TIR1_ARATH
ID TIR1_ARATH Reviewed; 594 AA.
AC Q570C0; A5YZP2; B2CVU0; O24660;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein TRANSPORT INHIBITOR RESPONSE 1;
DE AltName: Full=Weak ethylene-insensitive protein 1;
GN Name=TIR1; Synonyms=FBL1, WEI1; OrderedLocusNames=At3g62980;
GN ORFNames=T20O10.80;
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-147 AND GLY-441.
RX PubMed=9436980; DOI=10.1101/gad.12.2.198;
RA Ruegger M., Dewey E., Gray W.M., Hobbie L., Turner J., Estelle M.;
RT "The TIR1 protein of Arabidopsis functions in auxin response and is related
RT to human SKP2 and yeast grr1p.";
RL Genes Dev. 12:198-207(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-380.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
RC cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0,
RC cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0,
RC cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1, and cv. Wassilewskija;
RX PubMed=17435248; DOI=10.1534/genetics.107.071928;
RA Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
RT "The genetic architecture of shoot branching in Arabidopsis thaliana: a
RT comparative assessment of candidate gene associations vs. quantitative
RT trait locus mapping.";
RL Genetics 176:1223-1236(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-594.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 429-579.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Bay-0, cv. Br-0, cv. C24, cv. Ct-1,
RC cv. Cvi-0, cv. Edi-0, cv. Ei-2, cv. Ga-0, cv. Gy-0, cv. Kas-2, cv. Ll-0,
RC cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Sorbo,
RC cv. Wa-1, cv. Wassilewskija, cv. Wei-0, and cv. Wt-5;
RX PubMed=18305205; DOI=10.1104/pp.108.116582;
RA Ehrenreich I.M., Purugganan M.D.;
RT "Sequence variation of microRNAs and their binding sites in Arabidopsis.";
RL Plant Physiol. 146:1974-1982(2008).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH SKP1A;
RP SKP1B AND CUL1, DOMAIN, AND MUTAGENESIS OF PRO-10.
RX PubMed=10398681; DOI=10.1101/gad.13.13.1678;
RA Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
RA Crosby W.L., Yang M., Ma H., Estelle M.;
RT "Identification of an SCF ubiquitin-ligase complex required for auxin
RT response in Arabidopsis thaliana.";
RL Genes Dev. 13:1678-1691(1999).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11077244; DOI=10.1016/s1360-1385(00)01769-6;
RA Xiao W., Jang J.-C.;
RT "F-box proteins in Arabidopsis.";
RL Trends Plant Sci. 5:454-457(2000).
RN [10]
RP INTERACTION WITH IAA7 AND IAA17.
RX PubMed=11713520; DOI=10.1038/35104500;
RA Gray W.M., Kepinski S., Rouse D., Leyser O., Estelle M.;
RT "Auxin regulates SCF(TIR1)-dependent degradation of AUX/IAA proteins.";
RL Nature 414:271-276(2001).
RN [11]
RP INTERACTION WITH THE CSN COMPLEX.
RX PubMed=11337587; DOI=10.1126/science.1059776;
RA Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT SCF(TIR1) in mediating auxin response.";
RL Science 292:1379-1382(2001).
RN [12]
RP INTERACTION WITH RBX1.
RX PubMed=12215511; DOI=10.1105/tpc.003178;
RA Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
RT "Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF
RT function.";
RL Plant Cell 14:2137-2144(2002).
RN [13]
RP INTERACTION WITH IAA3.
RX PubMed=14617065; DOI=10.1046/j.1365-313x.2003.01909.x;
RA Tian Q., Nagpal P., Reed J.W.;
RT "Regulation of Arabidopsis SHY2/IAA3 protein turnover.";
RL Plant J. 36:643-651(2003).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 574-TRP--LEU-594.
RX PubMed=12606727; DOI=10.1073/pnas.0438070100;
RA Alonso J.M., Stepanova A.N., Solano R., Wisman E., Ferrari S.,
RA Ausubel F.M., Ecker J.R.;
RT "Five components of the ethylene-response pathway identified in a screen
RT for weak ethylene-insensitive mutants in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2992-2997(2003).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IAA12; IAA7 AND
RP SKP1A/ASK1.
RX PubMed=15992545; DOI=10.1016/j.devcel.2005.05.014;
RA Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L.,
RA Ehrismann J.S., Juergens G., Estelle M.;
RT "Plant development is regulated by a family of auxin receptor F box
RT proteins.";
RL Dev. Cell 9:109-119(2005).
RN [16]
RP FUNCTION, AND INTERACTION WITH AUX/IAA PROTEINS AND AUXIN.
RX PubMed=15917797; DOI=10.1038/nature03543;
RA Dharmasiri N., Dharmasiri S., Estelle M.;
RT "The F-box protein TIR1 is an auxin receptor.";
RL Nature 435:441-445(2005).
RN [17]
RP FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN, AND MUTAGENESIS OF
RP PRO-10; VAL-33 AND LYS-35.
RX PubMed=15917798; DOI=10.1038/nature03542;
RA Kepinski S., Leyser O.;
RT "The Arabidopsis F-box protein TIR1 is an auxin receptor.";
RL Nature 435:446-451(2005).
RN [18]
RP FUNCTION, AND INDUCTION.
RX PubMed=16627744; DOI=10.1126/science.1126088;
RA Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M.,
RA Voinnet O., Jones J.D.G.;
RT "A plant miRNA contributes to antibacterial resistance by repressing auxin
RT signaling.";
RL Science 312:436-439(2006).
RN [19] {ECO:0007744|PDB:2P1M, ECO:0007744|PDB:2P1N, ECO:0007744|PDB:2P1O, ECO:0007744|PDB:2P1P, ECO:0007744|PDB:2P1Q}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH SKP1A; NATURAL
RP AUXIN INDOLE-3-ACETATE; SYNTHETIC AUXIN ANALOGS 1-NAPHTHALENE ACETATE AND
RP 2,4-DICHLOROPHENOXYACETATE; AUX/IAA POLYPEPTIDE SUBSTRATE AND MYO-INOSITOL
RP HEXAKISPHOSPHATE.
RX PubMed=17410169; DOI=10.1038/nature05731;
RA Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C., Robinson C.V.,
RA Estelle M., Zheng N.;
RT "Mechanism of auxin perception by the TIR1 ubiquitin ligase.";
RL Nature 446:640-645(2007).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA
RP POLYPEPTIDE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND MYO-INOSITOL
RP HEXAKISPHOSPHATE, AND FUNCTION.
RX PubMed=18391211; DOI=10.1073/pnas.0711146105;
RA Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S., Nozaki H.;
RT "Small-molecule agonists and antagonists of F-box protein-substrate
RT interactions in auxin perception and signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008).
CC -!- FUNCTION: Auxin receptor that mediates Aux/IAA proteins proteasomal
CC degradation and auxin-regulated transcription. The SCF(TIR1) E3
CC ubiquitin ligase complex is involved in auxin-mediated signaling
CC pathway that regulate root and hypocotyl growth, lateral root
CC formation, cell elongation, and gravitropism. Appears to allow
CC pericycle cells to overcome G2 arrest prior to lateral root
CC development. Plays a role in ethylene signaling in roots. Confers
CC sensitivity to the virulent bacterial pathogen P.syringae.
CC {ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:12606727,
CC ECO:0000269|PubMed:15917797, ECO:0000269|PubMed:15917798,
CC ECO:0000269|PubMed:15992545, ECO:0000269|PubMed:16627744,
CC ECO:0000269|PubMed:18391211, ECO:0000269|PubMed:9436980}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with auxin. Part of a SCF E3 ubiquitin ligase
CC complex SCF(TIR1) composed of SKP1, CUL1, RBX1 and TIR1. SCF(TIR1)
CC interacts with the COP9 signalosome (CSN) complex. Interacts with
CC Aux/IAA proteins (IAA3, IAA7, IAA12 and IAA17) in an auxin-dependent
CC manner. The interaction with IAA3, a negative regulator of auxin
CC responses, is promoted by auxin, but repressed by juglon (5-hydroxy-
CC 1,4-naphthoquinone). Interactions with auxin-responsive proteins is
CC inactivated by auxin antagonists. {ECO:0000269|PubMed:10398681,
CC ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:11713520,
CC ECO:0000269|PubMed:12215511, ECO:0000269|PubMed:14617065,
CC ECO:0000269|PubMed:15917797, ECO:0000269|PubMed:15917798,
CC ECO:0000269|PubMed:15992545, ECO:0000269|PubMed:17410169,
CC ECO:0000269|PubMed:18391211}.
CC -!- INTERACTION:
CC Q570C0; Q9SU81: At4g29700; NbExp=3; IntAct=EBI-307183, EBI-25530262;
CC Q570C0; P93830: IAA17; NbExp=2; IntAct=EBI-307183, EBI-632243;
CC Q570C0; Q38822: IAA3; NbExp=3; IntAct=EBI-307183, EBI-307174;
CC Q570C0; Q38825: IAA7; NbExp=8; IntAct=EBI-307183, EBI-602959;
CC Q570C0; Q39255: SKP1A; NbExp=11; IntAct=EBI-307183, EBI-532357;
CC Q570C0; Q9FHW7: SKP1B; NbExp=7; IntAct=EBI-307183, EBI-604076;
CC Q570C0; Q93Z00: TCP14; NbExp=3; IntAct=EBI-307183, EBI-4424563;
CC Q570C0; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-307183, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers. In
CC adult plants, mostly expressed in floral stigma, anther filaments,
CC abscission zones and vascular tissues. {ECO:0000269|PubMed:10398681,
CC ECO:0000269|PubMed:9436980}.
CC -!- DEVELOPMENTAL STAGE: Abundant expression in developing embryos. In
CC young seedlings, expressed in root apical meristem, and expanding
CC cotyledons and hypocotyls. In older seedlings, still expressed in root
CC apical meristems, but also in lateral root primordia, stipules, shoot
CC apical meristem and vascular tissues. {ECO:0000269|PubMed:10398681}.
CC -!- INDUCTION: Repressed by miR393a (microRNA) in response to flg-22
CC (flagellin-derived peptide 22). {ECO:0000269|PubMed:16627744}.
CC -!- DOMAIN: The F-box is necessary for the interaction with SKP1.
CC {ECO:0000269|PubMed:10398681}.
CC -!- DISRUPTION PHENOTYPE: Plant are deficient in a variety of auxin-
CC regulated growth processes including lateral root formation, and
CC hypocotyl and cell elongation. {ECO:0000269|PubMed:9436980}.
CC -!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a structural
CC cofactor.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD94031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF005047; AAB69175.1; -; Genomic_DNA.
DR EMBL; AF005048; AAB69176.1; -; mRNA.
DR EMBL; AL163816; CAB87743.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80419.1; -; Genomic_DNA.
DR EMBL; BT001946; AAN71945.1; -; mRNA.
DR EMBL; EF598824; ABR04117.1; -; Genomic_DNA.
DR EMBL; EF598825; ABR04118.1; -; Genomic_DNA.
DR EMBL; EF598826; ABR04119.1; -; Genomic_DNA.
DR EMBL; EF598827; ABR04120.1; -; Genomic_DNA.
DR EMBL; EF598828; ABR04121.1; -; Genomic_DNA.
DR EMBL; EF598829; ABR04122.1; -; Genomic_DNA.
DR EMBL; EF598830; ABR04123.1; -; Genomic_DNA.
DR EMBL; EF598831; ABR04124.1; -; Genomic_DNA.
DR EMBL; EF598832; ABR04125.1; -; Genomic_DNA.
DR EMBL; EF598833; ABR04126.1; -; Genomic_DNA.
DR EMBL; EF598834; ABR04127.1; -; Genomic_DNA.
DR EMBL; EF598835; ABR04128.1; -; Genomic_DNA.
DR EMBL; EF598836; ABR04129.1; -; Genomic_DNA.
DR EMBL; EF598837; ABR04130.1; -; Genomic_DNA.
DR EMBL; EF598838; ABR04131.1; -; Genomic_DNA.
DR EMBL; EF598839; ABR04132.1; -; Genomic_DNA.
DR EMBL; EF598840; ABR04133.1; -; Genomic_DNA.
DR EMBL; EF598841; ABR04134.1; -; Genomic_DNA.
DR EMBL; EF598842; ABR04135.1; -; Genomic_DNA.
DR EMBL; EF598843; ABR04136.1; -; Genomic_DNA.
DR EMBL; EF598844; ABR04137.1; -; Genomic_DNA.
DR EMBL; EF598845; ABR04138.1; -; Genomic_DNA.
DR EMBL; EF598846; ABR04139.1; -; Genomic_DNA.
DR EMBL; EF598847; ABR04140.1; -; Genomic_DNA.
DR EMBL; AK220790; BAD94031.1; ALT_INIT; mRNA.
DR EMBL; EU550991; ACB31753.1; -; Genomic_DNA.
DR EMBL; EU550992; ACB31754.1; -; Genomic_DNA.
DR EMBL; EU550993; ACB31755.1; -; Genomic_DNA.
DR EMBL; EU550994; ACB31756.1; -; Genomic_DNA.
DR EMBL; EU550995; ACB31757.1; -; Genomic_DNA.
DR EMBL; EU550996; ACB31758.1; -; Genomic_DNA.
DR EMBL; EU550997; ACB31759.1; -; Genomic_DNA.
DR EMBL; EU550998; ACB31760.1; -; Genomic_DNA.
DR EMBL; EU550999; ACB31761.1; -; Genomic_DNA.
DR EMBL; EU551000; ACB31762.1; -; Genomic_DNA.
DR EMBL; EU551001; ACB31763.1; -; Genomic_DNA.
DR EMBL; EU551002; ACB31764.1; -; Genomic_DNA.
DR EMBL; EU551003; ACB31765.1; -; Genomic_DNA.
DR EMBL; EU551004; ACB31766.1; -; Genomic_DNA.
DR EMBL; EU551005; ACB31767.1; -; Genomic_DNA.
DR EMBL; EU551006; ACB31768.1; -; Genomic_DNA.
DR EMBL; EU551007; ACB31769.1; -; Genomic_DNA.
DR EMBL; EU551008; ACB31770.1; -; Genomic_DNA.
DR EMBL; EU551009; ACB31771.1; -; Genomic_DNA.
DR EMBL; EU551010; ACB31772.1; -; Genomic_DNA.
DR EMBL; EU551011; ACB31773.1; -; Genomic_DNA.
DR EMBL; EU551012; ACB31774.1; -; Genomic_DNA.
DR EMBL; EU551013; ACB31775.1; -; Genomic_DNA.
DR EMBL; EU551014; ACB31776.1; -; Genomic_DNA.
DR PIR; T48087; T48087.
DR RefSeq; NP_567135.1; NM_116163.4.
DR PDB; 2P1M; X-ray; 1.80 A; B=1-594.
DR PDB; 2P1N; X-ray; 2.50 A; B/E=1-594.
DR PDB; 2P1O; X-ray; 1.90 A; B=1-594.
DR PDB; 2P1P; X-ray; 2.21 A; B=1-594.
DR PDB; 2P1Q; X-ray; 1.91 A; B=1-594.
DR PDB; 3C6N; X-ray; 2.60 A; B=1-594.
DR PDB; 3C6O; X-ray; 2.70 A; B=1-594.
DR PDB; 3C6P; X-ray; 2.70 A; B=1-594.
DR PDBsum; 2P1M; -.
DR PDBsum; 2P1N; -.
DR PDBsum; 2P1O; -.
DR PDBsum; 2P1P; -.
DR PDBsum; 2P1Q; -.
DR PDBsum; 3C6N; -.
DR PDBsum; 3C6O; -.
DR PDBsum; 3C6P; -.
DR AlphaFoldDB; Q570C0; -.
DR SMR; Q570C0; -.
DR BioGRID; 10787; 24.
DR ComplexPortal; CPX-1343; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1515; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1516; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR ComplexPortal; CPX-1517; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1518; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1519; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
DR ComplexPortal; CPX-1520; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR ComplexPortal; CPX-1521; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
DR ComplexPortal; CPX-1522; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
DR ComplexPortal; CPX-1523; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
DR ComplexPortal; CPX-1524; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1525; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1526; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR ComplexPortal; CPX-1527; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
DR ComplexPortal; CPX-1528; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
DR ComplexPortal; CPX-1529; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
DR ComplexPortal; CPX-1530; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
DR ComplexPortal; CPX-1531; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1532; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
DR ComplexPortal; CPX-1533; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1534; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
DR ComplexPortal; CPX-1535; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1536; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1537; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1538; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1539; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1540; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1541; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1542; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1543; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1544; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1545; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1546; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1547; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1548; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1549; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1550; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1551; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1552; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1553; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1554; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1555; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
DR ComplexPortal; CPX-1557; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1558; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1559; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR ComplexPortal; CPX-1560; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1561; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1562; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK6.
DR ComplexPortal; CPX-1563; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR ComplexPortal; CPX-1564; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK8.
DR ComplexPortal; CPX-1565; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK9.
DR ComplexPortal; CPX-1566; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK10.
DR ComplexPortal; CPX-1567; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1568; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1569; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR ComplexPortal; CPX-1570; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK14.
DR ComplexPortal; CPX-1571; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK15.
DR ComplexPortal; CPX-1572; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK16.
DR ComplexPortal; CPX-1573; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK17.
DR ComplexPortal; CPX-1574; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1575; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK19.
DR ComplexPortal; CPX-1576; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1577; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK21.
DR ComplexPortal; CPX-1578; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
DR ComplexPortal; CPX-1579; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
DR ComplexPortal; CPX-1580; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
DR ComplexPortal; CPX-1581; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
DR ComplexPortal; CPX-1582; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
DR ComplexPortal; CPX-1583; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK6.
DR ComplexPortal; CPX-1584; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
DR ComplexPortal; CPX-1585; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK8.
DR ComplexPortal; CPX-1586; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK9.
DR ComplexPortal; CPX-1587; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK10.
DR ComplexPortal; CPX-1588; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
DR ComplexPortal; CPX-1589; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
DR ComplexPortal; CPX-1590; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
DR ComplexPortal; CPX-1591; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK14.
DR ComplexPortal; CPX-1592; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK15.
DR ComplexPortal; CPX-1593; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK16.
DR ComplexPortal; CPX-1594; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK17.
DR ComplexPortal; CPX-1595; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
DR ComplexPortal; CPX-1596; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK19.
DR ComplexPortal; CPX-1597; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
DR ComplexPortal; CPX-1598; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK21.
DR DIP; DIP-31740N; -.
DR ELM; Q570C0; -.
DR IntAct; Q570C0; 21.
DR STRING; 3702.AT3G62980.1; -.
DR iPTMnet; Q570C0; -.
DR PaxDb; Q570C0; -.
DR PRIDE; Q570C0; -.
DR ProteomicsDB; 232425; -.
DR EnsemblPlants; AT3G62980.1; AT3G62980.1; AT3G62980.
DR GeneID; 825473; -.
DR Gramene; AT3G62980.1; AT3G62980.1; AT3G62980.
DR KEGG; ath:AT3G62980; -.
DR Araport; AT3G62980; -.
DR TAIR; locus:2099237; AT3G62980.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q570C0; -.
DR OMA; WIEAMAT; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q570C0; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q570C0; -.
DR PRO; PR:Q570C0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q570C0; baseline and differential.
DR Genevisible; Q570C0; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:TAIR.
DR GO; GO:0010011; F:auxin binding; IDA:UniProtKB.
DR GO; GO:0038198; F:auxin receptor activity; IDA:UniProtKB.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IC:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IGI:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0048443; P:stamen development; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR041101; Transp_inhibit.
DR Pfam; PF18511; F-box_5; 1.
DR Pfam; PF18791; Transp_inhibit; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 6.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Auxin signaling pathway; Cell cycle; Developmental protein;
KW Ethylene signaling pathway; Nucleus; Plant defense; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..594
FT /note="Protein TRANSPORT INHIBITOR RESPONSE 1"
FT /id="PRO_0000119965"
FT DOMAIN 3..50
FT /note="F-box"
FT REGION 81..82
FT /note="Interaction with auxin-responsive proteins"
FT REGION 347..352
FT /note="Interaction with auxin-responsive proteins"
FT REGION 405..409
FT /note="Interaction with auxin-responsive proteins"
FT REGION 464..465
FT /note="Interaction with auxin-responsive proteins"
FT BINDING 74
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0000269|PubMed:18391211"
FT BINDING 113..114
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 344
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0000269|PubMed:18391211"
FT BINDING 401..403
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 403
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0007744|PDB:2P1P, ECO:0007744|PDB:2P1Q"
FT BINDING 436
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0000269|PubMed:18391211"
FT BINDING 438..439
FT /ligand="(indol-3-yl)acetate"
FT /ligand_id="ChEBI:CHEBI:30854"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0007744|PDB:2P1P, ECO:0007744|PDB:2P1Q"
FT BINDING 484..485
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT BINDING 509
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000269|PubMed:17410169,
FT ECO:0000269|PubMed:18391211"
FT SITE 139
FT /note="Interaction with auxin-responsive proteins"
FT SITE 165
FT /note="Interaction with auxin-responsive proteins"
FT SITE 380
FT /note="Interaction with auxin-responsive proteins"
FT SITE 489
FT /note="Interaction with auxin-responsive proteins"
FT MUTAGEN 10
FT /note="P->A: Abolishes SCF(TIR1) complex formation, altered
FT auxin-mediated response and reduced affinity for auxin."
FT /evidence="ECO:0000269|PubMed:10398681,
FT ECO:0000269|PubMed:15917798"
FT MUTAGEN 33
FT /note="V->A: No affinity for auxin."
FT /evidence="ECO:0000269|PubMed:15917798"
FT MUTAGEN 35
FT /note="K->A: No affinity for auxin."
FT /evidence="ECO:0000269|PubMed:15917798"
FT MUTAGEN 147
FT /note="G->D: In tir1-1; insensitive to auxin ubiquitously
FT and to ethylene in roots only."
FT /evidence="ECO:0000269|PubMed:9436980"
FT MUTAGEN 441
FT /note="G->D: In tir1-2; insensitive to auxin."
FT /evidence="ECO:0000269|PubMed:9436980"
FT MUTAGEN 574..594
FT /note="Missing: In tir1-101/wei1; insensitive to auxin
FT ubiquitously and to ethylene in roots only."
FT /evidence="ECO:0000269|PubMed:12606727"
FT CONFLICT 490
FT /note="D -> E (in Ref. 6; BAD94031)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="D -> G (in Ref. 6; BAD94031)"
FT /evidence="ECO:0000305"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2P1N"
FT HELIX 58..64
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 145..154
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 173..178
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3C6N"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:2P1M"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 421..430
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 445..454
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 495..500
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 502..507
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 508..516
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 520..529
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:2P1M"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 554..560
FT /evidence="ECO:0007829|PDB:2P1M"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:2P1M"
SQ SEQUENCE 594 AA; 66799 MW; 9E19ED5DABF40D07 CRC64;
MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI GNCYAVSPAT
VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM SSSYTWLEEI RLKRMVVTDD
CLELIAKSFK NFKVLVLSSC EGFSTDGLAA IAATCRNLKE LDLRESDVDD VSGHWLSHFP
DTYTSLVSLN ISCLASEVSF SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL
GTGGYTAEVR PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT
VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP FVMEPNVALT
EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT RFRLCIIEPK APDYLTLEPL
DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC
DSLRKLEIRD CPFGDKALLA NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE
RGAPDSRPES CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL
