ZDH21_ARATH
ID ZDH21_ARATH Reviewed; 413 AA.
AC Q5PNZ1; Q9FF67;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Probable protein S-acyltransferase 3;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At5g05070;
DE AltName: Full=Zinc finger DHHC domain-containing protein At5g05070;
GN Name=PAT03; OrderedLocusNames=At5g05070; ORFNames=MUG13.7;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2004) 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, TISSUE SPECIFICITY, 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.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: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in 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=BAB11529.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005245; BAB11529.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED90824.1; -; Genomic_DNA.
DR EMBL; BT020306; AAV85661.1; -; mRNA.
DR RefSeq; NP_196126.2; NM_120589.4.
DR AlphaFoldDB; Q5PNZ1; -.
DR SMR; Q5PNZ1; -.
DR STRING; 3702.AT5G05070.1; -.
DR PaxDb; Q5PNZ1; -.
DR PRIDE; Q5PNZ1; -.
DR ProteomicsDB; 232308; -.
DR EnsemblPlants; AT5G05070.1; AT5G05070.1; AT5G05070.
DR GeneID; 830389; -.
DR Gramene; AT5G05070.1; AT5G05070.1; AT5G05070.
DR KEGG; ath:AT5G05070; -.
DR Araport; AT5G05070; -.
DR TAIR; locus:2175349; AT5G05070.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_018741_7_2_1; -.
DR InParanoid; Q5PNZ1; -.
DR OMA; YDTEMGG; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q5PNZ1; -.
DR PRO; PR:Q5PNZ1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q5PNZ1; baseline and differential.
DR Genevisible; Q5PNZ1; AT.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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: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 InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasmic vesicle; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..413
FT /note="Probable protein S-acyltransferase 3"
FT /id="PRO_0000363606"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 171..221
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 364..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 47778 MW; 5D9A856A8312671C CRC64;
MQRERMSKKK ISQVHCIPSG DHILMTASSS KHIPHIRFYK AWKGNNRFCC GGRLIFGPDV
SSLYLTSFLI GAPALTFCIR MLVWIKRGDP FFNYTVLASG FILTLLDFTF LMLTSARDPG
IIPRNKTSMI LEDDSDSSLT QSMEWVNNKT PNLKIPRTKD VFVNGYTIKV KFCDTCLLYR
PPRASHCSIC NNCVQRFDHH CPWVGQCIAR RNYPFFICFI SSSTLLCIYV FVFSWINLIR
QPGKLWRTMS DDIVSVILIV YTFVAVWFVG GLTIFHFYLM STNQTTYENF RYRYDKKENP
YKRGLLKNVK EVLFAKIPPS QLDLRAMVPE EDDMTIASND SEYESEYTSS VRYDTEMGGK
LIKRDSPRKL PLPTRNLDDI KDISDNYDRS TTTREDASDR DPSFFSSQLD LPK
