PUB22_ARATH
ID PUB22_ARATH Reviewed; 435 AA.
AC Q9SVC6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase PUB22 {ECO:0000303|PubMed:11495788};
DE EC=2.3.2.27 {ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:18771922, ECO:0000269|PubMed:23170036};
DE AltName: Full=Plant U-box protein 22 {ECO:0000303|PubMed:11495788};
DE AltName: Full=RING-type E3 ubiquitin transferase PUB22 {ECO:0000303|PubMed:11495788};
DE AltName: Full=U-box domain-containing protein 22 {ECO:0000303|PubMed:11495788};
GN Name=PUB22 {ECO:0000303|PubMed:11495788};
GN OrderedLocusNames=At3g52450 {ECO:0000312|Araport:AT3G52450};
GN ORFNames=F22O6.170 {ECO:0000312|EMBL:CAB43434.1};
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 Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
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 [7]
RP FUNCTION, AUTOUBIQUITINATION, INDUCTION, MUTAGENESIS OF CYS-13 AND TRP-40,
RP AND CATALYTIC ACTIVITY.
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).
RN [8]
RP FUNCTION, INTERACTION WITH RPN12A, SUBCELLULAR LOCATION, INDUCTION,
RP AUTOUBIQUITINATION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=18664614; DOI=10.1105/tpc.108.060699;
RA Cho S.K., Ryu M.Y., Song C., Kwak J.M., Kim W.T.;
RT "Arabidopsis PUB22 and PUB23 are homologous U-Box E3 ubiquitin ligases that
RT play combinatory roles in response to drought stress.";
RL Plant Cell 20:1899-1914(2008).
RN [9]
RP FUNCTION, MUTAGENESIS OF CYS-13, INTERACTION WITH EXO70B2,
RP AUTO-UBIQUITINATION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=23170036; DOI=10.1105/tpc.112.104463;
RA Stegmann M., Anderson R.G., Ichimura K., Pecenkova T., Reuter P.,
RA Zarsky V., McDowell J.M., Shirasu K., Trujillo M.;
RT "The ubiquitin ligase PUB22 targets a subunit of the exocyst complex
RT required for PAMP-triggered responses in Arabidopsis.";
RL Plant Cell 24:4703-4716(2012).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that negatively regulates water
CC stress response. May control in coordination with PUB23 a drought
CC signaling pathway by ubiquitinating cytosolic RPN12a. Acts as negative
CC regulator of the immunity triggered by the pathogen-associated
CC molecular patterns (PAMPs), in association with PUB23 and PUB24.
CC Regulates EXO70B2 ubiquitination and degradation via the 26S proteasome
CC to attenuate PAMP-induced signaling (PubMed:23170036).
CC {ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:18771922,
CC ECO:0000269|PubMed:23170036}.
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; Evidence={ECO:0000269|PubMed:18664614,
CC ECO:0000269|PubMed:18771922, ECO:0000269|PubMed:23170036};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:18771922,
CC ECO:0000269|PubMed:23170036}.
CC -!- SUBUNIT: Interacts with RPN12A (PubMed:18664614). Binds to EXO70B2
CC (PubMed:23170036). {ECO:0000269|PubMed:18664614,
CC ECO:0000269|PubMed:23170036}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18664614}.
CC -!- INDUCTION: By cold, drought and salt stresses, bacterial elicitor
CC flg22, and bacterial and oomycete pathogens.
CC {ECO:0000269|PubMed:18664614, ECO:0000269|PubMed:18771922}.
CC -!- PTM: Auto-ubiquitinated leading to degradation via the 26S proteasome.
CC This Auto-ubiquitination is repressed by the bacterial elicitor flg22
CC thus leading to a transiently increased protein stabilization and
CC accumulation. {ECO:0000269|PubMed:18664614,
CC ECO:0000269|PubMed:18771922, ECO:0000269|PubMed:23170036}.
CC -!- DISRUPTION PHENOTYPE: Increased tolerance to drought stress.
CC {ECO:0000269|PubMed:18664614}.
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DR EMBL; AL050300; CAB43434.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78947.1; -; Genomic_DNA.
DR EMBL; BT015763; AAU90053.1; -; mRNA.
DR EMBL; BT020203; AAV59269.1; -; mRNA.
DR EMBL; AK228993; BAF00881.1; -; mRNA.
DR PIR; T08454; T08454.
DR RefSeq; NP_190813.1; NM_115105.4.
DR AlphaFoldDB; Q9SVC6; -.
DR SMR; Q9SVC6; -.
DR BioGRID; 9728; 13.
DR STRING; 3702.AT3G52450.1; -.
DR PaxDb; Q9SVC6; -.
DR PRIDE; Q9SVC6; -.
DR EnsemblPlants; AT3G52450.1; AT3G52450.1; AT3G52450.
DR GeneID; 824410; -.
DR Gramene; AT3G52450.1; AT3G52450.1; AT3G52450.
DR KEGG; ath:AT3G52450; -.
DR Araport; AT3G52450; -.
DR TAIR; locus:2079964; AT3G52450.
DR eggNOG; ENOG502QR1A; Eukaryota.
DR HOGENOM; CLU_006348_1_0_1; -.
DR InParanoid; Q9SVC6; -.
DR OMA; IQAWCTM; -.
DR OrthoDB; 744311at2759; -.
DR PhylomeDB; Q9SVC6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SVC6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SVC6; baseline and differential.
DR Genevisible; Q9SVC6; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
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; IGI:TAIR.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0002679; P:respiratory burst involved in defense response; IGI:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR CDD; cd16664; RING-Ubox_PUB; 1.
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; IPR045210; RING-Ubox_PUB.
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 Cytoplasm; Plant defense; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..435
FT /note="E3 ubiquitin-protein ligase PUB22"
FT /id="PRO_0000322166"
FT DOMAIN 6..81
FT /note="U-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01034"
FT MUTAGEN 13
FT /note="C->A: Loss of autoubiquitination and increased
FT accumulation (at protein level). Increased levels of
FT EXO70B2 (at protein level)."
FT /evidence="ECO:0000269|PubMed:18771922,
FT ECO:0000269|PubMed:23170036"
FT MUTAGEN 40
FT /note="W->A: Loss of autoubiquitination."
FT /evidence="ECO:0000269|PubMed:18771922"
SQ SEQUENCE 435 AA; 48877 MW; E920AEF37545DF93 CRC64;
MDQEIEIPSF FLCPISLDIM KDPVIVSTGI TYDRESIEKW LFSGKKNSCP VTKQVITETD
LTPNHTLRRL IQSWCTLNAS YGIERIPTPK PPICKSEIEK LIKESSSSHL NQVKCLKRLR
QIVSENTTNK RCLEAAEVPE FLANIVSNSV DTYNSPSSSL SSSNLNDMCQ SNMLENRFDS
SRSLMDEALS VLYHLDTSET ALKSLLNNKK GTNLVKTLTK IMQRGIYESR AYAALLLKKL
LEVADPMQII LLERELFGEV IQILHDQISH KATRSAMQIL VITCPWGRNR HKAVEGGTIS
MIIELLMDDT FSSERRNSEM AMVVLDMLCQ CAEGRAEFLN HGAAIAVVSK KILRVSQITS
ERAVRVLLSV GRFCATPSLL QEMLQLGVVA KLCLVLQVSC GNKTKEKAKE LLKLHARVWR
ESPCVPRNLY DSYPA
