SEBP1_ARATH
ID SEBP1_ARATH Reviewed; 490 AA.
AC O23264; Q42178; Q93WU0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Selenium-binding protein 1 {ECO:0000303|PubMed:18354042};
DE Short=AtSBP1 {ECO:0000303|PubMed:25274629};
GN Name=SBP1 {ECO:0000303|PubMed:18354042};
GN OrderedLocusNames=At4g14030 {ECO:0000312|Araport:AT4G14030};
GN ORFNames=dl3055c {ECO:0000312|EMBL:CAB10182.1},
GN FCAALL.79 {ECO:0000312|EMBL:CAB78445.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-145.
RC STRAIN=cv. Columbia; TISSUE=Seed;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-490.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=12026169; DOI=10.1094/mpmi.2002.15.4.313;
RA Flemetakis E., Agalou A., Kavroulakis N., Dimou M., Martsikovskaya A.,
RA Slater A., Spaink H.P., Roussis A., Katinakis P.;
RT "Lotus japonicus gene Ljsbp is highly conserved among plants and animals
RT and encodes a homologue to the mammalian selenium-binding proteins.";
RL Mol. Plant Microbe Interact. 15:313-322(2002).
RN [7]
RP INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY CADMIUM.
RX PubMed=18354042; DOI=10.1104/pp.107.114033;
RA Dutilleul C., Jourdain A., Bourguignon J., Hugouvieux V.;
RT "The Arabidopsis putative selenium-binding protein family: expression study
RT and characterization of SBP1 as a potential new player in cadmium
RT detoxification processes.";
RL Plant Physiol. 147:239-251(2008).
RN [9]
RP FUNCTION, INDUCTION, AND CADMIUM BINDING.
RC STRAIN=cv. Columbia;
RX PubMed=19710230; DOI=10.1104/pp.109.144808;
RA Hugouvieux V., Dutilleul C., Jourdain A., Reynaud F., Lopez V.,
RA Bourguignon J.;
RT "Arabidopsis putative selenium-binding protein1 expression is tightly
RT linked to cellular sulfur demand and can reduce sensitivity to stresses
RT requiring glutathione for tolerance.";
RL Plant Physiol. 151:768-781(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP FUNCTION, SELENIUM-BINDING SITES, AND MUTAGENESIS OF 21-CYS-CYS-22.
RX PubMed=25274629; DOI=10.1074/jbc.m114.571208;
RA Schild F., Kieffer-Jaquinod S., Palencia A., Cobessi D., Sarret G.,
RA Zubieta C., Jourdain A., Dumas R., Forge V., Testemale D., Bourguignon J.,
RA Hugouvieux V.;
RT "Biochemical and biophysical characterization of the selenium-binding and
RT reducing site in Arabidopsis thaliana homologue to mammals selenium-binding
RT protein 1.";
RL J. Biol. Chem. 289:31765-31776(2014).
RN [12]
RP INTERACTION WITH GRXS14 AND GRXS16.
RX PubMed=30824043; DOI=10.1016/j.plantsci.2019.01.021;
RA Valassakis C., Dervisi I., Agalou A., Papandreou N., Kapetsis G., Podia V.,
RA Haralampidis K., Iconomidou V.A., Spaink H.P., Roussis A.;
RT "Novel interactions of selenium binding protein family with the PICOT
RT containing proteins AtGRXS14 and AtGRXS16 in Arabidopsis thaliana.";
RL Plant Sci. 281:102-112(2019).
RN [13]
RP INTERACTION WITH DALL3, AND INDUCTION.
RX PubMed=31928671; DOI=10.1016/j.plantsci.2019.110357;
RA Dervisi I., Valassakis C., Agalou A., Papandreou N., Podia V.,
RA Haralampidis K., Iconomidou V.A., Kouvelis V.N., Spaink H.P., Roussis A.;
RT "Investigation of the interaction of DAD1-LIKE LIPASE 3 (DALL3) with
RT Selenium Binding Protein 1 (SBP1) in Arabidopsis thaliana.";
RL Plant Sci. 291:110357-110357(2020).
CC -!- FUNCTION: Binds cadmium and mediates lower sensitivity to stress
CC requiring glutathione (GSH) for tolerance (e.g. cadmium, selenate, and
CC hydrogen peroxide excess). Probably helps to detoxify cadmium
CC potentially through direct binding (PubMed:18354042, PubMed:19710230).
CC Binds selenium, cadmium, zinc and nickel in vitro (PubMed:25274629).
CC {ECO:0000269|PubMed:18354042, ECO:0000269|PubMed:19710230,
CC ECO:0000269|PubMed:25274629}.
CC -!- SUBUNIT: Interacts with GRXS14 and GRXS16 (PubMed:30824043). Interacts
CC with DALL3 (PubMed:31928671). {ECO:0000269|PubMed:30824043,
CC ECO:0000269|PubMed:31928671}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems and
CC flowers. {ECO:0000269|PubMed:18354042}.
CC -!- INDUCTION: Induced by cadmium (at protein level) (PubMed:16502469,
CC PubMed:18354042, PubMed:19710230). Induced by selenium (selenate),
CC copper and hydrogen peroxide H(2)O(2) (at protein level)
CC (PubMed:16502469, PubMed:18354042, PubMed:19710230). The induction in
CC response to sulfur starvation is repressed by glutathione (GSH) (at
CC protein level) (PubMed:19710230). {ECO:0000269|PubMed:16502469,
CC ECO:0000269|PubMed:18354042, ECO:0000269|PubMed:19710230}.
CC -!- SIMILARITY: Belongs to the selenium-binding protein family.
CC {ECO:0000305}.
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DR EMBL; Z97335; CAB10182.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78445.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83362.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83363.1; -; Genomic_DNA.
DR EMBL; AY062634; AAL32712.1; -; mRNA.
DR EMBL; AY128727; AAM91127.1; -; mRNA.
DR EMBL; Z27257; CAA81769.1; -; mRNA.
DR EMBL; AJ401229; CAC67446.1; -; mRNA.
DR PIR; D71401; D71401.
DR RefSeq; NP_001190723.1; NM_001203794.2.
DR RefSeq; NP_193139.1; NM_117478.6.
DR AlphaFoldDB; O23264; -.
DR SMR; O23264; -.
DR BioGRID; 12336; 1.
DR STRING; 3702.AT4G14030.1; -.
DR iPTMnet; O23264; -.
DR PaxDb; O23264; -.
DR PRIDE; O23264; -.
DR ProteomicsDB; 232925; -.
DR EnsemblPlants; AT4G14030.1; AT4G14030.1; AT4G14030.
DR EnsemblPlants; AT4G14030.2; AT4G14030.2; AT4G14030.
DR GeneID; 827039; -.
DR Gramene; AT4G14030.1; AT4G14030.1; AT4G14030.
DR Gramene; AT4G14030.2; AT4G14030.2; AT4G14030.
DR KEGG; ath:AT4G14030; -.
DR Araport; AT4G14030; -.
DR TAIR; locus:2129351; AT4G14030.
DR eggNOG; KOG0918; Eukaryota.
DR HOGENOM; CLU_032512_0_0_1; -.
DR InParanoid; O23264; -.
DR OMA; FDSEFNC; -.
DR OrthoDB; 483905at2759; -.
DR PhylomeDB; O23264; -.
DR PRO; PR:O23264; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23264; baseline and differential.
DR Genevisible; O23264; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008430; F:selenium binding; IEA:InterPro.
DR GO; GO:0071291; P:cellular response to selenium ion; IDA:TAIR.
DR GO; GO:0046686; P:response to cadmium ion; IDA:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:TAIR.
DR GO; GO:0000103; P:sulfate assimilation; IEP:TAIR.
DR InterPro; IPR008826; Se-bd.
DR PANTHER; PTHR23300; PTHR23300; 1.
DR Pfam; PF05694; SBP56; 1.
PE 1: Evidence at protein level;
KW Acetylation; Reference proteome; Selenium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..490
FT /note="Selenium-binding protein 1"
FT /id="PRO_0000174636"
FT SITE 21
FT /note="Selenium binding"
FT /evidence="ECO:0000269|PubMed:25274629"
FT SITE 22
FT /note="Selenium binding"
FT /evidence="ECO:0000269|PubMed:25274629"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 21..22
FT /note="CC->SS: Abolishes the capacity to bind selenium."
FT /evidence="ECO:0000269|PubMed:25274629"
FT CONFLICT 13
FT /note="V -> L (in Ref. 5; CAA81769)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..24
FT /note="GCCKY -> RMLQV (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..128
FT /note="RIYAIDTKE -> SHLCDLDTKG (in Ref. 5; CAA81769)"
FT /evidence="ECO:0000305"
FT CONFLICT 138..145
FT /note="YVDPKEIA -> VMLIPKEI (in Ref. 5; CAA81769)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="LA -> R (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="F -> L (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..199
FT /note="GH -> DI (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="D -> H (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 428..430
FT /note="DRQ -> VVS (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="V -> G (in Ref. 6; CAC67446)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54057 MW; 10EE7B9BCF2F0390 CRC64;
MATETEVVAP VTVSNGGSKG CCKYGGPGYA TPLAAMSGPS EKLIYVTAVY TGTGIDKPDY
LATVDVDPSS PSYSSVIHRL PMPFVGDELH HSGWNSCSSC HGDASVDRRY LVLPSLISGR
IYAIDTKENP RAPSLYKYVD PKEIADKTGL AFPHTAHCLA TGEILVSCLG DEEGNAKGNG
FLLLDSDFNI KNRWEKPGHS PLYGYDFWYQ PRHKTMISTS WGAPKAFSKG FNLQHVADGL
YGSHLHVYSW PGGEIKQLID LGPTGLLPLE IRFLHDPSKD TGFVGSALSS NMIRFFKNSD
ETWSHEVVIS VKPLKVENWI LPEMPGLITD FLISLDDRFI YFVNWLHGDI RQYNIEDPKN
PVLTGQIWVG GLLQKGSPVK AVGEDGNTFQ FEVPQIKGKS LRGGPQMIQL SLDGKRLYAT
NSLFSAWDRQ FYPEIMEKGS HIIQIDVDTE KGGLTINPDF FVDFGDEPDG PSLAHEMRYP
GGDCTSDIWI
