FBX14_ARATH
ID FBX14_ARATH Reviewed; 623 AA.
AC Q8RWQ8; B9DFR4; Q9STV5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=F-box protein FBX14;
DE AltName: Full=Transport inhibitor response 1-like protein;
DE Short=TIR1-like protein;
GN Name=FBX14; OrderedLocusNames=At4g24390; ORFNames=T22A6.220;
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=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 [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;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
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 [6]
RP LEUCINE-RICH REPEATS.
RX PubMed=12008900; DOI=10.1023/a:1014440531842;
RA Thelander M., Fredriksson D., Schouten J., Hoge J.H.C., Ronne H.;
RT "Cloning by pathway activation in yeast: identification of an Arabidopsis
RT thaliana F-box protein that can turn on glucose repression.";
RL Plant Mol. Biol. 49:69-79(2002).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex. May
CC interact with auxin and auxin-responsive proteins (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q8RWQ8; Q94BX2: At3g50910; NbExp=3; IntAct=EBI-1235922, EBI-4424796;
CC Q8RWQ8; Q39255: SKP1A; NbExp=3; IntAct=EBI-1235922, EBI-532357;
CC Q8RWQ8; Q93Z00: TCP14; NbExp=3; IntAct=EBI-1235922, EBI-4424563;
CC Q8RWQ8; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1235922, EBI-4426144;
CC Q8RWQ8; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-1235922, EBI-15192297;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The F-box is necessary for the interaction with SKP1.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a structural
CC cofactor. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45074.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB79349.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL078637; CAB45074.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL161561; CAB79349.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002687; AEE84897.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84898.1; -; Genomic_DNA.
DR EMBL; AY091772; AAM10320.1; -; mRNA.
DR EMBL; BT006340; AAP21148.1; -; mRNA.
DR EMBL; AK316873; BAH19581.1; -; mRNA.
DR PIR; T09902; T09902.
DR RefSeq; NP_567702.2; NM_118572.3.
DR RefSeq; NP_974607.1; NM_202878.2.
DR AlphaFoldDB; Q8RWQ8; -.
DR SMR; Q8RWQ8; -.
DR BioGRID; 13830; 12.
DR IntAct; Q8RWQ8; 14.
DR STRING; 3702.AT4G24390.1; -.
DR PaxDb; Q8RWQ8; -.
DR PRIDE; Q8RWQ8; -.
DR ProteomicsDB; 230506; -.
DR EnsemblPlants; AT4G24390.1; AT4G24390.1; AT4G24390.
DR EnsemblPlants; AT4G24390.2; AT4G24390.2; AT4G24390.
DR GeneID; 828541; -.
DR Gramene; AT4G24390.1; AT4G24390.1; AT4G24390.
DR Gramene; AT4G24390.2; AT4G24390.2; AT4G24390.
DR KEGG; ath:AT4G24390; -.
DR Araport; AT4G24390; -.
DR TAIR; locus:2135942; AT4G24390.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_022456_1_0_1; -.
DR InParanoid; Q8RWQ8; -.
DR OMA; FVWLSSC; -.
DR OrthoDB; 1282076at2759; -.
DR PhylomeDB; Q8RWQ8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8RWQ8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RWQ8; baseline and differential.
DR Genevisible; Q8RWQ8; 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; ISS:UniProtKB.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; ISS:UniProtKB.
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 Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR041567; COI1_F-box.
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; SM00367; LRR_CC; 4.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..623
FT /note="F-box protein FBX14"
FT /id="PRO_0000273545"
FT DOMAIN 54..97
FT /note="F-box"
FT REGION 18..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..127
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 394..399
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 451..455
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT REGION 510..511
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 20..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 447..449
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 482
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 530..531
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 426
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
FT SITE 535
FT /note="Interaction with auxin-responsive proteins"
FT /evidence="ECO:0000250"
SQ SEQUENCE 623 AA; 69500 MW; 7007CD8F4F5B2C9C CRC64;
MTEEDSSAKM SEDVEKYLNL NPPCSSSSSS SSAATFTNKS RNFKSSPPPC PDHVLENVLE
NVLQFLTSRC DRNAVSLVCR SWYRVEAQTR LEVFIGNCYS LSPARLIHRF KRVRSLVLKG
KPRFADFNLM PPNWGAQFSP WVAATAKAYP WLEKVHLKRM FVTDDDLALL AESFPGFKEL
TLVCCEGFGT SGIAIVANKC RQLKVLDLME SEVTDDELDW ISCFPEGETH LESLSFDCVE
SPINFKALEE LVVRSPFLKK LRTNRFVSLE ELHRLMVRAP QLTSLGTGSF SPDNVPQGEQ
QPDYAAAFRA CKSIVCLSGF REFRPEYLLA ISSVCANLTS LNFSYANISP HMLKPIISNC
HNIRVFWALD SIRDEGLQAV AATCKELREL RIFPFDPRED SEGPVSGVGL QAISEGCRKL
ESILYFCQNM TNGAVTAMSE NCPQLTVFRL CIMGRHRPDH VTGKPMDDGF GAIVKNCKKL
TRLAVSGLLT DEAFSYIGEY GKLIRTLSVA FAGNSDKALR YVLEGCPKLQ KLEIRDSPFG
DVGLRSGMHR YSNMRFVWLS SCLISRGGCR GVSHALPNVV VEVFGADGDD DEDTVTGDYV
ETLYLYRSLD GPRKDAPKFV TIL
