ZDHC1_ARATH
ID ZDHC1_ARATH Reviewed; 596 AA.
AC Q9C533;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable protein S-acyltransferase 22;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At1g69420;
DE AltName: Full=Zinc finger DHHC domain-containing protein At1g69420;
GN Name=PAT22; OrderedLocusNames=At1g69420; ORFNames=F10D13.9, F23O10.1;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
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, DEVELOPMENTAL STAGE, 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}. Cytoplasmic vesicle membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during bolting.
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=AAG52492.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG60091.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018364; AAG52492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC073178; AAG60091.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34922.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34923.1; -; Genomic_DNA.
DR EMBL; BX814193; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_177101.2; NM_105609.4.
DR RefSeq; NP_974114.1; NM_202385.2.
DR AlphaFoldDB; Q9C533; -.
DR BioGRID; 28495; 1.
DR IntAct; Q9C533; 1.
DR STRING; 3702.AT1G69420.1; -.
DR iPTMnet; Q9C533; -.
DR PaxDb; Q9C533; -.
DR PRIDE; Q9C533; -.
DR ProteomicsDB; 242959; -.
DR EnsemblPlants; AT1G69420.1; AT1G69420.1; AT1G69420.
DR EnsemblPlants; AT1G69420.2; AT1G69420.2; AT1G69420.
DR GeneID; 843274; -.
DR Gramene; AT1G69420.1; AT1G69420.1; AT1G69420.
DR Gramene; AT1G69420.2; AT1G69420.2; AT1G69420.
DR KEGG; ath:AT1G69420; -.
DR Araport; AT1G69420; -.
DR TAIR; locus:2007086; AT1G69420.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_020283_2_0_1; -.
DR InParanoid; Q9C533; -.
DR OMA; GKKIFQY; -.
DR OrthoDB; 557113at2759; -.
DR PhylomeDB; Q9C533; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q9C533; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C533; baseline and differential.
DR Genevisible; Q9C533; 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: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; Cell membrane; Cytoplasmic vesicle; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..596
FT /note="Probable protein S-acyltransferase 22"
FT /id="PRO_0000363589"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 163..213
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 102..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 596 AA; 65890 MW; 3F7BF5386F094DB7 CRC64;
MRKHGWQLPY HPLQVVAVAV FLALGFAFYV FFAPFVGKKI HQYIAMGIYT PLITCVVGLY
IWCAASDPAD RGVFRSKKYL KIPENGKFPL AKDIKDGCGS ATGGAKSHDG TCVEDTENGS
NKKLESSERS SLLRLLCSPC ALLCSCCSGK DESSEQMSED GMFYCSLCEV EVFKYSKHCR
VCDKCVDRFD HHCRWLNNCI GKRNYRKFFS LMVSAIFLLI MQWSTGIFVL VLCLLRRNQF
NADIALKLGS SFSLIPFVIV VGVCTVLAML ATLPLAQLFF FHILLIKKGI STYDYIVALR
EQEQELEAGG GQQSPQMSMI SSFTGLSSAS SFNTFHRGAW CTPPRLFLED QFDVVPPENA
SVSSYGKKSV VEERVKKKPQ PVKISPWTLA RLNAEEVSKA AAEARKKSKI IQPVARRENP
FVGLEASSSF GSSGRRMFPT KYEGVNNNGK QRRQSKRIRL PAELPLEPLM NVQTKAAMET
STSSGLAPLQ LEARSAFQTS RAMSGSGNVM VTSSPESSLD SHDIHPFRVS SEAEDAAQLN
GFSSAVGLMG QQRGQQQQQQ LSMMMMPLSR STSDGYDASG GEDSDQVPSR NIHKSR
