ETOL2_ARATH
ID ETOL2_ARATH Reviewed; 925 AA.
AC Q9LV01; F4KF02; Q0WQF6; Q6PWY1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=ETO1-like protein 2;
DE AltName: Full=Ethylene overproducer 1-like protein 2;
GN Name=EOL2; OrderedLocusNames=At5g58550; ORFNames=MQJ2, MZN1.1;
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 [MRNA], AND INTERACTION WITH ACS5.
RX PubMed=15118728; DOI=10.1038/nature02516;
RA Wang K.L.-C., Yoshida H., Lurin C., Ecker J.R.;
RT "Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 protein.";
RL Nature 428:945-950(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-925.
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 [6]
RP DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=18808454; DOI=10.1111/j.1365-313x.2008.03693.x;
RA Christians M.J., Gingerich D.J., Hansen M., Binder B.M., Kieber J.J.,
RA Vierstra R.D.;
RT "The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate
RT ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase
RT levels.";
RL Plant J. 57:332-345(2009).
CC -!- FUNCTION: Potential regulator of the ethylene pathway, which acts by
CC regulating the stability of 1-aminocyclopropane-1-carboxylate synthase
CC (ACS) enzymes. May act as a substrate-specific adapter that connects
CC ACS enzymes, such as ACS5, to ubiquitin ligase complexes, leading to
CC proteasomal degradation of ACS enzymes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:18808454}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with the C-terminal domain of ACS5.
CC {ECO:0000269|PubMed:15118728}.
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=Q9LV01-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Constitutively expressed in green and etiolated
CC seedlings. {ECO:0000269|PubMed:18808454}.
CC -!- DOMAIN: The BTB/POZ-like domain may mediate the interaction with some
CC component of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- SIMILARITY: Belongs to the ETO1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY572793; AAT01658.1; -; mRNA.
DR EMBL; AB020755; BAA97325.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB025632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED97067.1; -; Genomic_DNA.
DR EMBL; AK228743; BAF00643.1; -; mRNA.
DR RefSeq; NP_200663.2; NM_125241.5.
DR AlphaFoldDB; Q9LV01; -.
DR SMR; Q9LV01; -.
DR BioGRID; 21212; 4.
DR IntAct; Q9LV01; 2.
DR STRING; 3702.AT5G58550.1; -.
DR PaxDb; Q9LV01; -.
DR PeptideAtlas; Q9LV01; -.
DR PRIDE; Q9LV01; -.
DR ProteomicsDB; 222328; -. [Q9LV01-1]
DR GeneID; 835968; -.
DR KEGG; ath:AT5G58550; -.
DR Araport; AT5G58550; -.
DR eggNOG; ENOG502QRY8; Eukaryota.
DR InParanoid; Q9LV01; -.
DR OrthoDB; 163959at2759; -.
DR PhylomeDB; Q9LV01; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LV01; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LV01; baseline and differential.
DR Genevisible; Q9LV01; AT.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010105; P:negative regulation of ethylene-activated signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR044631; ETO1-like.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44203; PTHR44203; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF00515; TPR_1; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Ethylene signaling pathway;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..925
FT /note="ETO1-like protein 2"
FT /id="PRO_0000106291"
FT DOMAIN 207..307
FT /note="BTB"
FT REPEAT 409..442
FT /note="TPR 1"
FT REPEAT 538..571
FT /note="TPR 2"
FT REPEAT 664..697
FT /note="TPR 3"
FT REPEAT 738..771
FT /note="TPR 4"
FT REPEAT 773..803
FT /note="TPR 5"
FT REPEAT 834..867
FT /note="TPR 6"
FT REPEAT 869..900
FT /note="TPR 7"
FT COILED 509..533
FT /evidence="ECO:0000255"
FT CONFLICT 477
FT /note="M -> L (in Ref. 5; BAF00643)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="I -> T (in Ref. 4; AED97067 and 5; BAF00643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 925 AA; 105490 MW; 59B826631A3168B6 CRC64;
MRNLKLFERF KSTQVHAFTT QDSPSTSSNG SPRMMKFLGH PKSKSRSLLP HGFPTTDLLE
PPLDSYLKPI DLVESLSNLY RRIESSSESE ASMLYLEQYA VLRSLGDAKL LRRCLLNARR
HAIDVPCKVV FSAWLRFFRR EHELVGVESM DCNGLASECP KTSLTHGCDL NVDDEGCECS
TVCEDEFGSD DVKISKADEF SGLDEVSDIS FCVGSEKAKC VRSRIAALSR PFEAMLYGSF
VESTTSEIDF SENGISIEAM LALNIYSRIK RVDLFRVETV FELLQLASKF CCDDLKSECE
ARLAASVTDL DKALTFVEYA LEERTTLLLS ACLQVFLREL PQSLHNPKVM RFFCSSEAKE
QLAFLGSECV FLLYYFLSQV GMEEKLTTDT MLILLERTRE FARTNWQKAL SLHQMGCVLF
ERKDYKAAQF HFRLASSLGH VYSLAGVSRT EYKQGKRYSA YRLMNFLISN HKPHGWMYQE
RSLYNVGVEK LKDLATATEL DPTLSFPYKY RAVMKFEQKQ IKEAFQEIDR LIQFKLSPEC
LELRAWLYLA TGDRESCLRD LRAVLSLEPN YVVFGGKMRD DLVEALTAQC IEVESEADCW
VRLFDRWSAV DDVASLAVVH QMLQNDPSKN FLRFRQSLLL LRLNCQGAAM RCLRMAWNLA
TSEAERLVYE GWLLYDMGYV EETLTKAEEA ISIQRSFEAF FLKAYALADK NLDADEISCV
VQVLEEALKC PSDGLRKGQA LNNLGSIYIN LGMLDQAETA YKNAIEIKHI RARQGLARVY
FLKNQRKEAC EEMTKLIEKS CSKAAAYEKR SEYCEREKAK EDLDMATTLD PLRTYPYRYR
AAVLMDDQRE TEAVEELSKA IAFRPELQTL HLRAAFHEAT GNLSLATQDC EAALCLDPNH
TETLHLYSRS KDQASSIDNT IFGLD
