STOP2_ARATH
ID STOP2_ARATH Reviewed; 373 AA.
AC Q0WT24; Q9FFB9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein SENSITIVE TO PROTON RHIZOTOXICITY 2 {ECO:0000303|PubMed:23935008};
DE AltName: Full=Zinc finger protein STOP2 {ECO:0000303|PubMed:23935008};
GN Name=STOP2 {ECO:0000303|PubMed:23935008};
GN OrderedLocusNames=At5g22890 {ECO:0000312|Araport:AT5G22890};
GN ORFNames=MRN17.12 {ECO:0000312|EMBL:BAB10610.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
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 139-373.
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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23935008; DOI=10.1093/mp/sst116;
RA Kobayashi Y., Ohyama Y., Kobayashi Y., Ito H., Iuchi S., Fujita M.,
RA Zhao C.-R., Tanveer T., Ganesan M., Kobayashi M., Koyama H.;
RT "STOP2 activates transcription of several genes for Al- and low pH-
RT tolerance that are regulated by STOP1 in Arabidopsis.";
RL Mol. Plant 7:311-322(2014).
CC -!- FUNCTION: Probable transcription factor. Together with STOP1, plays a
CC critical role in tolerance to major stress factors in acid soils such
CC as proton H(+) and aluminum ion Al(3+). Required for the expression of
CC genes in response to acidic stress (e.g. ALMT1 and MATE), and Al-
CC activated citrate exudation. {ECO:0000269|PubMed:23935008}.
CC -!- INTERACTION:
CC Q0WT24; O80575: At2g44050; NbExp=3; IntAct=EBI-4424123, EBI-4473692;
CC Q0WT24; Q17TI5: BRX; NbExp=3; IntAct=EBI-4424123, EBI-4426649;
CC Q0WT24; O23160: MYB73; NbExp=3; IntAct=EBI-4424123, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23935008}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots (e.g. root tips
CC and lateral roots), leaves (e.g. at the edge of mature leaves, possibly
CC in hydathodes, and in vascular bundles), flowers (e.g. floral
CC filaments), stems, siliques and cotyledons.
CC {ECO:0000269|PubMed:23935008}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10610.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB005243; BAB10610.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED93094.1; -; Genomic_DNA.
DR EMBL; AK227740; BAE99724.1; -; mRNA.
DR EMBL; BT004810; AAO44076.1; -; mRNA.
DR RefSeq; NP_197680.2; NM_122195.4.
DR AlphaFoldDB; Q0WT24; -.
DR IntAct; Q0WT24; 13.
DR STRING; 3702.AT5G22890.1; -.
DR PaxDb; Q0WT24; -.
DR PRIDE; Q0WT24; -.
DR ProteomicsDB; 245220; -.
DR EnsemblPlants; AT5G22890.1; AT5G22890.1; AT5G22890.
DR GeneID; 832353; -.
DR Gramene; AT5G22890.1; AT5G22890.1; AT5G22890.
DR KEGG; ath:AT5G22890; -.
DR Araport; AT5G22890; -.
DR TAIR; locus:2172701; AT5G22890.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_029078_1_1_1; -.
DR InParanoid; Q0WT24; -.
DR OMA; CNTHEDN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q0WT24; -.
DR PRO; PR:Q0WT24; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q0WT24; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0010447; P:response to acidic pH; IMP:UniProtKB.
DR GO; GO:0010044; P:response to aluminum ion; IMP:UniProtKB.
DR InterPro; IPR044300; STOP1/2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR46352; PTHR46352; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..373
FT /note="Protein SENSITIVE TO PROTON RHIZOTOXICITY 2"
FT /id="PRO_0000440117"
FT ZN_FING 217..239
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 327..362
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
SQ SEQUENCE 373 AA; 42250 MW; BCAB12CA50053CF2 CRC64;
MHIHMMNRDE HIAKKVEGSI SSFSGETSTS SKQIYVNPVT TTGTKSMEDD DVSLSLLYNL
STLHEKVHQI QSLVSFYMVS TNNINQSSGS TSLAVANIGS LVQEIITAAS SMLYTCQQLQ
IGSNNNNNDI DNDQTVDAMV LEFSRQETDP GHDFVQESTN LFGVQERGQI SFPDQNLDWY
NTETINPKKD KHRSKPSSGS YDILELDVAD LLAKYTHYCQ ICGKGFKRDA NLRMHMRAHG
DEYKTREALI SPTSQDKKGG YSLKKHYYSC PQHGCRWNQR HEKFQPLKSV ICAKNHYKRS
HCPKMYMCRR CSVKHFSVLS DLRTHEKHCG DIKWVCSCGT KFSRKDKLMS HVSLFLGHVP
AHGSSKPPTI TLK
