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   27-MAR-2024, entry version 134.
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.Q9LPW7; -.
DR   PaxDb; 3702-AT1G12820-1; -.
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; AT1G12820; AFB3.
DR   eggNOG; KOG1947; Eukaryota.
DR   HOGENOM; CLU_022456_1_0_1; -.
DR   InParanoid; Q9LPW7; -.
DR   OMA; QGNHLIK; -.
DR   OrthoDB; 3060585at2759; -.
DR   PhylomeDB; Q9LPW7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9LPW7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPW7; baseline and differential.
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:0048443; P:stamen development; IGI:TAIR.
DR   CDD; cd22159; F-box_AtTIR1-like; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR041567; COI1_F-box.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR041101; Transp_inhibit.
DR   PANTHER; PTHR16134; F-BOX/TPR REPEAT PROTEIN POF3; 1.
DR   PANTHER; PTHR16134:SF152; PROTEIN AUXIN SIGNALING F-BOX 3; 1.
DR   Pfam; PF18511; F-box_5; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF18791; Transp_inhibit; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   Genevisible; Q9LPW7; AT.
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
//