; NM_201724.3. [Q3EC11-1]
DR AlphaFoldDB; Q3EC11; -.
DR SMR; Q3EC11; -.
DR BioGRID; 30135; 1.
DR IntAct; Q3EC11; 1.
DR STRING; 3702.AT2G14255.1; -.
DR PaxDb; Q3EC11; -.
DR PRIDE; Q3EC11; -.
DR ProteomicsDB; 242980; -. [Q3EC11-1]
DR EnsemblPlants; AT2G14255.1; AT2G14255.1; AT2G14255. [Q3EC11-1]
DR GeneID; 2745525; -.
DR Gramene; AT2G14255.1; AT2G14255.1; AT2G14255. [Q3EC11-1]
DR KEGG; ath:AT2G14255; -.
DR Araport; AT2G14255; -.
DR TAIR; locus:1006230134; AT2G14255.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_031257_3_0_1; -.
DR InParanoid; Q3EC11; -.
DR OMA; PWMAGIF; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q3EC11; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q3EC11; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q3EC11; baseline and differential.
DR Genevisible; Q3EC11; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
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: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:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; ANK repeat; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..536
FT /note="Probable protein S-acyltransferase 23"
FT /id="PRO_0000363590"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 57..86
FT /note="ANK 1"
FT REPEAT 90..119
FT /note="ANK 2"
FT REPEAT 123..153
FT /note="ANK 3"
FT REPEAT 157..186
FT /note="ANK 4"
FT REPEAT 190..219
FT /note="ANK 5"
FT REPEAT 225..254
FT /note="ANK 6"
FT DOMAIN 363..413
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 246..249
FT /note="SKAM -> VRNV (in Ref. 3; ABN04785)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 59988 MW; 1BBB18C651003487 CRC64;
MDSSEIEVVP LDSNSHQSPT ESPTITDVFS ASAYGDLHQL KHFVEHNGSS VSLPDDNGFY
ALQWAALNNS LHVAQYIIQH GGDVNSADNI QQTPLHWAAV KGSIDVADLL LQHGARIEAV
DVNGFRAVHV ASQYGQTAFV NHIIVDYAAD YNALDIEGRS PLHWAAYNGF TETVRLLLFR
DACQNRQDNT GCTPLHWAVI KENVEACTLL VHAGTKEELI LKDNTGSTPL KLASDKGHRQ
LALFLSKAMR TRKNSFVDKI FCGKLGETSY APMLFSLIVI LMVLFITSIV SASNLPKITA
MVGLWACFGL SCGVYALITF YRVSRKDPGY VKRTGEANSQ HTANDPLIDI NFKNPSWKGN
WSQLCPTCKI IRPVRSKHCP TCKRCVEQFD HHCPWISNCV GKKNKRYFLV FVIMGALTSF
VGGTTAVQRL WRGIPQVHHG ESWIKHIVIE HPDAAVFLFF DLLIFIATMT LTISQSYMIA
RNITTNELWN AKRFSYLRGP DGRFYNPYNH GLRRNCTDFL VHGYTRDDEV VPSSIL
