ZDH19_ARATH
ID ZDH19_ARATH Reviewed; 407 AA.
AC Q9SB58; Q0WWZ7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Protein S-acyltransferase 8;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At4g24630;
DE AltName: Full=Zinc finger DHHC domain-containing protein At4g24630;
GN Name=PAT08; OrderedLocusNames=At4g24630; ORFNames=F22K18.170;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-298.
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 [4]
RP IDENTIFICATION BY 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 [5]
RP IDENTIFICATION BY 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 [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, TISSUE SPECIFICITY, 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.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 -!- TISSUE SPECIFICITY: Expressed in flowers and pollen.
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=CAA23000.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79373.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035356; CAA23000.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79373.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84935.1; -; Genomic_DNA.
DR EMBL; AK226186; BAE98351.1; -; mRNA.
DR PIR; T05571; T05571.
DR RefSeq; NP_194194.2; NM_118596.3.
DR AlphaFoldDB; Q9SB58; -.
DR SMR; Q9SB58; -.
DR STRING; 3702.AT4G24630.1; -.
DR iPTMnet; Q9SB58; -.
DR SwissPalm; Q9SB58; -.
DR PaxDb; Q9SB58; -.
DR PRIDE; Q9SB58; -.
DR ProteomicsDB; 242974; -.
DR EnsemblPlants; AT4G24630.1; AT4G24630.1; AT4G24630.
DR GeneID; 828565; -.
DR Gramene; AT4G24630.1; AT4G24630.1; AT4G24630.
DR KEGG; ath:AT4G24630; -.
DR Araport; AT4G24630; -.
DR TAIR; locus:2121949; AT4G24630.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_018741_2_1_1; -.
DR InParanoid; Q9SB58; -.
DR OMA; SVPKRKW; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q9SB58; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q9SB58; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SB58; baseline and differential.
DR Genevisible; Q9SB58; 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; 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..407
FT /note="Protein S-acyltransferase 8"
FT /id="PRO_0000312030"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 136..186
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M306"
SQ SEQUENCE 407 AA; 46747 MW; 523003A85C366340 CRC64;
MTQRVFQVWK GSNKFILGGR LIFGPDARSL PLTLLLIIVP VVLFCVFVAR HLRHEFSPYN
AGYAIMVVAI LFTIYVLILL FFTSARDPGI VPRNSHPPEE DLRYETTVSA DGRQTPSVQI
PRTKEVIVNG VSVRVKYCDT CMLYRPPRCS HCSICNNCVE RFDHHCPWVG QCIGLRNYRY
FFMFVSSSTL LCIYIFSMSA VYIKILMDHQ QATVWRAMKE SPWAVVLMIY CFIALWFVGG
LTAFHLYLIS TNQTTYEKLR YRSSHSRSIV YNRGCPNNFL EVFCSKVKPS RNNFRAFIEE
EPPRVITLPS TTRESGEAED ENVTRRQKVE DDLDIGDDLM NLSRRCNAED ANNNQPHHTL
DIDHERAGSI RTEARHESWG RRSGSWDVAA TDVRESRSYA TAKDGRG
