PUB23_ARATH
ID PUB23_ARATH Reviewed; 411 AA.
AC Q84TG3; Q9SJ57;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase PUB23;
DE EC=2.3.2.27;
DE AltName: Full=Plant U-box protein 23;
DE AltName: Full=RING-type E3 ubiquitin transferase PUB23 {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 23;
GN Name=PUB23; OrderedLocusNames=At2g35930; ORFNames=F11F19.16;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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, AND MUTAGENESIS OF CYS-18 AND
RP TRP-45.
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, AND DISRUPTION PHENOTYPE.
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).
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 PUB22 and PUB24.
CC {ECO:0000269|PubMed:18664614, 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 -!- SUBUNIT: Interacts with RPN12A. {ECO:0000269|PubMed:18664614}.
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. {ECO:0000269|PubMed:18664614,
CC ECO:0000269|PubMed:18771922}.
CC -!- DISRUPTION PHENOTYPE: Increased tolerance to drought stress.
CC {ECO:0000269|PubMed:18664614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD21464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC007017; AAD21464.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC09178.1; -; Genomic_DNA.
DR EMBL; BT005829; AAO64764.1; -; mRNA.
DR EMBL; AK227343; BAE99354.1; -; mRNA.
DR PIR; G84774; G84774.
DR RefSeq; NP_181137.2; NM_129152.3.
DR AlphaFoldDB; Q84TG3; -.
DR SMR; Q84TG3; -.
DR BioGRID; 3510; 6.
DR IntAct; Q84TG3; 1.
DR STRING; 3702.AT2G35930.1; -.
DR PaxDb; Q84TG3; -.
DR PRIDE; Q84TG3; -.
DR EnsemblPlants; AT2G35930.1; AT2G35930.1; AT2G35930.
DR GeneID; 818166; -.
DR Gramene; AT2G35930.1; AT2G35930.1; AT2G35930.
DR KEGG; ath:AT2G35930; -.
DR Araport; AT2G35930; -.
DR TAIR; locus:2039265; AT2G35930.
DR eggNOG; ENOG502QR1A; Eukaryota.
DR HOGENOM; CLU_006348_1_1_1; -.
DR InParanoid; Q84TG3; -.
DR OMA; LEMADPM; -.
DR OrthoDB; 744311at2759; -.
DR PhylomeDB; Q84TG3; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q84TG3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q84TG3; baseline and differential.
DR Genevisible; Q84TG3; 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; 2.
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; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..411
FT /note="E3 ubiquitin-protein ligase PUB23"
FT /id="PRO_0000322167"
FT DOMAIN 11..86
FT /note="U-box"
FT REPEAT 132..173
FT /note="ARM 1"
FT REPEAT 175..203
FT /note="ARM 2"
FT REPEAT 221..261
FT /note="ARM 3"
FT REPEAT 263..306
FT /note="ARM 4"
FT MUTAGEN 18
FT /note="C->A: Loss of autoubiquitination."
FT /evidence="ECO:0000269|PubMed:18771922"
FT MUTAGEN 45
FT /note="W->A: Loss of autoubiquitination."
FT /evidence="ECO:0000269|PubMed:18771922"
SQ SEQUENCE 411 AA; 45823 MW; 383282956685D326 CRC64;
MSGGIMDEEI EIPPFFLCPI SLEIMKDPVI VSTGITYDRD SIEKWLFAGK KNSCPVTKQD
ITDADLTPNH TLRRLIQSWC TLNASYGVER IPTPRPPICK SEIEKLIRDS ASSHENQVKC
LKRLRQIVSE NATNKRCLEA AGVPEFLANI VSNDSENGSL TDEALNLLYH LETSETVLKN
LLNNKKDNNI VKSLTKIMQR GMYESRVYAT LLLKNILEVA DPMQSMTLKP EVFTEVVQIL
DDRISQKATK AAMHILVNIC PWGRNRHKAV EAGVISVIIE LLMDESFTSE RRGPEMAMVV
LDLLCQCAEG RAEFLNHGAA IAVVCKKILR VSQTASDRAV RVLLSVGRFC ATPALLHEML
QLGVVAKLCL VLQVSCGGKT KEKAKELLKL HARVWKDSPC LPKNMILAYP C
