ID   ETOL1_ARATH             Reviewed;         888 AA.
AC   Q9ZQX6; Q0WP84;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 140.
DE   RecName: Full=ETO1-like protein 1;
DE   AltName: Full=Ethylene overproducer 1-like protein 1;
GN   Name=EOL1; OrderedLocusNames=At4g02680; ORFNames=T10P11.24;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   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   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   [6]
RP   FUNCTION, INTERACTION WITH ACS4; ACS5 AND ACS9, 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: Possible 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 ACS4, ACS5 AND ACS9.
CC       {ECO:0000269|PubMed:15118728, ECO:0000269|PubMed:18808454}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers.
CC       {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}.
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DR   EMBL; AY572792; AAT01657.1; -; mRNA.
DR   EMBL; AC002330; AAC78270.1; -; Genomic_DNA.
DR   EMBL; AL161495; CAB77753.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82213.1; -; Genomic_DNA.
DR   EMBL; AK229195; BAF01065.1; -; mRNA.
DR   PIR; T01081; T01081.
DR   RefSeq; NP_192177.1; NM_116502.4.
DR   AlphaFoldDB; Q9ZQX6; -.
DR   SMR; Q9ZQX6; -.
DR   BioGRID; 13494; 2.
DR   IntAct; Q9ZQX6; 2.
DR   STRING; 3702.AT4G02680.1; -.
DR   PaxDb; Q9ZQX6; -.
DR   PRIDE; Q9ZQX6; -.
DR   ProteomicsDB; 222356; -.
DR   EnsemblPlants; AT4G02680.1; AT4G02680.1; AT4G02680.
DR   GeneID; 828205; -.
DR   Gramene; AT4G02680.1; AT4G02680.1; AT4G02680.
DR   KEGG; ath:AT4G02680; -.
DR   Araport; AT4G02680; -.
DR   TAIR; locus:2132402; AT4G02680.
DR   eggNOG; ENOG502QPQB; Eukaryota.
DR   HOGENOM; CLU_015650_0_0_1; -.
DR   InParanoid; Q9ZQX6; -.
DR   OMA; AWQEATT; -.
DR   OrthoDB; 142366at2759; -.
DR   PhylomeDB; Q9ZQX6; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9ZQX6; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9ZQX6; baseline and differential.
DR   Genevisible; Q9ZQX6; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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   GO; GO:0010364; P:regulation of ethylene biosynthetic process; IDA:TAIR.
DR   Gene3D; 1.25.40.10; -; 3.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR044631; ETO1-like.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44203; PTHR44203; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Ethylene signaling pathway; Reference proteome; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN           1..888
FT                   /note="ETO1-like protein 1"
FT                   /id="PRO_0000106290"
FT   DOMAIN          180..280
FT                   /note="BTB"
FT   REPEAT          381..414
FT                   /note="TPR 1"
FT   REPEAT          441..477
FT                   /note="TPR 2"
FT   REPEAT          511..544
FT                   /note="TPR 3"
FT   REPEAT          637..670
FT                   /note="TPR 4"
FT   REPEAT          711..744
FT                   /note="TPR 5"
FT   REPEAT          807..840
FT                   /note="TPR 6"
FT   REPEAT          842..873
FT                   /note="TPR 7"
FT   COILED          755..793
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   888 AA;  101043 MW;  7CFD01AF64E03437 CRC64;
     MRTFYPSDSC KESQLDSLNP QSWLQVERGK LSSSASSSAP LCRESFIKVP EPQILPHYKP
     LDYVEVLAQI HEELDTCPLQ ERSILYLLQY QVFRGLGETK LRRRSLQSAW QEATTVHEKV
     VFGSWLRYEK QGEEVITDLL SSCGKYSEEF VPLDIASYFP ATTASSPEAA SVKTNRSVSK
     NVVFKIGEEK IACQRRKIAS LSAPFHAMLY GNFTESLLDE IDMSENHVSS SAMRVVRDFS
     VVGVLIGVSK NLLLEVLVFA NKFCCERLKD ACDRELASLI SSMECAIELM DFALEENSPI
     LASSCLQVFL YEMPDSLNDE RVVEVLTRVN RSQVSTMAGK APFSLYSCLS EVSMCIDPRS
     DRTLGFLEKL VDFAENDRQQ VLGFHRLGCM RLLRKEYREA EEAFETAFNL GHVYSATGLA
     RLGYIQGHRL WAYEKLSSVI SSVSPPLGWM YQERSFYCEG DKKLEDLEKA TELDPTLTYP
     YMYRAVTRMS KQNAKAALEE INRILGFKLA LECLEIRFCL YLGMDDYEAA LRDIQAALTL
     CPDYRMFDGK VAGRQLQTLV YEHVENWTTA DCWMQLYEKW SNVDDIGSLS VIYQMLESDA
     CKGVLYFRQS LLLLRLNCPE AAMRSLQLAR EHASSDHERL VYEGWILYDT GHCEEGLQKA
     KESIGIKRSF EAYFLQAYAL AESSLDPSSS STVVSLLEDA LKCPSDRLRK GQALNNLGSV
     YVDCEKLDLA ADCYINALKV RHTRAHQGLA RVHFLRNDKA AAYEEMTRLI EKAQNNASAY
     EKRSEYCDRE LAKSDLEMVT RLDPLRVYPY RYRAAVLMDS RKEREAITEL SRAIAFKADL
     HLLHLRAAFH EHIGDVTSAL RDCRAALSVD PNHQEMLELH SRVNSHEP