ID   ETO1_ARATH              Reviewed;         951 AA.
AC   O65020; F4J4J0; Q6PWY3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 148.
DE   RecName: Full=Ethylene-overproduction protein 1;
DE   AltName: Full=Protein ETHYLENE OVERPRODUCER 1;
DE            Short=Protein ETO1;
GN   Name=ETO1; OrderedLocusNames=At3g51770; ORFNames=ATEM1.2;
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], FUNCTION, INTERACTION WITH ACS5 AND CUL3A, AND
RP   MUTAGENESIS OF PHE-466.
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=10645728; DOI=10.1023/a:1006395324818;
RA   Comella P., Wu H.-J., Laudie M., Berger C., Cooke R., Delseny M.,
RA   Grellet F.;
RT   "Fine sequence analysis of 60 kb around the Arabidopsis thaliana AtEm1
RT   locus on chromosome III.";
RL   Plant Mol. Biol. 41:687-700(1999).
RN   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=16091151; DOI=10.1186/1471-2229-5-14;
RA   Yoshida H., Nagata M., Saito K., Wang K.L., Ecker J.R.;
RT   "Arabidopsis ETO1 specifically interacts with and negatively regulates type
RT   2 1-aminocyclopropane-1-carboxylate synthases.";
RL   BMC Plant Biol. 5:14-14(2005).
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, DISRUPTION PHENOTYPE, AND
RP   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: Essential 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. {ECO:0000269|PubMed:15118728,
CC       ECO:0000269|PubMed:16091151, ECO:0000269|PubMed:18808454}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with the C-terminal domain of ACS4, ACS5 AND ACS9.
CC       Interacts with CUL3A. Putative component of a ubiquitin ligase complex
CC       containing CUL3. {ECO:0000269|PubMed:15118728,
CC       ECO:0000269|PubMed:18808454}.
CC   -!- INTERACTION:
CC       O65020; Q37001: ACS5; NbExp=3; IntAct=EBI-593440, EBI-593450;
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=O65020-1; Sequence=Displayed;
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   -!- DISRUPTION PHENOTYPE: Compact rosette with smaller leaves, reduced
CC       petiole lengths and shorter inflorescences.
CC       {ECO:0000269|PubMed:18808454}.
CC   -!- SIMILARITY: Belongs to the ETO1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC14404.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAC14404.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY572791; AAT01656.1; -; mRNA.
DR   EMBL; AF049236; AAC14404.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78840.1; -; Genomic_DNA.
DR   PIR; T51148; T51148.
DR   RefSeq; NP_190745.6; NM_115036.7.
DR   AlphaFoldDB; O65020; -.
DR   BioGRID; 9658; 3.
DR   IntAct; O65020; 1.
DR   STRING; 3702.AT3G51770.2; -.
DR   PaxDb; O65020; -.
DR   PeptideAtlas; O65020; -.
DR   PRIDE; O65020; -.
DR   ProteomicsDB; 222297; -. [O65020-1]
DR   GeneID; 824340; -.
DR   KEGG; ath:AT3G51770; -.
DR   Araport; AT3G51770; -.
DR   eggNOG; ENOG502QPQB; Eukaryota.
DR   HOGENOM; CLU_015650_0_0_1; -.
DR   InParanoid; O65020; -.
DR   PhylomeDB; O65020; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O65020; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O65020; baseline and differential.
DR   Genevisible; O65020; 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; IPR019734; TPR_repeat.
DR   PANTHER; PTHR44203; PTHR44203; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   PROSITE; PS50005; TPR; 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..951
FT                   /note="Ethylene-overproduction protein 1"
FT                   /id="PRO_0000106289"
FT   DOMAIN          242..342
FT                   /note="BTB"
FT   REPEAT          443..476
FT                   /note="TPR 1"
FT   REPEAT          539..572
FT                   /note="TPR 2"
FT   REPEAT          573..605
FT                   /note="TPR 3"
FT   REPEAT          698..731
FT                   /note="TPR 4"
FT   REPEAT          772..805
FT                   /note="TPR 5"
FT   REPEAT          807..837
FT                   /note="TPR 6"
FT   REPEAT          868..901
FT                   /note="TPR 7"
FT   REPEAT          903..934
FT                   /note="TPR 8"
FT   REGION          15..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          815..854
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         466
FT                   /note="F->I: In eto1-5; induces overproduction of ethylene
FT                   due to higher stability of ACS5."
FT                   /evidence="ECO:0000269|PubMed:15118728"
FT   CONFLICT        34
FT                   /note="T -> S (in Ref. 3; AEE78840)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   951 AA;  107040 MW;  E275B8B440163B70 CRC64;
     MRSLKLAEGC KGTQVYALNP SAPTPPPPPG NSSTGGGGGG GSGGGTGGVG DKLLQHLSDH
     LRVNSVRSKS SRTYPPPTQP NAVVSPEFLL PCGLPVTDLL EPQIDPCLKF VDLVEKMAQV
     YRRIENCSQF EKSGAYLEQC AIFRGISDPK LFRRSLRSSR QHAVDVHAKV VLASWLRFER
     REDELIGTTS MDCCGRNLEC PKATLVSGYD PESVYDPCVC SGASRSEMMN EDECSTSQEV
     DYDMSFCIGD EEVRCVRYKI ASLSRPFKAM LYGGFREMKR ATINFTQNGI SVEGMRAAEI
     FSRTNRLDNF PPNVVLELLK LANRFCCDEL KSACDSHLAH LVNSLDEAML LIEYGLEEAA
     YLLVAACLQV FLRELPSSMH NPNVIKIFCS AEGRERLASL GHASFTLYFF LSQIAMEDDM
     KSNTTVMLLE RLVECAVDSW EKQLAYHQLG VVMLERKEYK DAQRWFNAAV EAGHLYSLVG
     VARTKFKRDH RYSAYKIINS LISDHKATGW MHQERSLYCS GKEKLLDLDT ATEFDPTLTF
     PYKFRAVALV EENQFGAAIA ELNKILGFKA SPDCLEMRAW ISIGMEDYEG ALKDIRALLT
     LEPNFMMFNW KIHGDHMVEL LRPLAQQWSQ ADCWMQLYDR WSSVDDIGSL AVVHHMLAND
     PGKSLLRFRQ SLLLLRLNCQ KAAMRSLRLA RNHSKSEHER LVYEGWILYD TGHREEALAK
     AEESISIQRS FEAFFLKAYA LADSTLDPDS SNYVIQLLQE ALKCPSDGLR KGQALNNLGS
     VYVDCEKLDL AADCYTNALT IKHTRAHQGL ARVYHLKNQR KAAYDEMTKL IEKAQNNASA
     YEKRSEYCDR EMAQSDLCLA TQLDPLRTYP YRYRAAVLMD DHKESEAIDE LSRAISFKPD
     LQLLHLRAAF YDSMGEGASA IKDCEAALCI DPGHADTLEL YHKAREPNDQ K