SAD2_ARATH
ID SAD2_ARATH Reviewed; 1040 AA.
AC F4IRR2; Q56W71; Q8GZ12; Q9SIP2;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Importin beta-like SAD2 {ECO:0000305};
DE AltName: Full=Protein ENHANCED MIRNA ACTIVITY 1 {ECO:0000303|PubMed:21984696};
DE AltName: Full=Protein SUPER SENSITIVE TO ABA AND DROUGHT 2 {ECO:0000303|PubMed:16889648};
DE AltName: Full=Protein UNARMED 9 {ECO:0000303|PubMed:19234066};
GN Name=SAD2 {ECO:0000303|PubMed:16889648};
GN Synonyms=EMA1 {ECO:0000303|PubMed:21984696},
GN URM9 {ECO:0000303|PubMed:19234066};
GN OrderedLocusNames=At2g31660 {ECO:0000312|Araport:AT2G31660};
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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 669-1040.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16889648; DOI=10.1111/j.1365-313x.2006.02833.x;
RA Verslues P.E., Guo Y., Dong C.H., Ma W., Zhu J.K.;
RT "Mutation of SAD2, an importin beta-domain protein in Arabidopsis, alters
RT abscisic acid sensitivity.";
RL Plant J. 47:776-787(2006).
RN [6]
RP FUNCTION, AND INTERACTION WITH MYB4.
RX PubMed=17993626; DOI=10.1105/tpc.106.048900;
RA Zhao J., Zhang W., Zhao Y., Gong X., Guo L., Zhu G., Wang X., Gong Z.,
RA Schumaker K.S., Guo Y.;
RT "SAD2, an importin -like protein, is required for UV-B response in
RT Arabidopsis by mediating MYB4 nuclear trafficking.";
RL Plant Cell 19:3805-3818(2007).
RN [7]
RP FUNCTION.
RX PubMed=18713401; DOI=10.1111/j.1744-7909.2008.00695.x;
RA Gao Y., Gong X., Cao W., Zhao J., Fu L., Wang X., Schumaker K.S., Guo Y.;
RT "SAD2 in Arabidopsis functions in trichome initiation through mediating GL3
RT function and regulating GL1, TTG1 and GL2 expression.";
RL J. Integr. Plant Biol. 50:906-917(2008).
RN [8]
RP FUNCTION.
RX PubMed=19234066; DOI=10.1242/dev.030585;
RA Yoshida Y., Sano R., Wada T., Takabayashi J., Okada K.;
RT "Jasmonic acid control of GLABRA3 links inducible defense and trichome
RT patterning in Arabidopsis.";
RL Development 136:1039-1048(2009).
RN [9]
RP FUNCTION.
RX PubMed=21984696; DOI=10.1105/tpc.111.091058;
RA Wang W., Ye R., Xin Y., Fang X., Li C., Shi H., Zhou X., Qi Y.;
RT "An importin beta protein negatively regulates microRNA activity in
RT Arabidopsis.";
RL Plant Cell 23:3565-3576(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
CC -!- FUNCTION: Functions probably in nuclear protein import, either by
CC acting as autonomous nuclear transport receptor or as an adapter-like
CC protein in association with other importin subunits (Probable).
CC Involved in the regulation of the abscisic acid (ABA)-mediated pathway
CC in response to cold or salt stress (PubMed:16889648). Involved in UV-B
CC responses by regulating accumulation of UV-absorbing pigments through
CC mediation of MYB4 nuclear transport (PubMed:17993626). Involved in
CC trichome initiation by controlling GL1, GL2, GL3 and TTG1 transcription
CC and may affect an upstream regulator of GL3 and disrupt complex
CC function (PubMed:18713401, PubMed:19234066). Acts as negative regulator
CC miRNA activity by regulating miRNA loading into AGO1 complexes
CC (PubMed:21984696). {ECO:0000269|PubMed:16889648,
CC ECO:0000269|PubMed:17993626, ECO:0000269|PubMed:18713401,
CC ECO:0000269|PubMed:19234066, ECO:0000269|PubMed:21984696, ECO:0000305}.
CC -!- SUBUNIT: Interacts with MYB4. {ECO:0000269|PubMed:17993626}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16889648}. Nucleus
CC {ECO:0000269|PubMed:16889648}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, epidermal and guard cells of
CC leaves, stems and siliques. {ECO:0000269|PubMed:16889648}.
CC -!- DISRUPTION PHENOTYPE: Early flowering and increased sensitivity to
CC inhibition of seed germination and plant growth by exogenous ABA.
CC {ECO:0000269|PubMed:16889648}.
CC -!- SIMILARITY: Belongs to the importin beta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24843.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC41944.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC007071; AAD24843.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08570.1; -; Genomic_DNA.
DR EMBL; AK117271; BAC41944.1; ALT_FRAME; mRNA.
DR EMBL; AK222176; BAD95304.1; -; mRNA.
DR PIR; E84723; E84723.
DR RefSeq; NP_180724.2; NM_128723.3.
DR AlphaFoldDB; F4IRR2; -.
DR SMR; F4IRR2; -.
DR STRING; 3702.AT2G31660.1; -.
DR iPTMnet; F4IRR2; -.
DR PaxDb; F4IRR2; -.
DR PRIDE; F4IRR2; -.
DR ProMEX; F4IRR2; -.
DR ProteomicsDB; 232729; -.
DR EnsemblPlants; AT2G31660.1; AT2G31660.1; AT2G31660.
DR GeneID; 817722; -.
DR Gramene; AT2G31660.1; AT2G31660.1; AT2G31660.
DR KEGG; ath:AT2G31660; -.
DR Araport; AT2G31660; -.
DR TAIR; locus:2065939; AT2G31660.
DR eggNOG; KOG1991; Eukaryota.
DR HOGENOM; CLU_004196_1_0_1; -.
DR InParanoid; F4IRR2; -.
DR OMA; NHWWKCK; -.
DR OrthoDB; 159062at2759; -.
DR PRO; PR:F4IRR2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IRR2; baseline and differential.
DR Genevisible; F4IRR2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; IDA:TAIR.
DR GO; GO:0070922; P:RISC complex assembly; IMP:TAIR.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR013713; XPO2_central.
DR Pfam; PF08506; Cse1; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW Stress response; Transport.
FT CHAIN 1..1040
FT /note="Importin beta-like SAD2"
FT /id="PRO_0000431577"
FT DOMAIN 25..103
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REGION 893..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..927
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 1040 AA; 119247 MW; 256F8ABB354390AB CRC64;
MDLHSLALIL RTAALSPIPD ERKVSEQQLN QLEHTPQHLV RLLQIAVDGN CDMAVRQIAS
IQFKNLIAKN WSPEDCGPAV RQQQIFESDK ELVRDNILVY VTQVPTLLRS QLGESLKTII
YADYPEQWPR LLDWVKYNLQ NQQIYGALFV LRILSRKYEF KSDEERTPVS RIVEETFPQL
LTIFNGLIQI PNPSLEIAEL MKLICKIFWS SIYLELPRQL FDLNVFNAWM VLFLSVSERP
VPVEGQPMDP ELRKSWGWWK VKKWTVHILN RLYSRFGDPK LQSPENKPFA QMFQKNYAGR
ILEGHLNFLN TIRVGGYLPD RVINLLLQYL SNSISKNSMY KLLLPRLDVL LFEIVFPLMC
FNDNDQKLWE EDPHEYVRKG YNIIEDLYSP RTASMDFVNE LVRKRGKENL PKFVKFVVEI
FLSYEKATVE EKPYRQKDGA MLAVGALCDK LKQTDPYKSQ LELMLVQHIF PDFNSPVGHL
RAKAAWVAGQ YAHINFSDQN NFRKALHSVV SGLRDPDLPV RVDSVFALRS FVEACKDLNE
IRPILPQLLD EFFKLMNEVE NEDLVFTLET IVDKFGEEMA PFAFGLCQNL AAAFWRCLNT
SEANDDSDDM GALAAVGCLR AISTILESVS SLPQLFVEIE PTILPIMQKM LTTDGQEVFE
EVLEIASYMT FYSPSISLDI WSLWPLMVEA LVDWGIDFFP NILVPMDNFI SRGTAHFLTC
KEPDYQQSLY NVLSTLMTDR NIEDSEIESA PKLIEVVFQN CKGQVDQWVE PYLRLTVDRL
QRAETSYVKS LLIQVVANML YYNPGLTLGV LHNTGLASKV FDLWFQMLQQ KRKSGLPANF
KREHDKKVCC LGLTSLLALP GGQFPDEALQ RVFRATLDLL VAYKNQLAEA AKETEVDYEE
EMNGLQSSDD DYDDDGSDGE MDDTEEGDEA QSVKLQKLAA QAKAFHYDDD DDDDSDDDFS
DEDEFQSPID EVDAFVFFVD AIRVMQASDA QRFQNLNQSL DFTYQAIANG IAQHAELRRV
EIEKEKQKKL AAASTPVTAL
