AFB3_ARATH
ID AFB3_ARATH Reviewed; 577 AA.
AC Q9LPW7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein AUXIN SIGNALING F-BOX 3;
GN Name=AFB3; OrderedLocusNames=At1g12820; ORFNames=F13K23.7;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [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 FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CUL1; IAA7; IAA12 AND 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 [6]
RP FUNCTION.
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 [7]
RP 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).
CC -!- FUNCTION: Confers sensitivity to the virulent bacterial pathogen
CC P.syringae (By similarity). Component of SCF(ASK-cullin-F-box) E3
CC ubiquitin ligase complexes, which may mediate the ubiquitination and
CC subsequent proteasomal degradation of target proteins. Auxin receptor
CC that mediates Aux/IAA proteins proteasomal degradation and auxin-
CC regulated transcription. Involved in embryogenesis regulation by auxin.
CC {ECO:0000250, ECO:0000269|PubMed:15917797,
CC ECO:0000269|PubMed:15992545}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC Interacts with CUL1 and SKP1A/ASK1. Interacts with Aux/IAA proteins
CC (IAA7 and IAA12) in an auxin-dependent manner.
CC {ECO:0000269|PubMed:15992545}.
CC -!- INTERACTION:
CC Q9LPW7; Q93Z00: TCP14; NbExp=3; IntAct=EBI-617501, EBI-4424563;
CC Q9LPW7; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-617501, EBI-4426144;
CC Q9LPW7; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-617501, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in flowers.
CC {ECO:0000269|PubMed:15992545}.
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:0000250}.
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DR EMBL; AC012187; AAF78487.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28934.1; -; Genomic_DNA.
DR EMBL; AY099541; AAM20393.1; -; mRNA.
DR EMBL; BT002118; AAN72129.1; -; mRNA.
DR EMBL; AK227280; BAE99304.1; -; mRNA.
DR PIR; F86261; F86261.
DR RefSeq; NP_563915.1; NM_101152.5.
DR AlphaFoldDB; Q9LPW7; -.
DR SMR; Q9LPW7; -.
DR BioGRID; 23078; 5.
DR IntAct; Q9LPW7; 8.
DR STRING; 3702.AT1G12820.1; -.
DR PaxDb; Q9LPW7; -.
DR PRIDE; Q9LPW7; -.
DR ProteomicsDB; 244882; -.
DR EnsemblPlants; AT1G12820.1; AT1G12820.1; AT1G12820.
DR GeneID; 837838; -.
DR Gramene; AT1G12820.1; AT1G12820.1; AT1G12820.
DR KEGG; ath:AT1G12820; -.
DR Araport; AT1G12820; -.
DR TAIR; locus:2010366; AT1G12820.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q9LPW7; -.
DR OMA; LEVAPRC; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q9LPW7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9LPW7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPW7; baseline and differential.
DR Genevisible; Q9LPW7; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0010011; F:auxin binding; IGI:TAIR.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0071249; P:cellular response to nitrate; IEP:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0010152; P:pollen maturation; IGI:TAIR.
DR GO; GO:0080022; P:primary root development; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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; IPR001810; F-box_dom.
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.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Developmental protein; Nucleus; Plant defense;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..577
FT /note="Protein AUXIN SIGNALING F-BOX 3"
FT /id="PRO_0000272244"
FT DOMAIN 1..45
FT /note="F-box"
FT REGION 76..77
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 343..348
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 402..406
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 461..462
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 108..109
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 398..400
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 481..482
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT SITE 134
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 160
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 377
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 486
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 64906 MW; 8E419B4D83068661 CRC64;
MNYFPDEVIE HVFDFVASHK DRNSISLVCK SWHKIERFSR KEVFIGNCYA INPERLIRRF
PCLKSLTLKG KPHFADFNLV PHEWGGFVHP WIEALARSRV GLEELRLKRM VVTDESLDLL
SRSFANFKSL VLVSCEGFTT DGLASIAANC RHLRELDLQE NEIDDHRGQW LNCFPDSCTT
LMSLNFACLK GETNVAALER LVARSPNLKS LKLNRAVPLD ALARLMSCAP QLVDLGVGSY
ENEPDPESFA KLMTAIKKYT SLRSLSGFLE VAPLCLPAFY PICQNLISLN LSYAAEIQGN
HLIKLIQLCK RLQRLWILDS IGDKGLAVVA ATCKELQELR VFPSDVHGEE DNNASVTEVG
LVAISAGCPK LHSILYFCKQ MTNAALIAVA KNCPNFIRFR LCILEPHKPD HITFQSLDEG
FGAIVQACKG LRRLSVSGLL TDQVFLYIGM YAEQLEMLSI AFAGDTDKGM LYVLNGCKKM
RKLEIRDSPF GNAALLADVG RYETMRSLWM SSCEVTLGGC KRLAQNSPRL NVEIINENEN
NGMEQNEEDE REKVDKLYLY RTVVGTRKDA PPYVRIL
