ZDHC9_ARATH
ID ZDHC9_ARATH Reviewed; 443 AA.
AC Q0WQK2; Q9LJF4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Probable protein S-acyltransferase 7;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At3g26935;
DE AltName: Full=Zinc finger DHHC domain-containing protein At3g26935;
GN Name=PAT07; OrderedLocusNames=At3g26935; ORFNames=MOJ10.1;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-377, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [9]
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.7}.
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=BAB01189.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000602; BAB01189.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB026649; BAB01189.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77247.1; -; Genomic_DNA.
DR EMBL; AK228693; BAF00597.1; -; mRNA.
DR RefSeq; NP_850638.1; NM_180307.4.
DR AlphaFoldDB; Q0WQK2; -.
DR SMR; Q0WQK2; -.
DR STRING; 3702.AT3G26935.1; -.
DR iPTMnet; Q0WQK2; -.
DR PaxDb; Q0WQK2; -.
DR PRIDE; Q0WQK2; -.
DR ProteomicsDB; 232324; -.
DR EnsemblPlants; AT3G26935.1; AT3G26935.1; AT3G26935.
DR GeneID; 822311; -.
DR Gramene; AT3G26935.1; AT3G26935.1; AT3G26935.
DR KEGG; ath:AT3G26935; -.
DR Araport; AT3G26935; -.
DR TAIR; locus:2091960; AT3G26935.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_018741_2_2_1; -.
DR InParanoid; Q0WQK2; -.
DR OMA; SEHITIL; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q0WQK2; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q0WQK2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WQK2; baseline and differential.
DR Genevisible; Q0WQK2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; HDA:TAIR.
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 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Probable protein S-acyltransferase 7"
FT /id="PRO_0000363596"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 149..199
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 382..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19376835"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M306"
SQ SEQUENCE 443 AA; 49916 MW; 48AD4A5F29726D0D CRC64;
MYVVPPPQRS DSGSNGDLRV YQTWKGSNIF FLQGRFVFGP DVRSLALTIC LIAVPVTIFC
IFVARKLIDD FSDSWGVSIV AVAVVFTIYD LILLLLTSGR DPGIIPRNAH PPEPETLDGN
MDAGAGQTPQ LRLPRIKEVQ LNGITFKVKY CDTCMLYRPP RCSHCSICNN CVERFDHHCP
WVGQCIGMRN YRFFFMFVFS TTLLCIYVFA FCWVYIRKIM ESEHTTTWKA MLKTPASIVL
IIYTFISMWF VGGLTVFHLY LISTNQTTYE NFRYRYDRRS NPHNKGVVNN FKETFFSTIP
PSKNDFRAMV QREPPLPPRS VAGGFMSPNM GKANDEIEMG RKAVWADMGP AMSDHGDGKH
GNNERLHVKD GELGELSPDI RATVDEQSDR PSMHPRRSSW GRKSGSWDMS PEVMALAARV
GEQNQNGGGS SSGSGLVTEN RPT
