MAX2_ORYSJ
ID MAX2_ORYSJ Reviewed; 720 AA.
AC Q5VMP0; A0A0P0WSH6; C7J3G5; Q5VMP1;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=F-box/LRR-repeat MAX2 homolog {ECO:0000305};
DE AltName: Full=F-box and leucine-rich repeat MAX2 homolog {ECO:0000305};
DE AltName: Full=Protein DWARF 3 {ECO:0000303|PubMed:15659436};
GN Name=D3 {ECO:0000303|PubMed:15659436};
GN OrderedLocusNames=Os06g0154200 {ECO:0000312|EMBL:BAS96220.1},
GN LOC_Os06g06050 {ECO:0000305};
GN ORFNames=OSJNBa0085L11.6-1 {ECO:0000312|EMBL:BAD69288.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=15659436; DOI=10.1093/pcp/pci022;
RA Ishikawa S., Maekawa M., Arite T., Onishi K., Takamure I., Kyozuka J.;
RT "Suppression of tiller bud activity in tillering dwarf mutants of rice.";
RL Plant Cell Physiol. 46:79-86(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=17655651; DOI=10.1111/j.1365-313x.2007.03210.x;
RA Arite T., Iwata H., Ohshima K., Maekawa M., Nakajima M., Kojima M.,
RA Sakakibara H., Kyozuka J.;
RT "DWARF10, an RMS1/MAX4/DAD1 ortholog, controls lateral bud outgrowth in
RT rice.";
RL Plant J. 51:1019-1029(2007).
RN [7]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Shiokari;
RX PubMed=18690207; DOI=10.1038/nature07272;
RA Umehara M., Hanada A., Yoshida S., Akiyama K., Arite T., Takeda-Kamiya N.,
RA Magome H., Kamiya Y., Shirasu K., Yoneyama K., Kyozuka J., Yamaguchi S.;
RT "Inhibition of shoot branching by new terpenoid plant hormones.";
RL Nature 455:195-200(2008).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Shiokari;
RX PubMed=23025475; DOI=10.1111/j.1469-8137.2012.04339.x;
RA Yoshida S., Kameoka H., Tempo M., Akiyama K., Umehara M., Yamaguchi S.,
RA Hayashi H., Kyozuka J., Shirasu K.;
RT "The D3 F-box protein is a key component in host strigolactone responses
RT essential for arbuscular mycorrhizal symbiosis.";
RL New Phytol. 196:1208-1216(2012).
RN [9]
RP MUTAGENESIS OF PRO-21 AND ARG-36, AND INTERACTION WITH D14.
RX PubMed=24336200; DOI=10.1038/nature12870;
RA Jiang L., Liu X., Xiong G., Liu H., Chen F., Wang L., Meng X., Liu G.,
RA Yu H., Yuan Y., Yi W., Zhao L., Ma H., He Y., Wu Z., Melcher K., Qian Q.,
RA Xu H.E., Wang Y., Li J.;
RT "DWARF 53 acts as a repressor of strigolactone signalling in rice.";
RL Nature 504:401-405(2013).
RN [10]
RP FUNCTION, AND INTERACTION WITH D14.
RX PubMed=24336215; DOI=10.1038/nature12878;
RA Zhou F., Lin Q., Zhu L., Ren Y., Zhou K., Shabek N., Wu F., Mao H.,
RA Dong W., Gan L., Ma W., Gao H., Chen J., Yang C., Wang D., Tan J.,
RA Zhang X., Guo X., Wang J., Jiang L., Liu X., Chen W., Chu J., Yan C.,
RA Ueno K., Ito S., Asami T., Cheng Z., Wang J., Lei C., Zhai H., Wu C.,
RA Wang H., Zheng N., Wan J.;
RT "D14-SCF(D3)-dependent degradation of D53 regulates strigolactone
RT signalling.";
RL Nature 504:406-410(2013).
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 FUNCTION, INTERACTION WITH D14; SKP1; SKP5; SKP20 AND CUL1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24616269; DOI=10.1093/pcp/pcu045;
RA Zhao J., Wang T., Wang M., Liu Y., Yuan S., Gao Y., Yin L., Sun W.,
RA Peng L., Zhang W., Wan J., Li X.;
RT "DWARF3 participates in an SCF complex and associates with DWARF14 to
RT suppress rice shoot branching.";
RL Plant Cell Physiol. 55:1096-1109(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS).
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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 1-476 AND 516-720.
RX PubMed=30464344; DOI=10.1038/s41586-018-0743-5;
RA Shabek N., Ticchiarelli F., Mao H., Hinds T.R., Leyser O., Zheng N.;
RT "Structural plasticity of D3-D14 ubiquitin ligase in strigolactone
RT signalling.";
RL Nature 563:652-656(2018).
CC -!- FUNCTION: Involved in strigolactone (SL) signaling (PubMed:23025475,
CC PubMed:24336215, PubMed:24616269). Required for responses to SLs and
CC the establishment of arbuscular mycorrhiza symbiosis in rice
CC (PubMed:23025475). Strigolactone-dependent association of D3 with D14
CC and D53 (a repressor of SL signaling) triggers D53 ubiquitination and
CC degradation (PubMed:24616269). Controls tillering by suppressing
CC axillary bud activity (PubMed:15659436). Tiller is a specialized grain-
CC bearing branch that is formed on the unelongated basal internode and
CC grows independently of the mother stem (culm) by means of its own
CC adventitious roots (PubMed:15659436). {ECO:0000269|PubMed:15659436,
CC ECO:0000269|PubMed:23025475, ECO:0000269|PubMed:24336215,
CC ECO:0000269|PubMed:24616269}.
CC -!- SUBUNIT: Associates to a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-
CC protein ligase complex (Probable). Interacts with D14 in a
CC strigolactone-dependent manner (PubMed:24336200, PubMed:24336215,
CC PubMed:24616269). Interacts with SKP1, SKP5 and SKP20
CC (PubMed:24616269). {ECO:0000269|PubMed:24336200,
CC ECO:0000269|PubMed:24336215, ECO:0000269|PubMed:24616269,
CC ECO:0000305|PubMed:24616269}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24616269}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (PubMed:15659436). Expressed in
CC roots, culms, leaf blades, leaf sheaths, shoot bases and panicles
CC (PubMed:24616269). {ECO:0000269|PubMed:15659436,
CC ECO:0000269|PubMed:24616269}.
CC -!- DISRUPTION PHENOTYPE: Increased number of tillers and reduced plant
CC height. {ECO:0000269|PubMed:15659436, ECO:0000269|PubMed:17655651,
CC ECO:0000269|PubMed:18690207, ECO:0000269|PubMed:24616269}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD69289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP006533; BAD69288.1; -; Genomic_DNA.
DR EMBL; AP006533; BAD69289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008212; BAH93336.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS96220.1; -; Genomic_DNA.
DR EMBL; AK065478; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015643693.1; XM_015788207.1.
DR RefSeq; XP_015643694.1; XM_015788208.1.
DR PDB; 5HYW; X-ray; 3.01 A; A/C=1-720.
DR PDB; 5HZG; X-ray; 3.30 A; B/F=1-720.
DR PDB; 6BRO; X-ray; 2.50 A; B/D=1-720.
DR PDB; 6BRP; X-ray; 2.39 A; B/D=1-476, B/D=516-720.
DR PDB; 6BRQ; X-ray; 2.99 A; B/D=1-476, B/D=516-720.
DR PDBsum; 5HYW; -.
DR PDBsum; 5HZG; -.
DR PDBsum; 6BRO; -.
DR PDBsum; 6BRP; -.
DR PDBsum; 6BRQ; -.
DR AlphaFoldDB; Q5VMP0; -.
DR SMR; Q5VMP0; -.
DR STRING; 4530.OS06T0154200-01; -.
DR PaxDb; Q5VMP0; -.
DR PRIDE; Q5VMP0; -.
DR EnsemblPlants; Os06t0154200-01; Os06t0154200-01; Os06g0154200.
DR Gramene; Os06t0154200-01; Os06t0154200-01; Os06g0154200.
DR KEGG; osa:9272469; -.
DR eggNOG; ENOG502QS13; Eukaryota.
DR InParanoid; Q5VMP0; -.
DR OMA; WGHSLLS; -.
DR OrthoDB; 579663at2759; -.
DR PlantReactome; R-OSA-5654828; Strigolactone signaling.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR ExpressionAtlas; Q5VMP0; baseline and differential.
DR Genevisible; Q5VMP0; OS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0009926; P:auxin polar transport; IEA:EnsemblPlants.
DR GO; GO:0061137; P:bud dilation; IMP:Gramene.
DR GO; GO:0042335; P:cuticle development; IEA:EnsemblPlants.
DR GO; GO:0010187; P:negative regulation of seed germination; IEA:EnsemblPlants.
DR GO; GO:1902584; P:positive regulation of response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0009934; P:regulation of meristem structural organization; IEA:EnsemblPlants.
DR GO; GO:1900618; P:regulation of shoot system morphogenesis; IMP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEA:EnsemblPlants.
DR GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0010016; P:shoot system morphogenesis; IEA:EnsemblPlants.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR SMART; SM00367; LRR_CC; 4.
DR SUPFAM; SSF81383; SSF81383; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Leucine-rich repeat; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..720
FT /note="F-box/LRR-repeat MAX2 homolog"
FT /id="PRO_0000119967"
FT DOMAIN 14..60
FT /note="F-box"
FT REPEAT 71..134
FT /note="LRR 1"
FT REPEAT 135..158
FT /note="LRR 2"
FT REPEAT 159..189
FT /note="LRR 3"
FT REPEAT 190..218
FT /note="LRR 4"
FT REPEAT 219..247
FT /note="LRR 5"
FT REPEAT 248..279
FT /note="LRR 6"
FT REPEAT 280..316
FT /note="LRR 7"
FT REPEAT 317..344
FT /note="LRR 8"
FT REPEAT 345..372
FT /note="LRR 9"
FT REPEAT 373..398
FT /note="LRR 10"
FT REPEAT 399..435
FT /note="LRR 11"
FT REPEAT 436..452
FT /note="LRR 12"
FT REPEAT 453..510
FT /note="LRR 13"
FT REPEAT 511..537
FT /note="LRR 14"
FT REPEAT 538..571
FT /note="LRR 15"
FT REPEAT 572..606
FT /note="LRR 16"
FT REPEAT 607..644
FT /note="LRR 17"
FT REPEAT 645..720
FT /note="LRR 18"
FT MUTAGEN 21
FT /note="P->S: In d3; dwarf and high tillering phenotypes;
FT when associated with W-36."
FT /evidence="ECO:0000269|PubMed:24336200"
FT MUTAGEN 36
FT /note="R->W: In d3; dwarf and high tillering phenotypes;
FT when associated with S-21."
FT /evidence="ECO:0000269|PubMed:24336200"
FT CONFLICT 521
FT /note="M -> I (in Ref. 4; AK065478)"
FT /evidence="ECO:0000305"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 46..55
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:6BRP"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:6BRP"
FT TURN 187..191
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 278..287
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 330..339
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:6BRP"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 450..456
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:6BRP"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 585..592
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 644..650
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 657..664
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:6BRP"
FT HELIX 670..673
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:5HZG"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:6BRP"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:5HZG"
FT HELIX 706..715
FT /evidence="ECO:0007829|PDB:6BRP"
SQ SEQUENCE 720 AA; 79223 MW; 500F685E247A54B2 CRC64;
MAEEEEVEEG RSSSSAILDL PEPLLLHILS FLTDVRSRHR AALACGRMRA AERATRSELS
LRGDPRSPGF LFLSHAFRFP ALEHLDLSLV SPWGHPLLSS VPPCGGGGGG APSASSSSGM
NVYHPEAISE QNAFIAARLA GCFPAVTSLA VYCRDPTTLA NLTPHWQASL RRVKLVRWHQ
RPPTLPDGAD LEPLLETCAA LRELDLSEFY CWTEDVVRAL TTHPSATAAL THLDLGLAAA
TDGFKSSELG PIAASCPNLR KLVAPCLFNP RFSDCVGDDA LLSLATSCPR LTVLRLSEPF
EAAANIQREE AAITVAGLVA FFAALPALED FTMDLQHNVL EAAPAMEALA RRCPRIKFLT
LGSFQGLCKA SWLHLDGVAV CGGLESLYMK NCQDLTDASL AAIGRGCRRL AKFGIHGCDL
VTSAGIRRLA FTLRPTLKEV TVLHCRLLHT AECLTALSPI RDRIESLEIN CVWNTTEQPC
SVANGTTTEC DPEDDELGEV YESAAKKCRY MEFDDLGSWE MLRSLSLWFS AGQLLSPLIS
AGLDSCPVLE EISIKVEGDC RTCPRPAPRT IFGLSDLAGF PVLAKMKLDL SEAVGYALTA
PTGQMDLSLW ERFYLHGIES LQTLYELDYW PPQDKDVHHR SLTLPAVGLI QRCVGLRKLF
IHGTTHEHFM TFFLSIPNLR DMQLREDYYP APENDLMFTE MRAESWLRFE VQLNSRQIDD
