ZDH22_ARATH
ID ZDH22_ARATH Reviewed; 620 AA.
AC Q52T38; Q0WQT8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Protein S-acyltransferase 24;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing S-palmitoyltransferase;
DE AltName: Full=Palmitoyltransferase TIP1;
DE AltName: Full=Protein TIP GROWTH DEFECTIVE 1;
DE Short=AtTIP1;
DE AltName: Full=Zinc finger DHHC domain-containing protein TIP1;
GN Name=PAT24; Synonyms=TIP1; OrderedLocusNames=At5g20350; ORFNames=F5O24.240;
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 [MRNA], TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16100337; DOI=10.1105/tpc.105.031237;
RA Hemsley P.A., Kemp A.C., Grierson C.S.;
RT "The TIP GROWTH DEFECTIVE1 S-acyltransferase regulates plant cell growth in
RT Arabidopsis.";
RL Plant Cell 17:2554-2563(2005).
RN [2]
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 [3]
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 [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 DISRUPTION PHENOTYPE.
RX PubMed=8022944; DOI=10.1104/pp.103.3.979;
RA Schiefelbein J., Galway M., Masucci J., Ford S.;
RT "Pollen tube and root-hair tip growth is disrupted in a mutant of
RT Arabidopsis thaliana.";
RL Plant Physiol. 103:979-985(1993).
RN [6]
RP DISRUPTION PHENOTYPE.
RX AGRICOLA=IND20904399; DOI=10.1046/j.1469-8137.1998.00896.x;
RA Ryan E., Grierson C.S., Cavell A., Steer M., Dolan L.;
RT "TIP1 is required for both tip growth and non-tip growth in Arabidopsis.";
RL New Phytol. 138:49-58(1998).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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: Palmitoyltransferase involved in cell growth regulation.
CC {ECO:0000269|Ref.7}.
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 membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in root, leaf, inflorescence stem, pollen
CC and floral tissue. {ECO:0000269|PubMed:16100337,
CC ECO:0000269|PubMed:22968831}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC -!- DISRUPTION PHENOTYPE: Plants have defects in root hair growth and
CC pollen tube germination. {ECO:0000269|PubMed:16100337,
CC ECO:0000269|PubMed:8022944, ECO:0000269|Ref.6}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY965346; AAX89384.1; -; mRNA.
DR EMBL; AF296825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92834.1; -; Genomic_DNA.
DR EMBL; AK228596; BAF00511.1; -; mRNA.
DR RefSeq; NP_197535.2; NM_122042.4.
DR AlphaFoldDB; Q52T38; -.
DR SMR; Q52T38; -.
DR STRING; 3702.AT5G20350.1; -.
DR iPTMnet; Q52T38; -.
DR SwissPalm; Q52T38; -.
DR PaxDb; Q52T38; -.
DR PRIDE; Q52T38; -.
DR ProteomicsDB; 242954; -.
DR EnsemblPlants; AT5G20350.1; AT5G20350.1; AT5G20350.
DR GeneID; 832157; -.
DR Gramene; AT5G20350.1; AT5G20350.1; AT5G20350.
DR KEGG; ath:AT5G20350; -.
DR Araport; AT5G20350; -.
DR TAIR; locus:2149309; AT5G20350.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_031257_3_1_1; -.
DR InParanoid; Q52T38; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q52T38; -.
DR BRENDA; 2.3.1.225; 399.
DR PRO; PR:Q52T38; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q52T38; baseline and differential.
DR Genevisible; Q52T38; AT.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0000035; F:acyl binding; IDA:TAIR.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; ANK repeat; Cytoplasmic vesicle; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..620
FT /note="Protein S-acyltransferase 24"
FT /id="PRO_0000212915"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 64..93
FT /note="ANK 1"
FT REPEAT 97..126
FT /note="ANK 2"
FT REPEAT 164..193
FT /note="ANK 3"
FT REPEAT 197..226
FT /note="ANK 4"
FT REPEAT 232..261
FT /note="ANK 5"
FT DOMAIN 371..421
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 620 AA; 68234 MW; BF6247CB99911659 CRC64;
MSSEIEVVEE IQSNPKENGE SSSKGIEEES LKNDVYTAAA YGDLEKLHRL VECEGSSVSE
PDALGYYALQ WSALNNRVAV AQYLIEHGGD VNATDHTGQT ALHWSAVRGA IQVAELLLQE
GARVDATDMY GYQATHVAAQ YGQTAFLCHV VSKWNADPDV PDNDGRSPLH WAAYKGFADS
IRLLLFLDAY RGRQDKEGCT PLHWAAIRGN LEACTVLVQA GKKEDLMITD KTGLTPAQLA
AEKNHRQVSF FLGNARSLLE KRCDGSSPLG RLSKLGLAPV LWIMILLLLL VYTNSVVLAS
NLPKLTTGIG ALAWLGFILA TAGLFLFYRC SRKDPGYIRM NIHDPQTMKD DEPLLKIELN
NPALLAGNWT QLCATCKIIR PLRAKHCSTC DRCVEQFDHH CPWVSNCVGK KNKWEFFLFL
LLEVLAMLIT GGVTLARVLS DPSAPSSFGA WMSHVASNHV GALSFLLVEF CLFFSVAVLT
VIQASQISRN ITTNEMANAL RYSYLRGPGG RFRNPYDLGC RRNCSDFLVK GYNEDIECHE
EDATQRPEGI SMMQMQRNPN LQNGNGHVAI DVNPTHNSQS AHVHSANCSH SHNSKSKSDN
VPLGLGLGLS RNPTRPVVSP
