ZDH14_ARATH
ID ZDH14_ARATH Reviewed; 307 AA.
AC Q8VYP5; Q9LZY3;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable protein S-acyltransferase 14;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At3g60800;
DE AltName: Full=Zinc finger DHHC domain-containing protein At3g60800;
GN Name=PAT14; OrderedLocusNames=At3g60800; ORFNames=T4C21_210;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=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 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 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 [6]
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.5}.
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: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305}; Multi-pass membrane 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=CAB82684.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162295; CAB82684.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80109.1; -; Genomic_DNA.
DR EMBL; AY070381; AAL49877.1; -; mRNA.
DR EMBL; AY096574; AAM20224.1; -; mRNA.
DR EMBL; AK229274; BAF01138.1; -; mRNA.
DR PIR; T47891; T47891.
DR RefSeq; NP_191639.2; NM_115944.4.
DR AlphaFoldDB; Q8VYP5; -.
DR SMR; Q8VYP5; -.
DR BioGRID; 10565; 1.
DR IntAct; Q8VYP5; 1.
DR STRING; 3702.AT3G60800.1; -.
DR SwissPalm; Q8VYP5; -.
DR PaxDb; Q8VYP5; -.
DR PRIDE; Q8VYP5; -.
DR ProteomicsDB; 232345; -.
DR EnsemblPlants; AT3G60800.1; AT3G60800.1; AT3G60800.
DR GeneID; 825251; -.
DR Gramene; AT3G60800.1; AT3G60800.1; AT3G60800.
DR KEGG; ath:AT3G60800; -.
DR Araport; AT3G60800; -.
DR TAIR; locus:2101806; AT3G60800.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_2_1_1; -.
DR InParanoid; Q8VYP5; -.
DR OMA; AICVLKM; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q8VYP5; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q8VYP5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYP5; baseline and differential.
DR Genevisible; Q8VYP5; AT.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0019707; F:protein-cysteine S-acyltransferase activity; IDA:TAIR.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
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 GO; GO:1900055; P:regulation of leaf senescence; IMP:TAIR.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IGI:TAIR.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..307
FT /note="Probable protein S-acyltransferase 14"
FT /id="PRO_0000363600"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 127..177
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 157
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 307 AA; 34688 MW; B7B2BE3A97D435CD CRC64;
MHRSGTTMAW NVFKFCTALR GLGSIMILLV LGVVGVTYYA VVLTNYGPAL SQGGLDSLAA
LTILILFHFL LAMLLWSYFS VVFTDPGVVP PNWRPSTDEE RGESDPLNSL DFVGLQSDSS
SSNPRVRFCR KCNQLKPSRC HHCSVCGRCV LKMDHHCVWV VNCVGALNYK YFLLFLFYTF
LETTLVTLVL MPHFIAFFSD EEIPGTPGTL ATTFLAFVLN LAFALSVMGF LIMHISLVAG
NTTTIEAYEK KTTTKWRYDL GKKKNFEQVF GMDKRYWLIP GYTEEDLRRM PELQGLEYPS
KPDFDSQ
