ZDH20_ARATH
ID ZDH20_ARATH Reviewed; 254 AA.
AC Q500Z2; Q9FYD4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Probable protein S-acyltransferase 15;
DE EC=2.3.1.225;
DE AltName: Full=Probable palmitoyltransferase At5g04270;
DE AltName: Full=Zinc finger DHHC domain-containing protein At5g04270;
GN Name=PAT15; OrderedLocusNames=At5g04270; ORFNames=F21E1_190, T19N18.6;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis cDNA clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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, 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: 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 -!- 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=CAC05509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391716; CAC05509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BT022075; AAY27062.1; -; mRNA.
DR AlphaFoldDB; Q500Z2; -.
DR SMR; Q500Z2; -.
DR STRING; 3702.AT5G04270.1; -.
DR PaxDb; Q500Z2; -.
DR PRIDE; Q500Z2; -.
DR EnsemblPlants; AT5G04270.1; AT5G04270.1; AT5G04270.
DR Gramene; AT5G04270.1; AT5G04270.1; AT5G04270.
DR Araport; AT5G04270; -.
DR TAIR; locus:2146713; AT5G04270.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_7_0_1; -.
DR InParanoid; Q500Z2; -.
DR PhylomeDB; Q500Z2; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q500Z2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q500Z2; baseline and differential.
DR Genevisible; Q500Z2; 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..254
FT /note="Probable protein S-acyltransferase 15"
FT /id="PRO_0000363605"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 75..125
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 105
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 254 AA; 28643 MW; 1D836983DF53E3D9 CRC64;
MGFVYYVTLF VFIDDWVGLQ SSAGKLNALL FSLLASLCLF SLSICVLVDP GRVPASYAPD
VEDSGWSNSN VTETRKCDKC FAYKPLRTHH CRVCRRCVLK MDHHCLWINN CVGYANYKAF
FILVFYATVA SIYSTVLLVC CAFKNGDSYA GNVPLKTFIV SCGIFMIGLS ITLGTLLCWH
IYLITHNMTT IEHYDSKRAS WLARKSGQSY RHQFDVGFYK NLTSVLGPNM IKWLCPTFTR
NPEDGISFSA SRDS
