KEG_ARATH
ID KEG_ARATH Reviewed; 1625 AA.
AC Q9FY48; Q27YP2; Q9FY47;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=E3 ubiquitin-protein ligase KEG;
DE EC=2.3.2.27;
DE EC=2.7.11.1;
DE AltName: Full=Protein KEEP ON GOING;
DE AltName: Full=RING finger protein KEG;
DE AltName: Full=RING-type E3 ubiquitin transferase KEG {ECO:0000305};
GN Name=KEG; OrderedLocusNames=At5g13530; ORFNames=T6I14.60, T6I14.70;
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], DISRUPTION PHENOTYPE, PHOSPHORYLATION,
RP UBIQUITINATION, AND INTERACTION WITH ABI5.
RX PubMed=17194765; DOI=10.1105/tpc.106.046532;
RA Stone S.L., Williams L.A., Farmer L.M., Vierstra R.D., Callis J.;
RT "KEEP ON GOING, a RING E3 ligase essential for Arabidopsis growth and
RT development, is involved in abscisic acid signaling.";
RL Plant Cell 18:3415-3428(2006).
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 GENE FAMILY ORGANIZATION.
RX PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT "Evaluation and classification of RING-finger domains encoded by the
RT Arabidopsis genome.";
RL Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN [5]
RP GENE FAMILY.
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLY-1144.
RX PubMed=18815384; DOI=10.1104/pp.108.127605;
RA Wawrzynska A., Christiansen K.M., Lan Y., Rodibaugh N.L., Innes R.W.;
RT "Powdery mildew resistance conferred by loss of the ENHANCED DISEASE
RT RESISTANCE1 protein kinase is suppressed by a missense mutation in KEEP ON
RT GOING, a regulator of abscisic acid signaling.";
RL Plant Physiol. 148:1510-1522(2008).
RN [7]
RP FUNCTION, AUTOUBIQUITINATION, PHOSPHORYLATION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 29-CYS--HIS-31 AND LYS-176.
RC STRAIN=cv. Columbia;
RX PubMed=20682837; DOI=10.1105/tpc.110.076075;
RA Liu H., Stone S.L.;
RT "Abscisic acid increases Arabidopsis ABI5 transcription factor levels by
RT promoting KEG E3 ligase self-ubiquitination and proteasomal degradation.";
RL Plant Cell 22:2630-2641(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EDR1, AND MUTAGENESIS OF
RP GLY-1144.
RX PubMed=21343429; DOI=10.1104/pp.110.171785;
RA Gu Y., Innes R.W.;
RT "The KEEP ON GOING protein of Arabidopsis recruits the ENHANCED DISEASE
RT RESISTANCE1 protein to trans-Golgi network/early endosome vesicles.";
RL Plant Physiol. 155:1827-1838(2011).
CC -!- FUNCTION: Mediates E2-dependent protein ubiquitination. Acts as a
CC negative regulator of abscisic acid signaling. Required for ABI5
CC degradation, by mediating its ubiquitination. Together with EDR1, may
CC regulate endocytic trafficking and/or the formation of signaling
CC complexes on trans-Golgi network (TGN)/ early endosome (EE) vesicles
CC during stress responses. {ECO:0000269|PubMed:18815384,
CC ECO:0000269|PubMed:20682837, ECO:0000269|PubMed:21343429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
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 ABI5 and EDR1. {ECO:0000269|PubMed:17194765,
CC ECO:0000269|PubMed:21343429}.
CC -!- INTERACTION:
CC Q9FY48; Q9SJN0: ABI5; NbExp=2; IntAct=EBI-1955729, EBI-1778690;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:21343429}. Early endosome
CC {ECO:0000269|PubMed:21343429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FY48-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues of young seedlings. In
CC flowering plants, only detected in the youngest part of the stem,
CC anthers and the receptacle of immature siliques. Not found in mature
CC leave, older parts of the stem, flower parts other than anthers or
CC mature siliques. {ECO:0000269|PubMed:18815384}.
CC -!- DEVELOPMENTAL STAGE: Expressed mainly in the actively growing and
CC dividing cells. {ECO:0000269|PubMed:18815384}.
CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC ubiquitin-conjugating enzyme. {ECO:0000250}.
CC -!- PTM: Autophosphotylated and autoubiquitinated in vitro.
CC {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC -!- PTM: Phosphorylation enhances self-ubiquitination.
CC {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC -!- PTM: Autoubiquitinated in response to abscisic acid (ABA) and
CC subsequently targeted to proteolysis. {ECO:0000269|PubMed:17194765,
CC ECO:0000269|PubMed:20682837}.
CC -!- DISRUPTION PHENOTYPE: Plants are seedling lethal and are hypersensitive
CC to glucose and abscisic acid. High accumulation of ABI5.
CC {ECO:0000269|PubMed:17194765, ECO:0000269|PubMed:20682837}.
CC -!- CAUTION: The protein kinase domain is predicted to be catalytically
CC inactive but PubMed:17194765 shows an in vitro activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05430.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAC05431.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ315360; ABC46683.1; -; mRNA.
DR EMBL; AL391710; CAC05430.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL391710; CAC05431.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91908.1; -; Genomic_DNA.
DR RefSeq; NP_196857.2; NM_121356.3. [Q9FY48-1]
DR AlphaFoldDB; Q9FY48; -.
DR SMR; Q9FY48; -.
DR BioGRID; 16475; 12.
DR IntAct; Q9FY48; 1.
DR STRING; 3702.AT5G13530.1; -.
DR iPTMnet; Q9FY48; -.
DR PaxDb; Q9FY48; -.
DR ProteomicsDB; 237084; -. [Q9FY48-1]
DR EnsemblPlants; AT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
DR GeneID; 831197; -.
DR Gramene; AT5G13530.1; AT5G13530.1; AT5G13530. [Q9FY48-1]
DR KEGG; ath:AT5G13530; -.
DR Araport; AT5G13530; -.
DR TAIR; locus:2185061; AT5G13530.
DR eggNOG; KOG0198; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR HOGENOM; CLU_243239_0_0_1; -.
DR InParanoid; Q9FY48; -.
DR OMA; IVRVEEY; -.
DR OrthoDB; 24404at2759; -.
DR PhylomeDB; Q9FY48; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9FY48; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FY48; baseline and differential.
DR Genevisible; Q9FY48; AT.
DR GO; GO:0005769; C:early endosome; IDA:TAIR.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0048589; P:developmental growth; IMP:TAIR.
DR GO; GO:0016197; P:endosomal transport; IMP:TAIR.
DR GO; GO:0045324; P:late endosome to vacuole transport; IDA:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0033184; P:positive regulation of histone ubiquitination; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0032940; P:secretion by cell; IMP:TAIR.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR044584; KEG.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR040847; SH3_15.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46960; PTHR46960; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF18346; SH3_15; 6.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Alternative splicing; ANK repeat;
KW ATP-binding; Endosome; Golgi apparatus; Kinase; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1625
FT /note="E3 ubiquitin-protein ligase KEG"
FT /id="PRO_0000356172"
FT DOMAIN 141..427
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 467..496
FT /note="ANK 1"
FT REPEAT 510..540
FT /note="ANK 2"
FT REPEAT 544..573
FT /note="ANK 3"
FT REPEAT 579..608
FT /note="ANK 4"
FT REPEAT 612..641
FT /note="ANK 5"
FT REPEAT 647..676
FT /note="ANK 6"
FT REPEAT 685..720
FT /note="ANK 7"
FT REPEAT 725..754
FT /note="ANK 8"
FT REPEAT 758..787
FT /note="ANK 9"
FT REPEAT 791..826
FT /note="ANK 10"
FT REPEAT 832..863
FT /note="ANK 11"
FT ZN_FING 10..56
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 29..31
FT /note="CGH->AGA: Small sterile plants unable to
FT polyubiquitinate ABI5."
FT /evidence="ECO:0000269|PubMed:20682837"
FT MUTAGEN 176
FT /note="K->R: Loss of kinase activity associated with the
FT loss of ABA-induced KEG autoubiquitination and subsequent
FT degradation."
FT /evidence="ECO:0000269|PubMed:20682837"
FT MUTAGEN 1144
FT /note="G->S: In keg-4/supp69; confers resistance to 6%
FT glucose and suppresses abscisic acid signaling. Suppression
FT of EDR1 disruption- (edr1-) mediated disease resistance.
FT Reduced endosomal localization but increased localization
FT to the endoplasmic reticulum and cytosol."
FT /evidence="ECO:0000269|PubMed:18815384,
FT ECO:0000269|PubMed:21343429"
SQ SEQUENCE 1625 AA; 178216 MW; 8F16ECA3DC32B9C4 CRC64;
MVGRVKVPCC SVCHTRYNED ERVPLLLQCG HGFCKDCLSK MFSTSSDTTL TCPRCRHVSV
VGNSVQGLRK NYAMLALIHA ASGGANFDCD YTDDEDDDDE EDGSDEDGAR AARGFHASSS
INSLCGPVIE VGAHPEMKLV RQIGEESSSG GFGGVEMWDA TVAGGGGRCK HRVAVKKMTL
TEDMDVEWMQ GQLESLRRAS MWCRNVCTFH GVVKMDGSLC LLMDRCFGSV QSEMQRNEGR
LTLEQILRYG ADVARGVAEL HAAGVICMNI KPSNLLLDAS GNAVVSDYGL APILKKPTCQ
KTRPEFDSSK VTLYTDCVTL SPHYTAPEAW GPVKKLFWED ASGVSPESDA WSFGCTLVEM
CTGSTPWDGL SREEIFQAVV KARKVPPQYE RIVGVGIPRE LWKMIGECLQ FKPSKRPTFN
AMLATFLRHL QEIPRSPSAS PDNGIAKICE VNIVQAPRAT NIGVFQDNPN NLHRVVLEGD
FEGVRNILAK AAAGGGGSSV RSLLEAQNAD GQSALHLACR RGSAELVEAI LEYGEANVDI
VDKDGDPPLV FALAAGSPQC VHVLIKKGAN VRSRLREGSG PSVAHVCSYH GQPDCMRELL
VAGADPNAVD DEGETVLHRA VAKKYTDCAI VILENGGSRS MTVSNAKCLT PLHMCVATWN
VAVIKRWVEV SSPEEISQAI NIPSPVGTAL CMAASIRKDH EKEGRELVQI LLAAGADPTA
QDAQHGRTAL HTAAMANNVE LVRVILDAGV NANIRNVHNT IPLHMALARG ANSCVSLLLE
SGSDCNIQDD EGDNAFHIAA DAAKMIRENL DWLIVMLRSP DAAVDVRNHS GKTVRDFLEA
LPREWISEDL MEALLKRGVH LSPTIYEVGD WVKFKRGITT PLHGWQGAKP KSVGFVQTIL
EKEDMIIAFC SGEARVLANE VVKLIPLDRG QHVRLRADVK EPRFGWRGQS RDSVGTVLCV
DEDGILRVGF PGASRGWKAD PAEMERVEEF KVGDWVRIRQ NLTSAKHGFG SVVPGSMGIV
YCVRPDSSLL VELSYLPNPW HCEPEEVEPV APFRIGDRVC VKRSVAEPRY AWGGETHHSV
GKISEIENDG LLIIEIPNRP IPWQADPSDM EKIDDFKVGD WVRVKASVSS PKYGWEDITR
NSIGVMHSLD EDGDVGIAFC FRSKPFSCSV TDVEKVTPFH VGQEIHMTPS ITQPRLGWSN
ETPATIGKVM RIDMDGTLSA QVTGRQTLWR VSPGDAELLS GFEVGDWVRS KPSLGNRPSY
DWSNVGRESI AVVHSIQETG YLELACCFRK GRWSTHYTDL EKIPALKVGQ FVHFQKGITE
PRWGWRAAKP DSRGIITTVH ADGEVRVAFF GLPGLWRGDP ADLEVEPMFE VGEWVRLREG
VSCWKSVGPG SVGVVHGVGY EGDEWDGTTS VSFCGEQERW AGPTSHLEKA KKLVVGQKTR
VKLAVKQPRF GWSGHSHGSV GTISAIDADG KLRIYTPAGS KTWMLDPSEV ETIEEEELKI
GDWVRVKASI TTPTYQWGEV NPSSTGVVHR MEDGDLCVSF CFLDRLWLCK AGELERIRPF
RIGDRVKIKD GLVTPRWGWG METHASKGHV VGVDANGKLR IKFLWREGRP WIGDPADIVL
DETSG
