ZDHC5_ARATH
ID ZDHC5_ARATH Reviewed; 397 AA.
AC Q3EBC2; Q0WR40; Q9CAW1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Probable protein S-acyltransferase 17;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At3g04970;
DE AltName: Full=Zinc finger DHHC domain-containing protein At3g04970;
GN Name=PAT17; OrderedLocusNames=At3g04970; ORFNames=T9J14.8;
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] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3EBC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3EBC2-2; Sequence=VSP_036314, VSP_036315;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009465; AAG51421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74169.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74170.1; -; Genomic_DNA.
DR EMBL; BX824996; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK228483; BAF00409.1; -; mRNA.
DR RefSeq; NP_187148.2; NM_111369.4. [Q3EBC2-1]
DR RefSeq; NP_974224.1; NM_202495.2. [Q3EBC2-2]
DR AlphaFoldDB; Q3EBC2; -.
DR STRING; 3702.AT3G04970.1; -.
DR PaxDb; Q3EBC2; -.
DR ProteomicsDB; 242953; -. [Q3EBC2-1]
DR EnsemblPlants; AT3G04970.1; AT3G04970.1; AT3G04970. [Q3EBC2-1]
DR EnsemblPlants; AT3G04970.2; AT3G04970.2; AT3G04970. [Q3EBC2-2]
DR GeneID; 819657; -.
DR Gramene; AT3G04970.1; AT3G04970.1; AT3G04970. [Q3EBC2-1]
DR Gramene; AT3G04970.2; AT3G04970.2; AT3G04970. [Q3EBC2-2]
DR KEGG; ath:AT3G04970; -.
DR Araport; AT3G04970; -.
DR TAIR; locus:2114895; AT3G04970.
DR eggNOG; KOG1312; Eukaryota.
DR InParanoid; Q3EBC2; -.
DR OMA; CEYCHLE; -.
DR PhylomeDB; Q3EBC2; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q3EBC2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q3EBC2; baseline and differential.
DR Genevisible; Q3EBC2; 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; Alternative splicing; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..397
FT /note="Probable protein S-acyltransferase 17"
FT /id="PRO_0000363593"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 160..210
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 190
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 302..316
FT /note="TFKWREYISLNKKLS -> VLTFPSLEINYVSPS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036314"
FT VAR_SEQ 317..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036315"
FT CONFLICT 74
FT /note="D -> N (in Ref. 3; BX824996)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="P -> T (in Ref. 4; BAF00409)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> N (in Ref. 3; BX824996)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="V -> M (in Ref. 3; BX824996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 44946 MW; 1B179FB4FE9E7CF7 CRC64;
MAVQWLLVCH GMMTLTVVIS FLCGQWPIFK GTPFQWIHYF LTFGAYDYFL RFVGFVFGSK
GTDVILSVEY FCCDRPNPIL QVIYIAIMGS TYFLTAKSSF IYIPGYYLGD VHKYTSFLAV
IVGVILFLLT CFSDPGTVNA ENVSRYISAY PYDDIIYSKK ECSTCKIPKP ARSKHCSICN
RCVARFDHHC GWMNNCIGER NTKYFMAFLL WHFLLCLYGT VAIGFILAGR VKELRVVHIL
TVYYGVDKSF RSLAPRVIQW LVGTYNTQIL LMVFLAIVSL LLAGFFAYHA NLCLTNTTTN
ETFKWREYIS LNKKLSEAKA SAAALKAGMS CELKKPSAES KCFGLCGRSS AREEEVKADA
IAKRNLYDRG SFQNVSEIVF PLSSRPSSSN KSKRKSE
