SMXL6_ARATH
ID SMXL6_ARATH Reviewed; 979 AA.
AC Q9LML2;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein SMAX1-LIKE 6 {ECO:0000303|PubMed:23893171};
DE Short=AtSMXL6 {ECO:0000303|PubMed:23893171};
DE AltName: Full=Protein D53-like 2 {ECO:0000303|PubMed:24336200};
DE Short=AtD53-like 2 {ECO:0000303|PubMed:24336200};
DE AltName: Full=Protein D53-like SMXL 6 {ECO:0000303|PubMed:26546446};
GN Name=SMXL6 {ECO:0000303|PubMed:23893171};
GN OrderedLocusNames=At1g07200 {ECO:0000312|Araport:AT1G07200};
GN ORFNames=F10K1.9 {ECO:0000312|EMBL:AAF82200.1};
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 INTERACTION WITH TPR3.
RX PubMed=22065421; DOI=10.1104/pp.111.186999;
RA Causier B., Ashworth M., Guo W., Davies B.;
RT "The TOPLESS interactome: a framework for gene repression in Arabidopsis.";
RL Plant Physiol. 158:423-438(2012).
RN [4]
RP IDENTIFICATION.
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 [5]
RP INDUCTION BY STRIGOLACTONE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23893171; DOI=10.1104/pp.113.221259;
RA Stanga J.P., Smith S.M., Briggs W.R., Nelson D.C.;
RT "SUPPRESSOR OF MORE AXILLARY GROWTH2 1 controls seed germination and
RT seedling development in Arabidopsis.";
RL Plant Physiol. 163:318-330(2013).
RN [6]
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 [7]
RP FUNCTION, MUTAGENESIS OF 706-ARG--THR-709 AND 833-LEU--PRO-838,
RP UBIQUITINATION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAX2; TPR2 AND
RP D14.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26546447; DOI=10.1105/tpc.15.00562;
RA Soundappan I., Bennett T., Morffy N., Liang Y., Stanga J.P., Abbas A.,
RA Leyser O., Nelson D.C.;
RT "SMAX1-LIKE/D53 family members enable distinct MAX2-dependent responses to
RT strigolactones and karrikins in Arabidopsis.";
RL Plant Cell 27:3143-3159(2015).
RN [9]
RP INTERACTION WITH D14.
RX PubMed=25713176; DOI=10.1093/pcp/pcv028;
RA Umehara M., Cao M., Akiyama K., Akatsu T., Seto Y., Hanada A., Li W.,
RA Takeda-Kamiya N., Morimoto Y., Yamaguchi S.;
RT "Structural requirements of strigolactones for shoot branching inhibition
RT in rice and Arabidopsis.";
RL Plant Cell Physiol. 56:1059-1072(2015).
CC -!- FUNCTION: Probable component of a transcriptional corepressor complex
CC involved in branching control. Regulates cotyledon expansion and
CC lateral root growth, but not germination or hypocotyl elongation.
CC Promotes auxin transport and PIN1 accumulation in the stem and
CC represses BRC1/TCP18 expression in axillary buds (PubMed:26546447,
CC PubMed:26546446). {ECO:0000269|PubMed:26546446,
CC ECO:0000269|PubMed:26546447}.
CC -!- SUBUNIT: Interacts with TPL/TPR in an EAR-motif dependent manner
CC (PubMed:22065421). Interacts with TPR3 (PubMed:22065421). Interacts
CC with MAX2 and TPR2 (PubMed:26546446). Interacts with D14
CC (PubMed:26546446, PubMed:25713176). The interaction with D14 occurs in
CC the presence of (2'R) stereoisomers of strigolactones, but not (2'S)
CC stereoisomers (PubMed:25713176). {ECO:0000269|PubMed:22065421,
CC ECO:0000269|PubMed:25713176, ECO:0000269|PubMed:26546446}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26546446}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9LML2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in roots, seedlings and axillary branches
CC (PubMed:23893171). Expressed in the primary rosette buds and expanding
CC leaves of adult rosettes, the vasculature of the hypocotyls,
CC cotyledons, and mature roots, and in the midvein and petioles of young
CC leaves (PubMed:26546447). {ECO:0000269|PubMed:23893171,
CC ECO:0000269|PubMed:26546447}.
CC -!- INDUCTION: Up-regulated by strigolactone treatment.
CC {ECO:0000269|PubMed:23893171}.
CC -!- DOMAIN: Contains 1 EAR motif required for the interaction with TPR2.
CC {ECO:0000269|PubMed:26546446}.
CC -!- PTM: Ubiquitinated upon strigolactone treatment (PubMed:26546446).
CC Probable proteolytic target of SCF(MAX2)-mediated stigolactone
CC signaling (PubMed:26546447). {ECO:0000269|PubMed:26546446,
CC ECO:0000269|PubMed:26546447}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Suppresses max2 phenotypes
CC associated with strigolactone-D14-regulated growth. Smxl6 and max2
CC double mutants have branching and inflorescence heights similar to max2
CC mutants. {ECO:0000269|PubMed:26546447}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; AC067971; AAF82200.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28092.1; -; Genomic_DNA.
DR PIR; B86207; B86207.
DR RefSeq; NP_001077474.1; NM_001084005.3. [Q9LML2-1]
DR AlphaFoldDB; Q9LML2; -.
DR STRING; 3702.AT1G07200.2; -.
DR PaxDb; Q9LML2; -.
DR PRIDE; Q9LML2; -.
DR ProteomicsDB; 232624; -. [Q9LML2-1]
DR EnsemblPlants; AT1G07200.2; AT1G07200.2; AT1G07200. [Q9LML2-1]
DR GeneID; 837231; -.
DR Gramene; AT1G07200.2; AT1G07200.2; AT1G07200. [Q9LML2-1]
DR KEGG; ath:AT1G07200; -.
DR Araport; AT1G07200; -.
DR TAIR; locus:2007412; AT1G07200.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_006575_0_2_1; -.
DR InParanoid; Q9LML2; -.
DR OMA; NCANEAL; -.
DR OrthoDB; 182446at2759; -.
DR PhylomeDB; Q9LML2; -.
DR PRO; PR:Q9LML2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LML2; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:1902347; P:response to strigolactone; IMP:TAIR.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..979
FT /note="Protein SMAX1-LIKE 6"
FT /id="PRO_0000435715"
FT DOMAIN 8..190
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 12..86
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 100..190
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT MOTIF 833..837
FT /note="EAR"
FT /evidence="ECO:0000305|PubMed:26546446"
FT MUTAGEN 706..709
FT /note="Missing: In smxl6d; decreased ubiquitination and
FT increased resistance to degradation."
FT /evidence="ECO:0000269|PubMed:26546446"
FT MUTAGEN 833..838
FT /note="Missing: Loss of interaction with TPR2."
FT /evidence="ECO:0000269|PubMed:26546446"
SQ SEQUENCE 979 AA; 107806 MW; CD20E05FCDCD4EB5 CRC64;
MPTPVTTARE CLTEEAARAL DDAVVVARRR SHAQTTSLHA VSALLAMPSS ILREVCVSRA
ARSVPYSSRL QFRALELCVG VSLDRLPSSK SPATEEDPPV SNSLMAAIKR SQANQRRHPE
SYHLQQIHAS NNGGGGCQTT VLKVELKYFI LSILDDPIVN RVFGEAGFRS SEIKLDVLHP
PVTQLSSRFS RGRCPPLFLC NLPNSDPNRE FPFSGSSGFD ENSRRIGEVL GRKDKKNPLL
IGNCANEALK TFTDSINSGK LGFLQMDISG LSLISIEKEI SEILADGSKN EEEIRMKVDD
LGRTVEQSGS KSGIVLNLGE LKVLTSEANA ALEILVSKLS DLLKHESKQL SFIGCVSSNE
TYTKLIDRFP TIEKDWDLHV LPITASTKPS TQGVYPKSSL MGSFVPFGGF FSSTSNFRVP
LSSTVNQTLS RCHLCNEKYL QEVAAVLKAG SSLSLADKCS EKLAPWLRAI ETKEDKGITG
SSKALDDANT SASQTAALQK KWDNICQSIH HTPAFPKLGF QSVSPQFPVQ TEKSVRTPTS
YLETPKLLNP PISKPKPMED LTASVTNRTV SLPLSCVTTD FGLGVIYASK NQESKTTREK
PMLVTLNSSL EHTYQKDFKS LREILSRKVA WQTEAVNAIS QIICGCKTDS TRRNQASGIW
LALLGPDKVG KKKVAMTLSE VFFGGKVNYI CVDFGAEHCS LDDKFRGKTV VDYVTGELSR
KPHSVVLLEN VEKAEFPDQM RLSEAVSTGK IRDLHGRVIS MKNVIVVVTS GIAKDNATDH
VIKPVKFPEE QVLSARSWKL QIKLGDATKF GVNKRKYELE TAQRAVKVQR SYLDLNLPVN
ETEFSPDHEA EDRDAWFDEF IEKVDGKVTF KPVDFDELAK NIQEKIGSHF ERCFGSETHL
ELDKEVILQI LAASWSSLSS GEEEGRTIVD QWMQTVLARS FAEAKQKYGS NPMLGVKLVA
SSSGLASGVE LPAKVDVIW
