SMR5_ARATH
ID SMR5_ARATH Reviewed; 82 AA.
AC Q9LNX4; F4HQP3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cyclin-dependent protein kinase inhibitor SMR5 {ECO:0000303|PubMed:17599908, ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
DE AltName: Full=Protein SIAMESE-RELATED 5 {ECO:0000303|PubMed:17599908, ECO:0000303|PubMed:24399300, ECO:0000303|PubMed:26546445};
GN Name=SMR5 {ECO:0000303|PubMed:17599908, ECO:0000303|PubMed:24399300,
GN ECO:0000303|PubMed:26546445};
GN OrderedLocusNames=At1g07500 {ECO:0000312|Araport:AT1G07500};
GN ORFNames=F22G5.11 {ECO:0000312|EMBL:AAF79549.1};
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 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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17599908; DOI=10.1074/jbc.m703326200;
RA Peres A., Churchman M.L., Hariharan S., Himanen K., Verkest A.,
RA Vandepoele K., Magyar Z., Hatzfeld Y., Van Der Schueren E., Beemster G.T.,
RA Frankard V., Larkin J.C., Inze D., De Veylder L.;
RT "Novel plant-specific cyclin-dependent kinase inhibitors induced by biotic
RT and abiotic stresses.";
RL J. Biol. Chem. 282:25588-25596(2007).
RN [5]
RP INTERACTION WITH CDKA-1 AND D-TYPE CYCLINS.
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 [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY SOG1; DNA DAMAGE AND OXIDATIVE
RP STRESS, 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 INDUCTION BY IRON.
RX PubMed=25624148; DOI=10.1016/j.molp.2014.11.014;
RA Reyt G., Boudouf S., Boucherez J., Gaymard F., Briat J.F.;
RT "Iron- and ferritin-dependent reactive oxygen species distribution: impact
RT on Arabidopsis root system architecture.";
RL Mol. Plant 8:439-453(2015).
RN [9]
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:26546445). Acts as a potent cell cycle inhibitor, regulating a
CC hydroxyurea-dependent checkpoint in leaves (PubMed:24399300). Essential
CC to activate a high-light-dependent cell cycle checkpoint
CC (PubMed:24399300). {ECO:0000269|PubMed:24399300,
CC ECO:0000269|PubMed:26546445}.
CC -!- SUBUNIT: Interacts with CDKA-1 and D-type cyclins (PubMed:20706207).
CC {ECO:0000269|PubMed:20706207}.
CC -!- TISSUE SPECIFICITY: Expressed in columella cells in the roots and in
CC root meristems after induction. {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). Up-regulated by DNA damage and oxidative stress
CC (PubMed:24399300). Directly regulated by the transcription factor SOG1
CC (PubMed:24399300). Down-regulated by iron excess treatment
CC (PubMed:25624148). {ECO:0000269|PubMed:17227549,
CC ECO:0000269|PubMed:21613568, ECO:0000269|PubMed:24399300,
CC ECO:0000269|PubMed:25624148}.
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DR EMBL; AC022464; AAF79549.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28136.2; -; Genomic_DNA.
DR RefSeq; NP_001318942.1; NM_001331703.1.
DR AlphaFoldDB; Q9LNX4; -.
DR IntAct; Q9LNX4; 3.
DR PRIDE; Q9LNX4; -.
DR EnsemblPlants; AT1G07500.1; AT1G07500.1; AT1G07500.
DR GeneID; 837264; -.
DR Gramene; AT1G07500.1; AT1G07500.1; AT1G07500.
DR KEGG; ath:AT1G07500; -.
DR Araport; AT1G07500; -.
DR TAIR; locus:2024957; AT1G07500.
DR OMA; TRDDCRI; -.
DR PhylomeDB; Q9LNX4; -.
DR PRO; PR:Q9LNX4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LNX4; differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006974; P:cellular response to DNA damage stimulus; IGI:TAIR.
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; Protein kinase inhibitor; Reference proteome.
FT CHAIN 1..82
FT /note="Cyclin-dependent protein kinase inhibitor SMR5"
FT /id="PRO_0000438464"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 82 AA; 9212 MW; 6D5881BC8D6D675C CRC64;
MEEKNYDDGD TVTVDDDYQM GCTTPTRDDC RIPAYPPCPP PVRRKRSLLG FGKKREPPKK
GYFQPPDLDL FFSVVAASQA AT
