SMR2_ARATH
ID SMR2_ARATH Reviewed; 111 AA.
AC Q9SGE2; Q9LMZ1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cyclin-dependent protein kinase inhibitor SMR2 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
DE AltName: Full=Protein SIAMESE-RELATED 2 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
GN Name=SMR2 {ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
GN OrderedLocusNames=At1g08180; ORFNames=T23G18.4, T6D22.27;
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 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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH CYCD2-1, 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 [6]
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 [7]
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 [8]
RP FUNCTION, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
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: Cyclin-dependent protein kinase (CDK) inhibitor that
CC restricts cell proliferation and cooperates with SIM and SMR1 to
CC promote endoreplication during leaf development (PubMed:26546445).
CC {ECO:0000269|PubMed:26546445}.
CC -!- SUBUNIT: Interacts with CYCD2-1 (PubMed:17098811). Interacts with
CC CDKB1-1 (PubMed:20706207). {ECO:0000269|PubMed:17098811,
CC ECO:0000269|PubMed:20706207}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17098811}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots and stems
CC (PubMed:17098811). Expressed in the root vascular tissue
CC (PubMed:24399300). {ECO:0000269|PubMed:17098811,
CC ECO:0000269|PubMed:24399300}.
CC -!- DISRUPTION PHENOTYPE: Larger leaves with an increased cell number.
CC {ECO:0000269|PubMed:26546445}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC011438; AAF18255.1; -; Genomic_DNA.
DR EMBL; AC026875; AAF79829.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28258.1; -; Genomic_DNA.
DR EMBL; BT004747; AAO44013.1; -; mRNA.
DR EMBL; BT005800; AAO64202.1; -; mRNA.
DR EMBL; AK227946; BAE99914.1; -; mRNA.
DR PIR; B86216; B86216.
DR RefSeq; NP_172296.1; NM_100692.3.
DR AlphaFoldDB; Q9SGE2; -.
DR BioGRID; 22580; 3.
DR IntAct; Q9SGE2; 4.
DR STRING; 3702.AT1G08180.1; -.
DR PaxDb; Q9SGE2; -.
DR PRIDE; Q9SGE2; -.
DR ProteomicsDB; 232643; -.
DR EnsemblPlants; AT1G08180.1; AT1G08180.1; AT1G08180.
DR GeneID; 837339; -.
DR Gramene; AT1G08180.1; AT1G08180.1; AT1G08180.
DR KEGG; ath:AT1G08180; -.
DR Araport; AT1G08180; -.
DR TAIR; locus:2199998; AT1G08180.
DR eggNOG; ENOG502SUX3; Eukaryota.
DR HOGENOM; CLU_2174516_0_0_1; -.
DR InParanoid; Q9SGE2; -.
DR OMA; IPEVETC; -.
DR OrthoDB; 1589982at2759; -.
DR PhylomeDB; Q9SGE2; -.
DR PRO; PR:Q9SGE2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGE2; baseline and differential.
DR Genevisible; Q9SGE2; 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:0045839; P:negative regulation of mitotic nuclear division; IBA:GO_Central.
DR GO; GO:0032875; P:regulation of DNA endoreduplication; IEA:InterPro.
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..111
FT /note="Cyclin-dependent protein kinase inhibitor SMR2"
FT /id="PRO_0000418065"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 111 AA; 12910 MW; FB8A841B4078A9EC CRC64;
MSKLLETLEE EKTVEQKPRS QEEEDHQDSS KKEELLESLC TPTSSDHKIP EVETCPPPPR
KRPREISLTK KTRLSKDLRF FEATDVGSQE VETLFVHEPN HVRKKRRSNS A