RSA1_ARATH
ID RSA1_ARATH Reviewed; 1340 AA.
AC F4IS91; O81059; Q0WQ79; Q8W4H5;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protein SHORT ROOT IN SALT MEDIUM 1 {ECO:0000303|PubMed:24009530};
DE Short=AtRSA1 {ECO:0000303|PubMed:24009530};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1579 {ECO:0000303|PubMed:15266054};
GN Name=RSA1 {ECO:0000303|PubMed:24009530};
GN Synonyms=emb1579 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At2g03150 {ECO:0000312|Araport:AT2G03150};
GN ORFNames=T18E12.18 {ECO:0000312|EMBL:AEC05669.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-828.
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 DISRUPTION PHENOTYPE [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-685, SUBCELLULAR
RP LOCATION, INTERACTION WITH BHLH148/RITF1 AND CALCIUM, TISSUE SPECIFICITY,
RP AND INDUCTION BY SALT STRESS.
RC STRAIN=cv. Columbia, and cv. Columbia GL1;
RX PubMed=24009530; DOI=10.1371/journal.pgen.1003755;
RA Guan Q., Wu J., Yue X., Zhang Y., Zhu J.;
RT "A nuclear calcium-sensing pathway is critical for gene regulation and salt
RT stress tolerance in Arabidopsis.";
RL PLoS Genet. 9:E1003755-E1003755(2013).
CC -!- FUNCTION: Required for salt tolerance and sodium (Na) homeostasis after
CC salt stress. Together with BHLH148/RITF1, regulates the transcription
CC of several genes involved in the detoxification of reactive oxygen
CC species (ROS) generated by salt (NaCl) stress. Binds calcium.
CC {ECO:0000269|PubMed:24009530}.
CC -!- SUBUNIT: Interacts with BHLH148/RITF1. {ECO:0000269|PubMed:24009530}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24009530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IS91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IS91-2; Sequence=VSP_059721, VSP_059722;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously at high levels, including in
CC guard cells. {ECO:0000269|PubMed:24009530}.
CC -!- INDUCTION: Slightly induced by salt (NaCl) stress.
CC {ECO:0000269|PubMed:24009530}.
CC -!- DISRUPTION PHENOTYPE: Defective embryo arrested at cotyledon stage
CC (PubMed:15266054). Hypersensitivity to salt (NaCl) stress leading to
CC reduced roots and shoots growth and altered germination, and associated
CC with altered sodium (Na) homeostasis and over-accumulation of reactive
CC oxygen species (ROS). Hypersensitivity to hydrogen peroxide H(2)O(2)
CC and methyl viologen (MV) (PubMed:24009530).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:24009530}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34487.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AC005313; AAC34487.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05669.1; -; Genomic_DNA.
DR EMBL; AK228824; BAF00720.1; -; mRNA.
DR EMBL; AY062555; AAL32633.1; -; mRNA.
DR PIR; T02711; T02711.
DR RefSeq; NP_178414.2; NM_126366.5. [F4IS91-1]
DR AlphaFoldDB; F4IS91; -.
DR SMR; F4IS91; -.
DR STRING; 3702.AT2G03150.1; -.
DR iPTMnet; F4IS91; -.
DR PaxDb; F4IS91; -.
DR PRIDE; F4IS91; -.
DR ProteomicsDB; 226783; -. [F4IS91-1]
DR EnsemblPlants; AT2G03150.1; AT2G03150.1; AT2G03150. [F4IS91-1]
DR GeneID; 814844; -.
DR Gramene; AT2G03150.1; AT2G03150.1; AT2G03150. [F4IS91-1]
DR KEGG; ath:AT2G03150; -.
DR Araport; AT2G03150; -.
DR TAIR; locus:2056881; AT2G03150.
DR eggNOG; KOG4246; Eukaryota.
DR HOGENOM; CLU_006390_0_0_1; -.
DR InParanoid; F4IS91; -.
DR OMA; GHQIHDR; -.
DR OrthoDB; 172375at2759; -.
DR PRO; PR:F4IS91; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IS91; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IDA:TAIR.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR GO; GO:0055078; P:sodium ion homeostasis; IMP:TAIR.
DR InterPro; IPR045354; BURAN.
DR InterPro; IPR025224; CCAR1/CCAR2.
DR InterPro; IPR025954; DBC1/CARP1_inactive_NUDIX_dom.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045353; LAIKA.
DR PANTHER; PTHR14304; PTHR14304; 1.
DR Pfam; PF19257; BURAN; 1.
DR Pfam; PF14443; DBC1; 1.
DR Pfam; PF19256; LAIKA; 1.
DR SMART; SM01122; DBC1; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Nucleus; Reference proteome;
KW Stress response; Transit peptide.
FT CHAIN 1..1340
FT /note="Protein SHORT ROOT IN SALT MEDIUM 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000445015"
FT DOMAIN 1270..1305
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 355..426
FT /evidence="ECO:0000255"
FT COILED 1052..1086
FT /evidence="ECO:0000255"
FT COMPBIAS 9..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1201..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1226..1269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 611..616
FT /note="HSFMAI -> QRNFGQ (in isoform 2)"
FT /id="VSP_059721"
FT VAR_SEQ 617..1340
FT /note="Missing (in isoform 2)"
FT /id="VSP_059722"
FT MUTAGEN 685
FT /note="P->L: In rsa1-1; hypersensitivity to salt (NaCl)
FT stress."
FT /evidence="ECO:0000269|PubMed:24009530"
FT CONFLICT 487
FT /note="V -> F (in Ref. 4; AAL32633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1340 AA; 150913 MW; 517DB2ABF7ECED80 CRC64;
MHRDMYSSRG TGYGQQQYGS QSGYSQNLGS GYPGSSVSGG AEGGSQISLS SRHPSITGAP
QETDIGGGYR SHLSTAASHY GTQYGSVYGS TSLSSSQPLS TNGLGSSVLD NRSGYVPTLP
DSPKFASGSY LSPSSHGYGQ KTDDLYSDKL SGYIPVDRRQ YGEQSSSYLG RELQNEPTRR
YADPSNFARQ TDLYDRIDQA SLLRGEQLLK MQSLHTSSVD AGVNRQTDYL TERSSTVRHS
DQEAMHYGGR LESDPHGLSV RNTSSYASQH TPSLLGAVPR RNLDDYIYPE SSSNPGYGVS
LPPGRDYGTG KGIHSAASLD LDYPGGMLAR GTGAAPRVDD LRKGDRASYL REFDLREEER
RREDQRARDK EREREREREH DRERERQRER ERQRARDRER ERILERREKE RQGERERERK
RALEIKRDRT PTARATSKDT KERTPVPKSI SRDARSSSLR RDAHHREASI RRSSPIKPIR
RDYVCKVLSS RLVDMERDYV TLDKRYPRLF VPSEFSKVVV NWPKQKLTLS MHTAVSFEHD
YIEDGGADVK STSTKPLALK TGGKSVWNAK MVLMSGLSRT ALEDLASDKF FEDRIPHICN
ILKFAVLKKD HSFMAIGGSW DPTDGMDPSV DQSSLIQTML RHSKDKLHLD LSNCRHWNPF
LEIHYDRVGT DGVFSYKEIT VLFVPDLSEC LPSFDVWRTQ WLAHRKALTE RDRLLSQEVK
KDTVEVTKDA EKKSPGDTSG TPTTGTKKTV KKIIKRVVKR PVNDGKATGM KGEKSDVPEH
VAIPETTVPK EESTGTSSNK KIVKKVAETG DTSDPSAKAN EQTPAKTIVK KKIIKRVAKR
KVAEIDNKMD GDSKKDGDSD EKKVMEVGKK SSDSGSVEMK PTAESLEDVK DENASKTVDV
KQETGSPDTK KKEGASSSSK KDTKTGEDKK AEKKNNSETM SEGKKIDRNN TDEKEVKEKV
TEKEIKERGG KDESRIQVKD RKKCEEPPRA GFILQTKRNK DSKLRSLSAS LDSLLDYTDK
DLDESSFEIS LFAESLYEML QYQMGSRIFE FLKKLRVKIV RQRNQRKRHQ EELSVKQNEA
KSQDKRQKTA EHEDKEASVI SESAPGKDDK ETSGKETVDG SREIADKEAV AKTKETLGSK
EVTVGEAVNM EVENQDEEDD DGDDDPEEDP EEDPEEDPEE DPEEDPEECE EMDVANTEQE
EPAEEPQKKE ENLEKTSGTV ADPITEAETD NRKEERGPND SKTEIKPKSE TEKHGKQDGG
TSDAAKREET VDKELLQAFR FFDRNQAGYV RVEDMRVTIH SLGKFLSHRE VKELVQSALL
ESNTGRDDRI LYNKLVRLSL
