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SMXL4_ARATH
ID   SMXL4_ARATH             Reviewed;        1017 AA.
AC   Q9SZR3;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Protein SMAX1-LIKE 4 {ECO:0000303|PubMed:23893171};
DE            Short=AtSMXL4 {ECO:0000303|PubMed:23893171};
DE   AltName: Full=Protein HEAT SHOCK PROTEIN-RELATED {ECO:0000303|PubMed:26603028};
DE            Short=AtHSPR {ECO:0000303|PubMed:26603028};
DE            EC=3.6.3.- {ECO:0000269|PubMed:26603028};
GN   Name=SMXL4 {ECO:0000303|PubMed:23893171};
GN   Synonyms=HSPR {ECO:0000303|PubMed:26603028};
GN   OrderedLocusNames=At4g29920 {ECO:0000312|Araport:AT4G29920};
GN   ORFNames=F27B13.160 {ECO:0000312|EMBL:CAB43667.1};
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   TISSUE SPECIFICITY, 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   [4]
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=24675528; DOI=10.1016/j.plaphy.2014.02.019;
RA   Zhang L., Yang T., Li X., Hao H., Xu S., Cheng W., Sun Y., Wang C.;
RT   "Cloning and characterization of a novel Athspr promoter specifically
RT   active in vascular tissue.";
RL   Plant Physiol. Biochem. 78:88-96(2014).
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY SLAT AND ABSCISIC ACID.
RX   PubMed=26603028; DOI=10.1111/tpj.13080;
RA   Yang T., Zhang L., Hao H., Zhang P., Zhu H., Cheng W., Wang Y., Wang X.,
RA   Wang C.;
RT   "Nuclear-localized AtHSPR links abscisic acid-dependent salt tolerance and
RT   antioxidant defense in Arabidopsis.";
RL   Plant J. 84:1274-1294(2015).
CC   -!- FUNCTION: Probable component of a transcriptional corepressor complex
CC       involved in salt tolerance through modulation of reactive oxygen
CC       species levels, abscisic acid-dependent stomatal closure,
CC       photosynthesis and K(+) /Na(+) homeostasis (PubMed:26603028). Has an in
CC       vitro ATPase activity (PubMed:26603028). {ECO:0000269|PubMed:26603028}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=348 uM for ATP {ECO:0000269|PubMed:26603028};
CC         Vmax=0.77 umol/h/mg enzyme {ECO:0000269|PubMed:26603028};
CC         Note=kcat is 0.17 min(-1) for ATP. {ECO:0000269|PubMed:26603028};
CC   -!- SUBUNIT: Interacts probably with TPL/TPR in an EAR-motif dependent
CC       manner. {ECO:0000250|UniProtKB:Q9FHH2}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26603028}.
CC   -!- TISSUE SPECIFICITY: Detected in seedlings and roots (PubMed:23893171).
CC       Expressed specifically in vascular tissues (PubMed:24675528). Expressed
CC       in flowers, stems, siliques, leaves and roots, with the highest
CC       expression in open flowers and the lowest in leaves (PubMed:26603028).
CC       {ECO:0000269|PubMed:23893171, ECO:0000269|PubMed:24675528,
CC       ECO:0000269|PubMed:26603028}.
CC   -!- INDUCTION: Up-regulated by salt and abscisic acid treatment.
CC       {ECO:0000269|PubMed:26603028}.
CC   -!- DISRUPTION PHENOTYPE: Reduced drought tolerance and hypersensitivity to
CC       salt stress, resulting in poor growth in normal soil.
CC       {ECO:0000269|PubMed:26603028}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AL050352; CAB43667.1; -; Genomic_DNA.
DR   EMBL; AL161575; CAB79750.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85693.1; -; Genomic_DNA.
DR   PIR; T08553; T08553.
DR   RefSeq; NP_194721.1; NM_119138.2.
DR   AlphaFoldDB; Q9SZR3; -.
DR   STRING; 3702.AT4G29920.1; -.
DR   iPTMnet; Q9SZR3; -.
DR   PaxDb; Q9SZR3; -.
DR   PRIDE; Q9SZR3; -.
DR   EnsemblPlants; AT4G29920.1; AT4G29920.1; AT4G29920.
DR   GeneID; 829115; -.
DR   Gramene; AT4G29920.1; AT4G29920.1; AT4G29920.
DR   KEGG; ath:AT4G29920; -.
DR   Araport; AT4G29920; -.
DR   TAIR; locus:2123944; AT4G29920.
DR   eggNOG; KOG1051; Eukaryota.
DR   HOGENOM; CLU_006575_0_0_1; -.
DR   InParanoid; Q9SZR3; -.
DR   PhylomeDB; Q9SZR3; -.
DR   SABIO-RK; Q9SZR3; -.
DR   PRO; PR:Q9SZR3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SZR3; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0033500; P:carbohydrate homeostasis; IGI:TAIR.
DR   GO; GO:0042631; P:cellular response to water deprivation; IMP:TAIR.
DR   GO; GO:0010233; P:phloem transport; IGI:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF02861; Clp_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1017
FT                   /note="Protein SMAX1-LIKE 4"
FT                   /id="PRO_0000435713"
FT   DOMAIN          8..183
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          12..91
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          105..183
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          196..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           859..863
FT                   /note="EAR"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1017 AA;  113784 MW;  90809F6CBCB99821 CRC64;
     MRTGAYTVHQ TLTPEAASVL KQSLTLARRR GHSQVTPLHV ASTLLTSSRS NLFRRACLKS
     NPFTALGRQM AHPSLHCRAL ELCFNVSLNR LPTNPNPLFQ TQPSLSNALV AALKRAQAHQ
     RRGCVEQQQS QQNQPFLAVK VELEQLVVSI LDDPSVSRVM REAGLSSVSV KSNIEDDSSV
     VSPVFYGSSS SVGVFSSPCS PSSSENNQGG GTLSPNPSKI WHAHLTNHHS FEQNPFFHFP
     KGKTFTPDQA FPVREDANPV IEVLLGKKNN KKRNTVIVGD SVSLTEGVVA KLMGRIERGE
     VPDDLKQTHF IKFQFSQVGL NFMKKEDIEG QVRELKRKID SFTSWGGKGV IVCLGDLDWA
     VWGGGNSASS SNYSAADHLV EEIGRLVYDY SNTGAKVWLL GTASYQTYMR CQMKQPPLDV
     HWALQAVSIP SGGLSLTLHA SSSEMASQVM EMKPFRVKEE EEGAREEEEE DKLNFCGECA
     FNYEKEAKAF ISAQHKILPP WLQPHGDNNN INQKDELSGL RKKWNRFCQA LHHKKPSMTA
     WRAEQSSSVL PGSLMDSSLK QNSRASSSVA KFRRQNSCTI EFSFGSNRQE GLKKTDELSL
     DGFKSNNDEG VKTKITLALG HSPFPSDSEN SEEEEPEKAI KMSKLLEKLH ENIPWQKDVL
     PSIVEAMEES VKRSKRKDAW MLVSGNDVTA KRRLAITLTT SLFGSHENML KINLRTSKAS
     EACEELKNAL KKKEEVVILI ERVDLADAQF MNILVDRFEA GDLDGFQGKK SQIIFLLTRE
     DDECVENEHF VIPMVLNCNK SGSGLVNNKR KPEYDAAPTM IKKKNPRIEE DDDESNVACD
     ISNIKKEFSR QLKFESNALD LNLRVDADED EEEEAKPATE ISSGFEERFL DSIQNRFDFT
     VLSDEDITKF FVTKIKDSCE EILGQREERF GFTVDAELIE KFYKGCGFFA NGLFEEWVKE
     VFQRGLVTVK NGGKEGISVI NLCLGGIDMI DQGEVYEEEE GFMGTCLPNR IHVSFVD
 
 
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