SMR1_ARATH
ID SMR1_ARATH Reviewed; 128 AA.
AC Q9LPP4; Q8GXB8; Q8LDA2;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Cyclin-dependent protein kinase inhibitor SMR1 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
DE AltName: Full=Protein LOSS OF GIANT CELLS FROM ORGANS;
DE AltName: Full=Protein SIAMESE-RELATED 1 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
GN Name=SMR1 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
GN Synonyms=LGO; OrderedLocusNames=At3g10525; ORFNames=F13M14.31, F18K10.10;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17098811; DOI=10.1105/tpc.106.044834;
RA Churchman M.L., Brown M.L., Kato N., Kirik V., Huelskamp M., Inze D.,
RA De Veylder L., Walker J.D., Zheng Z., Oppenheimer D.G., Gwin T.,
RA Churchman J., Larkin J.C.;
RT "SIAMESE, a plant-specific cell cycle regulator, controls endoreplication
RT onset in Arabidopsis thaliana.";
RL Plant Cell 18:3145-3157(2006).
RN [7]
RP INDUCTION BY DOUBLE-STRANDED DNA BREAKS-INDUCING TREATMENTS.
RX PubMed=17227549; DOI=10.1111/j.1365-313x.2006.02931.x;
RA Culligan K.M., Robertson C.E., Foreman J., Doerner P., Britt A.B.;
RT "ATR and ATM play both distinct and additive roles in response to ionizing
RT radiation.";
RL Plant J. 48:947-961(2006).
RN [8]
RP INTERACTION WITH CDKB1-1.
RX PubMed=20706207; DOI=10.1038/msb.2010.53;
RA Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
RA Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y., De Bodt S.,
RA Maere S., Laukens K., Pharazyn A., Ferreira P.C.G., Eloy N., Renne C.,
RA Meyer C., Faure J.-D., Steinbrenner J., Beynon J., Larkin J.C.,
RA Van de Peer Y., Hilson P., Kuiper M., De Veylder L., Van Onckelen H.,
RA Inze D., Witters E., De Jaeger G.;
RT "Targeted interactomics reveals a complex core cell cycle machinery in
RT Arabidopsis thaliana.";
RL Mol. Syst. Biol. 6:397-397(2010).
RN [9]
RP FUNCTION, MUTAGENESIS OF PRO-62, AND DISRUPTION PHENOTYPE.
RX PubMed=20485493; DOI=10.1371/journal.pbio.1000367;
RA Roeder A.H., Chickarmane V., Cunha A., Obara B., Manjunath B.S.,
RA Meyerowitz E.M.;
RT "Variability in the control of cell division underlies sepal epidermal
RT patterning in Arabidopsis thaliana.";
RL PLoS Biol. 8:E1000367-E1000367(2010).
RN [10]
RP INDUCTION BY ZEOCIN.
RX PubMed=21613568; DOI=10.1073/pnas.1103584108;
RA Adachi S., Minamisawa K., Okushima Y., Inagaki S., Yoshiyama K., Kondou Y.,
RA Kaminuma E., Kawashima M., Toyoda T., Matsui M., Kurihara D., Matsunaga S.,
RA Umeda M.;
RT "Programmed induction of endoreduplication by DNA double-strand breaks in
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:10004-10009(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH CPR5.
RX PubMed=25455564; DOI=10.1016/j.chom.2014.10.005;
RA Wang S., Gu Y., Zebell S.G., Anderson L.K., Wang W., Mohan R., Dong X.;
RT "A noncanonical role for the CKI-RB-E2F cell-cycle signaling pathway in
RT plant effector-triggered immunity.";
RL Cell Host Microbe 16:787-794(2014).
RN [12]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24399300; DOI=10.1105/tpc.113.118943;
RA Yi D., Alvim Kamei C.L., Cools T., Vanderauwera S., Takahashi N.,
RA Okushima Y., Eekhout T., Yoshiyama K.O., Larkin J., Van den Daele H.,
RA Conklin P., Britt A., Umeda M., De Veylder L.;
RT "The Arabidopsis SIAMESE-RELATED cyclin-dependent kinase inhibitors SMR5
RT and SMR7 regulate the DNA damage checkpoint in response to reactive oxygen
RT species.";
RL Plant Cell 26:296-309(2014).
RN [13]
RP FUNCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=26546445; DOI=10.1105/tpc.15.00489;
RA Kumar N., Harashima H., Kalve S., Bramsiepe J., Wang K., Sizani B.L.,
RA Bertrand L.L., Johnson M.C., Faulk C., Dale R., Simmons L.A.,
RA Churchman M.L., Sugimoto K., Kato N., Dasanayake M., Beemster G.,
RA Schnittger A., Larkin J.C.;
RT "Functional conservation in the SIAMESE-RELATED family of cyclin-dependent
RT kinase inhibitors in land plants.";
RL Plant Cell 27:3065-3080(2015).
CC -!- FUNCTION: Probable cyclin-dependent protein kinase (CDK) inhibitor that
CC functions as a repressor of mitosis in the endoreduplication cell cycle
CC (PubMed:17098811, PubMed:26546445). Cooperates with SIM and SMR2 to
CC promote endoreplication during leaf development (PubMed:26546445).
CC Specifically regulates endoreduplication in epidermal pavement cells to
CC produce the cell size pattern (PubMed:20485493). Is necessary for giant
CC cell formation (PubMed:20485493). Positive regulator of effector-
CC triggered immunity (ETI) (PubMed:25455564).
CC {ECO:0000269|PubMed:20485493, ECO:0000269|PubMed:25455564,
CC ECO:0000269|PubMed:26546445, ECO:0000305|PubMed:17098811}.
CC -!- SUBUNIT: Interacts with CDKB1-1 (PubMed:20706207). Interacts with CPR5
CC (PubMed:25455564). {ECO:0000269|PubMed:20706207,
CC ECO:0000269|PubMed:25455564}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17098811}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques and
CC flowers (PubMed:17098811). Expressed in the root elongation zone
CC (PubMed:24399300). {ECO:0000269|PubMed:17098811,
CC ECO:0000269|PubMed:24399300}.
CC -!- INDUCTION: Up-regulated by double-stranded DNA breaks-inducing
CC treatments (PubMed:17227549). Up-regulated by zeocin treatment
CC (PubMed:21613568). {ECO:0000269|PubMed:17227549,
CC ECO:0000269|PubMed:21613568}.
CC -!- DISRUPTION PHENOTYPE: Increased number of smaller cells and loss of
CC giant cells in sepals due to both a decrease in endoreduplication and
CC an average decrease in the duration of the cell cycle.
CC {ECO:0000269|PubMed:20485493}.
CC -!- MISCELLANEOUS: Over-expression of SMR1 produces additional giant cells
CC on sepals. {ECO:0000305|PubMed:20485493}.
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DR EMBL; AC013428; AAF76354.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74920.1; -; Genomic_DNA.
DR EMBL; AK118323; BAC42937.1; -; mRNA.
DR EMBL; BT024579; ABD38918.1; -; mRNA.
DR EMBL; AY086115; AAM63322.1; -; mRNA.
DR RefSeq; NP_566377.1; NM_111888.3.
DR AlphaFoldDB; Q9LPP4; -.
DR BioGRID; 5551; 10.
DR IntAct; Q9LPP4; 9.
DR STRING; 3702.AT3G10525.1; -.
DR iPTMnet; Q9LPP4; -.
DR PaxDb; Q9LPP4; -.
DR PRIDE; Q9LPP4; -.
DR EnsemblPlants; AT3G10525.1; AT3G10525.1; AT3G10525.
DR GeneID; 820217; -.
DR Gramene; AT3G10525.1; AT3G10525.1; AT3G10525.
DR KEGG; ath:AT3G10525; -.
DR Araport; AT3G10525; -.
DR TAIR; locus:505006334; AT3G10525.
DR HOGENOM; CLU_130615_0_0_1; -.
DR InParanoid; Q9LPP4; -.
DR OMA; IIMNREE; -.
DR OrthoDB; 1569151at2759; -.
DR PhylomeDB; Q9LPP4; -.
DR PRO; PR:Q9LPP4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LPP4; baseline and differential.
DR Genevisible; Q9LPP4; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IBA:GO_Central.
DR GO; GO:0032877; P:positive regulation of DNA endoreduplication; IMP:TAIR.
DR GO; GO:0090393; P:sepal giant cell development; IMP:TAIR.
DR InterPro; IPR040389; SMR.
DR PANTHER; PTHR33142; PTHR33142; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Protein kinase inhibitor; Reference proteome.
FT CHAIN 1..128
FT /note="Cyclin-dependent protein kinase inhibitor SMR1"
FT /id="PRO_0000418064"
FT REGION 17..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 62
FT /note="P->S: In lgo-1; loss of giant cells in sepals."
FT /evidence="ECO:0000269|PubMed:20485493"
FT CONFLICT 40
FT /note="R -> S (in Ref. 5; AAM63322)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="V -> A (in Ref. 3; BAC42937)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="V -> I (in Ref. 5; AAM63322)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14614 MW; BF272EEE4EB97134 CRC64;
MDLELLQDLS KFNFPTPIKI RSKTSKTKKD EGDDDEDDLR CSTPTSQEHK IPAVVDSPPP
PPRKPRPPPS APSATAALMI RSCKRKLLVS TCEIIMNREE IDRFFSSVYN ETSTTAKRRR
SYPYCSRR
