MAX2_ARATH
ID MAX2_ARATH Reviewed; 693 AA.
AC Q9SIM9; Q947K3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=F-box protein MAX2 {ECO:0000303|PubMed:11874909};
DE AltName: Full=F-box/LRR-repeat protein 7 {ECO:0000303|PubMed:11077244};
DE AltName: Full=Protein KARRIKIN INSENSITIVE 1 {ECO:0000305};
DE AltName: Full=Protein MORE AXILLARY BRANCHING 2 {ECO:0000303|PubMed:11874909};
DE AltName: Full=Protein ORESARA 9 {ECO:0000303|PubMed:11487692};
GN Name=MAX2 {ECO:0000303|PubMed:11874909};
GN Synonyms=FBL7 {ECO:0000303|PubMed:11077244}, KAI1 {ECO:0000305},
GN ORE9 {ECO:0000303|PubMed:11487692};
GN OrderedLocusNames=At2g42620 {ECO:0000312|Araport:AT2G42620};
GN ORFNames=F14N22.11 {ECO:0000312|EMBL:AAD22992.2};
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, DOMAIN F-BOX, LEUCINE-RICH REPEATS,
RP AND INTERACTION WITH SKP1A/ASK1.
RX PubMed=11487692; DOI=10.2307/3871318;
RA Woo H.R., Chung K.M., Park J.-H., Oh S.A., Ahn T., Hong S.H., Jang S.K.,
RA Nam H.G.;
RT "ORE9, an F-box protein that regulates leaf senescence in Arabidopsis.";
RL Plant Cell 13:1779-1790(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION.
RX PubMed=9351240; DOI=10.1111/j.0960-7412.1997.00527.x;
RA Oh S.A., Park J.-H., Lee G.I., Paek K.H., Park S.K., Nam H.G.;
RT "Identification of three genetic loci controlling leaf senescence in
RT Arabidopsis thaliana.";
RL Plant J. 12:527-535(1997).
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 FUNCTION.
RX PubMed=11874909; DOI=10.1242/dev.129.5.1131;
RA Stirnberg P., van de Sande K., Leyser H.M.O.;
RT "MAX1 and MAX2 control shoot lateral branching in Arabidopsis.";
RL Development 129:1131-1141(2002).
RN [7]
RP FUNCTION.
RX PubMed=15737939; DOI=10.1016/j.devcel.2005.01.009;
RA Booker J., Sieberer T., Wright W., Williamson L., Willett B., Stirnberg P.,
RA Turnbull C., Srinivasan M., Goddard P., Leyser O.;
RT "MAX1 encodes a cytochrome P450 family member that acts downstream of
RT MAX3/4 to produce a carotenoid-derived branch-inhibiting hormone.";
RL Dev. Cell 8:443-449(2005).
RN [8]
RP FUNCTION.
RX PubMed=16546078; DOI=10.1016/j.cub.2006.01.058;
RA Bennett T., Sieberer T., Willett B., Booker J., Luschnig C., Leyser O.;
RT "The Arabidopsis MAX pathway controls shoot branching by regulating auxin
RT transport.";
RL Curr. Biol. 16:553-563(2006).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DOMAIN F-BOX, AND
RP INTERACTION WITH SKP1A/ASK1 AND CUL1.
RX PubMed=17346265; DOI=10.1111/j.1365-313x.2007.03032.x;
RA Stirnberg P., Furner I.J., Ottoline Leyser H.M.;
RT "MAX2 participates in an SCF complex which acts locally at the node to
RT suppress shoot branching.";
RL Plant J. 50:80-94(2007).
RN [10]
RP FUNCTION.
RX PubMed=22357928; DOI=10.1242/dev.074567;
RA Waters M.T., Nelson D.C., Scaffidi A., Flematti G.R., Sun Y.K., Dixon K.W.,
RA Smith S.M.;
RT "Specialisation within the DWARF14 protein family confers distinct
RT responses to karrikins and strigolactones in Arabidopsis.";
RL Development 139:1285-1295(2012).
RN [11]
RP REVIEW.
RX PubMed=25179782; DOI=10.1016/j.pbi.2014.08.001;
RA Bennett T., Leyser O.;
RT "Strigolactone signalling: standing on the shoulders of DWARFs.";
RL Curr. Opin. Plant Biol. 22:7-13(2014).
RN [12]
RP INTERACTION WITH SMXL6; SMXL7 AND SMXL8.
RX PubMed=26546446; DOI=10.1105/tpc.15.00605;
RA Wang L., Wang B., Jiang L., Liu X., Li X., Lu Z., Meng X., Wang Y.,
RA Smith S.M., Li J.;
RT "Strigolactone signaling in Arabidopsis regulates shoot development by
RT targeting D53-like SMXL repressor proteins for ubiquitination and
RT degradation.";
RL Plant Cell 27:3128-3142(2015).
RN [13]
RP FUNCTION, AND INDUCTION BY EIN3.
RX PubMed=26507893; DOI=10.1093/jxb/erv438;
RA Zhang Y., Liu J., Chai J., Xing D.;
RT "Mitogen-activated protein kinase 6 mediates nuclear translocation of ORE3
RT to promote ORE9 gene expression in methyl jasmonate-induced leaf
RT senescence.";
RL J. Exp. Bot. 67:83-94(2016).
RN [14]
RP SUBUNIT, AND INTERACTION WITH D14.
RX PubMed=27479325; DOI=10.1038/nature19073;
RA Yao R., Ming Z., Yan L., Li S., Wang F., Ma S., Yu C., Yang M., Chen L.,
RA Chen L., Li Y., Yan C., Miao D., Sun Z., Yan J., Sun Y., Wang L., Chu J.,
RA Fan S., He W., Deng H., Nan F., Li J., Rao Z., Lou Z., Xie D.;
RT "DWARF14 is a non-canonical hormone receptor for strigolactone.";
RL Nature 536:469-473(2016).
CC -!- FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase
CC complexes, which may mediate the ubiquitination and subsequent
CC proteasomal degradation of target proteins. Promotes the senescence. Is
CC necessary for responses to strigolactones and karrikins. Contributes to
CC the selective repression of axillary shoots and moderates the branching
CC by regulating negatively the auxin transport in primary stems, in an
CC AXR1-independent manner (PubMed:11487692, PubMed:11874909,
CC PubMed:15737939, PubMed:16546078, PubMed:22357928, PubMed:9351240).
CC Required for the progression of leaf senescence mediated by methyl
CC jasmonate (PubMed:26507893). Required at each node to suppress axillary
CC bud growth (PubMed:17346265). {ECO:0000269|PubMed:11487692,
CC ECO:0000269|PubMed:11874909, ECO:0000269|PubMed:15737939,
CC ECO:0000269|PubMed:16546078, ECO:0000269|PubMed:17346265,
CC ECO:0000269|PubMed:22357928, ECO:0000269|PubMed:26507893,
CC ECO:0000269|PubMed:9351240}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex
CC (PubMed:11487692, PubMed:17346265). Interacts with SKP1A/ASK1
CC (PubMed:11487692, PubMed:17346265). Interacts with CUL1
CC (PubMed:17346265). Interacts with SMXL6, SMXL7 and SMXL8
CC (PubMed:26546446). Interacts with D14. Forms a complex with D14 and
CC SKP1A/ASK1 in presence of strigolactone (PubMed:27479325).
CC {ECO:0000269|PubMed:11487692, ECO:0000269|PubMed:17346265,
CC ECO:0000269|PubMed:26546446, ECO:0000269|PubMed:27479325}.
CC -!- INTERACTION:
CC Q9SIM9; Q9LNT9: ASK4; NbExp=3; IntAct=EBI-25529872, EBI-604085;
CC Q9SIM9; Q8GY60: At4g03415; NbExp=3; IntAct=EBI-25529872, EBI-25529942;
CC Q9SIM9; O82754: At4g23050; NbExp=3; IntAct=EBI-25529872, EBI-1238561;
CC Q9SIM9; A0A178V0W2: AXX17_At4g30790; NbExp=3; IntAct=EBI-25529872, EBI-25529973;
CC Q9SIM9; Q39255: SKP1A; NbExp=3; IntAct=EBI-25529872, EBI-532357;
CC Q9SIM9; Q9FHW7: SKP1B; NbExp=3; IntAct=EBI-25529872, EBI-604076;
CC Q9SIM9; Q9SP35: TIM17-2; NbExp=3; IntAct=EBI-25529872, EBI-25529919;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17346265}.
CC -!- TISSUE SPECIFICITY: Expressed in the vasculature of growing leaves and
CC roots, rosette axillary bud, flowers, siliques, funiculi and stems.
CC {ECO:0000269|PubMed:17346265}.
CC -!- INDUCTION: Up-regulated upon binding of EIN3 to the promoter during
CC methyl jasmonate-induced leaf senescence.
CC {ECO:0000269|PubMed:26507893}.
CC -!- DOMAIN: The F-box domain (1-55) is required for activity of the protein
CC and for the interaction with SKP1A/ASK1. {ECO:0000269|PubMed:11487692,
CC ECO:0000269|PubMed:17346265}.
CC -!- MISCELLANEOUS: 'Oresara' means 'long living' in Korean.
CC {ECO:0000305|PubMed:11487692}.
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DR EMBL; AF305597; AAK97303.1; -; mRNA.
DR EMBL; AC007087; AAD22992.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10149.1; -; Genomic_DNA.
DR PIR; B84856; B84856.
DR RefSeq; NP_565979.1; NM_129823.3.
DR AlphaFoldDB; Q9SIM9; -.
DR SMR; Q9SIM9; -.
DR BioGRID; 4199; 14.
DR IntAct; Q9SIM9; 7.
DR STRING; 3702.AT2G42620.1; -.
DR PaxDb; Q9SIM9; -.
DR PRIDE; Q9SIM9; -.
DR ProteomicsDB; 238886; -.
DR EnsemblPlants; AT2G42620.1; AT2G42620.1; AT2G42620.
DR GeneID; 818862; -.
DR Gramene; AT2G42620.1; AT2G42620.1; AT2G42620.
DR KEGG; ath:AT2G42620; -.
DR Araport; AT2G42620; -.
DR TAIR; locus:2041499; AT2G42620.
DR eggNOG; ENOG502QS13; Eukaryota.
DR HOGENOM; CLU_024476_0_0_1; -.
DR InParanoid; Q9SIM9; -.
DR OMA; WGHSLLS; -.
DR OrthoDB; 579663at2759; -.
DR PhylomeDB; Q9SIM9; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SIM9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIM9; baseline and differential.
DR Genevisible; Q9SIM9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0061137; P:bud dilation; IEA:EnsemblPlants.
DR GO; GO:0042335; P:cuticle development; IMP:TAIR.
DR GO; GO:0010187; P:negative regulation of seed germination; IMP:TAIR.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; TAS:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:1900618; P:regulation of shoot system morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0009416; P:response to light stimulus; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IGI:TAIR.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0010016; P:shoot system morphogenesis; IMP:TAIR.
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 Pfam; PF18511; F-box_5; 1.
DR SMART; SM00367; LRR_CC; 3.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Developmental protein; Leucine-rich repeat;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..693
FT /note="F-box protein MAX2"
FT /id="PRO_0000272266"
FT DOMAIN 3..50
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 9..34
FT /note="LRR 1"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 49..74
FT /note="LRR 2"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 75..100
FT /note="LRR 3"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 110..135
FT /note="LRR 4"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 141..167
FT /note="LRR 5"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 168..196
FT /note="LRR 6"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 200..225
FT /note="LRR 7"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 232..257
FT /note="LRR 8"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 274..299
FT /note="LRR 9"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 302..327
FT /note="LRR 10"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 332..356
FT /note="LRR 11"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 357..382
FT /note="LRR 12"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 383..409
FT /note="LRR 13"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 410..436
FT /note="LRR 14"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 480..505
FT /note="LRR 15"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 508..532
FT /note="LRR 16"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 541..565
FT /note="LRR 17"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REPEAT 608..637
FT /note="LRR 18"
FT /evidence="ECO:0000269|PubMed:11487692"
FT REGION 445..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 77415 MW; F25B70B219F48CC6 CRC64;
MASTTLSDLP DVILSTISSL VSDSRARNSL SLVSHKFLAL ERSTRSHLTI RGNARDLSLV
PDCFRSISHL DLSFLSPWGH TLLASLPIDH QNLLALRLKF CFPFVESLNV YTRSPSSLEL
LLPQWPRIRH IKLLRWHQRA SQIPTGGDFV PIFEHCGGFL ESLDLSNFYH WTEDLPPVLL
RYADVAARLT RLDLLTASFT EGYKSSEIVS ITKSCPNLKT FRVACTFDPR YFEFVGDETL
SAVATSSPKL TLLHMVDTAS LANPRAIPGT EAGDSAVTAG TLIEVFSGLP NLEELVLDVG
KDVKHSGVAL EALNSKCKKL RVLKLGQFQG VCSATEWRRL DGVALCGGLQ SLSIKNSGDL
TDMGLVAIGR GCCKLTTFEI QGCENVTVDG LRTMVSLRSK TLTDVRISCC KNLDTAASLK
AIEPICDRIK RLHIDCVWSG SEDEEVEGRV ETSEADHEEE DDGYERSQKR CKYSFEEEHC
STSDVNGFCS EDRVWEKLEY LSLWINVGEF LTPLPMTGLD DCPNLEEIRI KIEGDCRGKR
RPAEPEFGLS CLALYPKLSK MQLDCGDTIG FALTAPPMQM DLSLWERFFL TGIGSLSLSE
LDYWPPQDRD VNQRSLSLPG AGLLQECLTL RKLFIHGTAH EHFMNFLLRI PNLRDVQLRA
DYYPAPENDM STEMRVGSCS RFEDQLNSRN IID
