PUB24_ARATH
ID PUB24_ARATH Reviewed; 456 AA.
AC Q9SF15; B9DGA6; F4J7H3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=E3 ubiquitin-protein ligase PUB24;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 24;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB24 {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 24;
GN Name=PUB24; OrderedLocusNames=At3g11840; ORFNames=F26K24.13;
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;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11495788; DOI=10.1016/s1360-1385(01)01960-4;
RA Azevedo C., Santos-Rosa M.J., Shirasu K.;
RT "The U-box protein family in plants.";
RL Trends Plant Sci. 6:354-358(2001).
RN [7]
RP GENE FAMILY ORGANIZATION.
RX PubMed=14657406; DOI=10.1104/pp.103.029553;
RA Mudgil Y., Shiu S.-H., Stone S.L., Salt J.N., Goring D.R.;
RT "A large complement of the predicted Arabidopsis ARM repeat proteins are
RT members of the U-box E3 ubiquitin ligase family.";
RL Plant Physiol. 134:59-66(2004).
RN [8]
RP FUNCTION, INDUCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF CYS-16 AND
RP TRP-43.
RX PubMed=18771922; DOI=10.1016/j.cub.2008.07.085;
RA Trujillo M., Ichimura K., Casais C., Shirasu K.;
RT "Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase
RT triplet in Arabidopsis.";
RL Curr. Biol. 18:1396-1401(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that acts as negative regulator
CC of the immunity triggered by the pathogen-associated molecular patterns
CC (PAMPs), in association with PUB22 and PUB23.
CC {ECO:0000269|PubMed:18771922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- INDUCTION: By the bacterial elicitor flg22, and bacterial and oomycete
CC pathogens. {ECO:0000269|PubMed:18771922}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:18771922}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH19773.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC016795; AAF23200.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75107.2; -; Genomic_DNA.
DR EMBL; AK228955; BAF00844.1; -; mRNA.
DR EMBL; AK317081; BAH19773.1; ALT_INIT; mRNA.
DR EMBL; AY084238; AAM67265.1; -; mRNA.
DR RefSeq; NP_566402.2; NM_112017.4.
DR AlphaFoldDB; Q9SF15; -.
DR SMR; Q9SF15; -.
DR STRING; 3702.AT3G11840.1; -.
DR PaxDb; Q9SF15; -.
DR PRIDE; Q9SF15; -.
DR ProteomicsDB; 226253; -.
DR EnsemblPlants; AT3G11840.1; AT3G11840.1; AT3G11840.
DR GeneID; 820357; -.
DR Gramene; AT3G11840.1; AT3G11840.1; AT3G11840.
DR KEGG; ath:AT3G11840; -.
DR Araport; AT3G11840; -.
DR eggNOG; ENOG502SC8Q; Eukaryota.
DR HOGENOM; CLU_006348_1_0_1; -.
DR InParanoid; Q9SF15; -.
DR OMA; VNCFEEI; -.
DR OrthoDB; 666272at2759; -.
DR PhylomeDB; Q9SF15; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SF15; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF15; baseline and differential.
DR Genevisible; Q9SF15; AT.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045185; PUB22/23/24-like.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22849; PTHR22849; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51698; U_BOX; 1.
PE 1: Evidence at protein level;
KW Plant defense; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..456
FT /note="E3 ubiquitin-protein ligase PUB24"
FT /id="PRO_0000322168"
FT DOMAIN 9..83
FT /note="U-box"
FT MUTAGEN 16
FT /note="C->A: Loss of autoubiquitination."
FT /evidence="ECO:0000269|PubMed:18771922"
FT MUTAGEN 43
FT /note="W->A: Loss of autoubiquitination."
FT /evidence="ECO:0000269|PubMed:18771922"
SQ SEQUENCE 456 AA; 51287 MW; 509873CAC065BB8D CRC64;
MDQEEEEIEI PNYFICPISL EIMKDPVTTV SGITYDRQNI VKWLEKVPSC PVTKQPLPLD
SDLTPNHMLR RLIQHWCVEN ETRGVVRIST PRVPPGKLNV VEEIKNLKKF GQEALGREET
LQKLEVLAMD GNNRRLMCEC GVHKSLILFV VKCTSEDEDG RRRIKGLDES LRLLHLIGIP
SNDAKTILME NDRVMESLTW VLHQEDFLSK AYTIVLLRNL TEYTSSHIVE RLNPEIFKGI
IGFLKDVVNS VNRTSPTVRE TVQSSSRPSL GKTEPSKLDH SLVIKQAVTA ALMILLETSS
WSRNRSLLVD LGAVSELIEL EISYTGEKRI TELMLGVLSR LCCCANGRAE ILAHRGGIAV
VTKRLLRVSP AADDRAISIL TTVSKFSPEN MVVEEMVNVG TVEKLCSVLG MDCGLNLKEK
AKEILKDHFD EWKKFPCIDI TLLTKLLSIS PKGPKI
