ZDHC3_ARATH
ID ZDHC3_ARATH Reviewed; 565 AA.
AC Q6DR03; O22814; Q8L8C4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein S-acyltransferase 21;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At2g33640;
DE AltName: Full=Zinc finger DHHC domain-containing protein At2g33640;
GN Name=PAT21; OrderedLocusNames=At2g33640; ORFNames=F4P9.41;
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].
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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).
CC -!- FUNCTION: S-acyltransferase involved in protein lipid modification.
CC {ECO:0000269|PubMed:22968831, ECO:0000269|Ref.6}.
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: Cell membrane {ECO:0000305}; Multi-pass membrane
CC 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=AAB80679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002332; AAB80679.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08865.1; -; Genomic_DNA.
DR EMBL; AY102547; AAM76752.1; -; mRNA.
DR EMBL; AY649312; AAT69229.1; -; mRNA.
DR PIR; A84748; A84748.
DR RefSeq; NP_180922.2; NM_128924.4.
DR AlphaFoldDB; Q6DR03; -.
DR STRING; 3702.AT2G33640.1; -.
DR iPTMnet; Q6DR03; -.
DR PaxDb; Q6DR03; -.
DR PRIDE; Q6DR03; -.
DR EnsemblPlants; AT2G33640.1; AT2G33640.1; AT2G33640.
DR GeneID; 817930; -.
DR Gramene; AT2G33640.1; AT2G33640.1; AT2G33640.
DR KEGG; ath:AT2G33640; -.
DR Araport; AT2G33640; -.
DR TAIR; locus:2051068; AT2G33640.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_020283_2_1_1; -.
DR InParanoid; Q6DR03; -.
DR OMA; LCTPPNI; -.
DR OrthoDB; 290340at2759; -.
DR PhylomeDB; Q6DR03; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q6DR03; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6DR03; baseline and differential.
DR Genevisible; Q6DR03; 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:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0016417; F:S-acyltransferase activity; IGI:TAIR.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:TAIR.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0018345; P:protein palmitoylation; IGI:TAIR.
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; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..565
FT /note="Protein S-acyltransferase 21"
FT /id="PRO_0000363591"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 144..194
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 348..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 264
FT /note="M -> T (in Ref. 3 and 4; AAM76752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 62139 MW; B5AA41AD7BA8F821 CRC64;
MARRHGWQLP AHTFQVVAIT VFFLLTVAYY AFFAPFLGNK LYEYIAIGVY SFLAFSVLVL
YIRCTGIDPA DPGIFVKADN TPAHKSQNSN YVPENASAID GGPYIRHGSG CCSAIGRFIC
GCLVIQDCRR DTQQEQSNEQ EEALFCSLCN AEVRMFSKHC RSCGKCVDGF DHHCRWLNNC
VGQKNYISFV CLMAASFFWL IAEFGVGVTV FVRCFVDQKA MEHLITEKLG LGFSRPPFAA
VVVVCTTLSL LALIPLGELF FFHMILIRKG ITTYEYVVAL RAQTEPLGTS VDELDQTSQY
PSPASSAVTA TSARSSLGLS IQYRGASLCT PPNIFVDQQD DVIQHLEPGP VRSTIDPDSL
SQKKPPQRQQ VRINPWKLAK LDSKEASKAA AKARASSSVL LPVSSRQNPY KTSSNVSGRS
SPGRGKPADS ESCSLSSPGL TRDHFNPMYM SSPANESPLN EEESRNAVVA ARRNLPSSDE
SSVVWDPEAG RFVSLSRIPG TDVGGPLGNE CLNTITSTGT DRSRRARGNP LTGYFQQVRS
QRGDQLPVFM PTDSQLHRHL STRFH
