ZDH23_ARATH
ID ZDH23_ARATH Reviewed; 410 AA.
AC Q9FLM3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Probable protein S-acyltransferase 6;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At5g41060;
DE AltName: Full=Zinc finger DHHC domain-containing protein At5g41060;
GN Name=PAT06; OrderedLocusNames=At5g41060; ORFNames=MEE6.13;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 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, 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: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FLM3-1; Sequence=Displayed;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB010072; BAB09708.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94631.1; -; Genomic_DNA.
DR EMBL; AY045978; AAK76652.1; -; mRNA.
DR EMBL; AY079326; AAL85057.1; -; mRNA.
DR RefSeq; NP_198922.1; NM_123471.4. [Q9FLM3-1]
DR AlphaFoldDB; Q9FLM3; -.
DR SMR; Q9FLM3; -.
DR STRING; 3702.AT5G41060.1; -.
DR iPTMnet; Q9FLM3; -.
DR PaxDb; Q9FLM3; -.
DR PRIDE; Q9FLM3; -.
DR ProteomicsDB; 242946; -. [Q9FLM3-1]
DR EnsemblPlants; AT5G41060.1; AT5G41060.1; AT5G41060. [Q9FLM3-1]
DR GeneID; 834108; -.
DR Gramene; AT5G41060.1; AT5G41060.1; AT5G41060. [Q9FLM3-1]
DR KEGG; ath:AT5G41060; -.
DR Araport; AT5G41060; -.
DR TAIR; locus:2163001; AT5G41060.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_018741_2_2_1; -.
DR InParanoid; Q9FLM3; -.
DR OMA; HADEEVT; -.
DR PhylomeDB; Q9FLM3; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q9FLM3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLM3; baseline and differential.
DR Genevisible; Q9FLM3; 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; IEA:UniProtKB-SubCell.
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; Alternative splicing; Cell membrane; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..410
FT /note="Probable protein S-acyltransferase 6"
FT /id="PRO_0000363607"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 147..197
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 108..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0WQK2"
SQ SEQUENCE 410 AA; 46369 MW; A693174A518FA168 CRC64;
MYVVTPPQRS GFGSDCDLRV YQTWKGSNIF CLQGRFIFGP DVRSLGLTIS LIVAPVTIFC
IFVASKLMDD FSDSWGVSII LVAVVFTIYD LILLMLTSGR DPGIIPRNSH PPEPEVVDGN
TGSGTSQTPR LPRVKEVEVN GKVFKVKYCD TCMLYRPPRC SHCSICNNCV ERFDHHCPWV
GQCIAQRNYR FFFMFVFSTT LLCVYVFAFC CVYIKKIKES EDISILKAML KTPASIALIL
YTFISTFFVG GLTCFHLYLI STNQTTYENF RYSYDRHSNP HNKGVVDNFK EIFFSPIPPS
KNNFRAMVPR ENPMPSRSVV GGFMSPNMGK ANDDIEMGRK GVWAMAEHGD GKDGNNNERF
HVNDNELNEL SPDMGNIVNG DEQINRPNNH PRNANWEMSP EVMALSARRA
