ZDH16_ARATH
ID ZDH16_ARATH Reviewed; 508 AA.
AC Q9M115; F4JG49; Q9ZSI8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Protein S-acyltransferase 18;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At4g01730;
DE AltName: Full=Zinc finger DHHC domain-containing protein At4g01730;
GN Name=PAT18; OrderedLocusNames=At4g01730; ORFNames=T15B16.11;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, GENE FAMILY, AND
RP 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.3}.
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 -!- 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=AAC72868.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB77743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF104919; AAC72868.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161492; CAB77743.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82070.1; -; Genomic_DNA.
DR PIR; C85022; C85022.
DR PIR; T02002; T02002.
DR RefSeq; NP_192082.4; NM_116403.5.
DR AlphaFoldDB; Q9M115; -.
DR STRING; 3702.AT4G01730.1; -.
DR PaxDb; Q9M115; -.
DR PRIDE; Q9M115; -.
DR ProteomicsDB; 232346; -.
DR EnsemblPlants; AT4G01730.1; AT4G01730.1; AT4G01730.
DR GeneID; 826911; -.
DR Gramene; AT4G01730.1; AT4G01730.1; AT4G01730.
DR KEGG; ath:AT4G01730; -.
DR Araport; AT4G01730; -.
DR TAIR; locus:2133447; AT4G01730.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_040236_0_0_1; -.
DR InParanoid; Q9M115; -.
DR OMA; VSINPWK; -.
DR OrthoDB; 290340at2759; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q9M115; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M115; baseline and differential.
DR Genevisible; Q9M115; 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..508
FT /note="Protein S-acyltransferase 18"
FT /id="PRO_0000363602"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 158..208
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 443..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 508 AA; 57904 MW; 173907C4BCBE9BCC CRC64;
MTRRRHGWQR PLHPLQIVGA VIYSVLVAAF YVFLGFFLGN RIAVIALLSV FSSVAVSVIV
LFVRCTAIDP TDKTSAKKKR KDKSKGVLMK LRVKVVLSQV VVRFFRRLER KILRNFLRRT
YLDPWKSSVQ LEPLLPFPLV MKDDDSVTPD PKEEDDISYC SLCDLEVKRS SKHCRTCNRC
VEGFDHHCRW LNNCVGKKNY TTFILLMVFV LLMLIIEGGT ALAVFVRCFV DKKGMEMELK
RRLYVEFPQW ALATISIILV LFTAYGSAAM GQLFLFHVVL IRKGMRTYDY ILAMKEENQF
TEVDPFDELD SSSDESSDFD SPERLRPTFI SKFMCRKANE NQQRLSIKIE GDEQSPSSTL
INKKPGFHVS INPWKLITLS SEKALQAAEK AKERLRKTKP VSGTEENSLK PLPLETKFGL
LLDPDNNNTV LQPSTTAAVK LQVSPGRFSS PRRRFSGSSS STVPSPKQKY RTNFDLKLTE
VSRELESYIS RQVLCSVIKQ DGSEASPR
