STOP1_ARATH
ID STOP1_ARATH Reviewed; 499 AA.
AC Q9C8N5; A5A8C1; Q8LA79;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 154.
DE RecName: Full=Protein SENSITIVE TO PROTON RHIZOTOXICITY 1 {ECO:0000303|PubMed:17535918};
DE AltName: Full=Zinc finger protein STOP1 {ECO:0000303|PubMed:17535918};
GN Name=STOP1 {ECO:0000303|PubMed:17535918};
GN OrderedLocusNames=At1g34370 {ECO:0000312|Araport:AT1G34370};
GN ORFNames=F7P12.7 {ECO:0000312|EMBL:AAG51898.1};
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 [GENOMIC DNA], FUNCTION, VARIANTS ASN-10; GLY-27;
RP ASN-60 AND VAL-109, INDUCTION BY SHOCK ACID TREATMENTS, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Col-4, cv. Est-1, cv. Fr-3, cv. Goe-0, cv. Kb-0, cv. Kl-5,
RC cv. Landsberg erecta, cv. Li-1, cv. Lo-1, cv. Pi-0, cv. Tu-0, and
RC cv. Van-3;
RX PubMed=17535918; DOI=10.1073/pnas.0700117104;
RA Iuchi S., Koyama H., Iuchi A., Kobayashi Y., Kitabayashi S., Kobayashi Y.,
RA Ikka T., Hirayama T., Shinozaki K., Kobayashi M.;
RT "Zinc finger protein STOP1 is critical for proton tolerance in Arabidopsis
RT and coregulates a key gene in aluminum tolerance.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9900-9905(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=15236668; DOI=10.1186/1471-2164-5-39;
RA Englbrecht C.C., Schoof H., Boehm S.;
RT "Conservation, diversification and expansion of C2H2 zinc finger proteins
RT in the Arabidopsis thaliana genome.";
RL BMC Genomics 5:39-39(2004).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18826429; DOI=10.1111/j.1365-313x.2008.03696.x;
RA Liu J., Magalhaes J.V., Shaff J., Kochian L.V.;
RT "Aluminum-activated citrate and malate transporters from the MATE and ALMT
RT families function independently to confer Arabidopsis aluminum tolerance.";
RL Plant J. 57:389-399(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19321711; DOI=10.1104/pp.108.134700;
RA Sawaki Y., Iuchi S., Kobayashi Y., Kobayashi Y., Ikka T., Sakurai N.,
RA Fujita M., Shinozaki K., Shibata D., Kobayashi M., Koyama H.;
RT "STOP1 regulates multiple genes that protect arabidopsis from proton and
RT aluminum toxicities.";
RL Plant Physiol. 150:281-294(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, 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 STOP2, 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:17535918,
CC ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:19321711,
CC ECO:0000269|PubMed:23935008}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19321711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000312|Araport:AT1G34370};
CC Name=1;
CC IsoId=Q9C8N5-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots (e.g. root tips and lateral
CC roots), leaves, flowers (e.g. stigma, sepal, anther, and filament),
CC stems, siliques and cotyledons. {ECO:0000269|PubMed:23935008}.
CC -!- INDUCTION: By shock H(+) and Al(3+) treatments.
CC {ECO:0000269|PubMed:17535918}.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to H(+) and Al(3+) rhizotoxicity,
CC reduced induction of genes such as ALMT1 and MATE in response to acidic
CC stress, and impaired Al-activated citrate exudation.
CC {ECO:0000269|PubMed:17535918, ECO:0000269|PubMed:18826429,
CC ECO:0000269|PubMed:19321711, ECO:0000269|PubMed:23935008}.
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DR EMBL; AB300236; BAF62148.1; -; Genomic_DNA.
DR EMBL; AB300237; BAF62149.1; -; Genomic_DNA.
DR EMBL; AB300238; BAF62150.1; -; Genomic_DNA.
DR EMBL; AB300239; BAF62151.1; -; Genomic_DNA.
DR EMBL; AB300240; BAF62152.1; -; Genomic_DNA.
DR EMBL; AB300241; BAF62153.1; -; Genomic_DNA.
DR EMBL; AB300242; BAF62154.1; -; Genomic_DNA.
DR EMBL; AB300243; BAG16782.1; -; Genomic_DNA.
DR EMBL; AB300244; BAF62155.1; -; Genomic_DNA.
DR EMBL; AB300245; BAF62156.1; -; Genomic_DNA.
DR EMBL; AB300246; BAF62157.1; -; Genomic_DNA.
DR EMBL; AB300247; BAF62158.1; -; Genomic_DNA.
DR EMBL; AC023913; AAG51898.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31703.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31704.1; -; Genomic_DNA.
DR EMBL; AK227128; BAE99177.1; -; mRNA.
DR EMBL; AY087985; AAM65531.1; -; mRNA.
DR PIR; A86468; A86468.
DR RefSeq; NP_174697.1; NM_103160.5. [Q9C8N5-1]
DR RefSeq; NP_849746.1; NM_179415.1. [Q9C8N5-1]
DR AlphaFoldDB; Q9C8N5; -.
DR BioGRID; 25571; 3.
DR IntAct; Q9C8N5; 1.
DR STRING; 3702.AT1G34370.2; -.
DR MetOSite; Q9C8N5; -.
DR PaxDb; Q9C8N5; -.
DR PRIDE; Q9C8N5; -.
DR ProteomicsDB; 228424; -. [Q9C8N5-1]
DR EnsemblPlants; AT1G34370.1; AT1G34370.1; AT1G34370. [Q9C8N5-1]
DR EnsemblPlants; AT1G34370.2; AT1G34370.2; AT1G34370. [Q9C8N5-1]
DR GeneID; 840339; -.
DR Gramene; AT1G34370.1; AT1G34370.1; AT1G34370. [Q9C8N5-1]
DR Gramene; AT1G34370.2; AT1G34370.2; AT1G34370. [Q9C8N5-1]
DR KEGG; ath:AT1G34370; -.
DR Araport; AT1G34370; -.
DR TAIR; locus:2036303; AT1G34370.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q9C8N5; -.
DR OMA; KHNMSTA; -.
DR PhylomeDB; Q9C8N5; -.
DR PRO; PR:Q9C8N5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8N5; baseline and differential.
DR Genevisible; Q9C8N5; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0071453; P:cellular response to oxygen levels; IMP:TAIR.
DR GO; GO:0071472; P:cellular response to salt stress; IGI:TAIR.
DR GO; GO:1900037; P:regulation of cellular response to hypoxia; IMP:TAIR.
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; 2.
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 2: Evidence at transcript level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..499
FT /note="Protein SENSITIVE TO PROTON RHIZOTOXICITY 1"
FT /id="PRO_0000380136"
FT ZN_FING 244..266
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..385
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 10
FT /note="T -> N (in strain: cv. Est-1)"
FT /evidence="ECO:0000269|PubMed:17535918"
FT VARIANT 27
FT /note="C -> G (in strain: cv. Est-1)"
FT /evidence="ECO:0000269|PubMed:17535918"
FT VARIANT 60
FT /note="S -> N (in strain: cv. Est-1)"
FT /evidence="ECO:0000269|PubMed:17535918"
FT VARIANT 109
FT /note="L -> V (in strain: cv. Est-1)"
FT /evidence="ECO:0000269|PubMed:17535918"
FT CONFLICT 400
FT /note="T -> R (in Ref. 5; AAM65531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 55207 MW; A997994F205740C5 CRC64;
METEDDLCNT NWGSSSSKSR EPGSSDCGNS TFAGFTSQQK WEDASILDYE MGVEPGLQES
IQANVDFLQG VRAQAWDPRT MLSNLSFMEQ KIHQLQDLVH LLVGRGGQLQ GRQDELAAQQ
QQLITTDLTS IIIQLISTAG SLLPSVKHNM STAPGPFTGQ PGSAVFPYVR EANNVASQSQ
NNNNCGAREF DLPKPVLVDE REGHVVEEHE MKDEDDVEEG ENLPPGSYEI LQLEKEEILA
PHTHFCTICG KGFKRDANLR MHMRGHGDEY KTAAALAKPN KESVPGSEPM LIKRYSCPFL
GCKRNKEHKK FQPLKTILCV KNHYKRTHCD KSFTCSRCHT KKFSVIADLK THEKHCGKNK
WLCSCGTTFS RKDKLFGHIA LFQGHTPAIP LEETKPSAST STQRGSSEGG NNNQGMVGFN
LGSASNANQE TTQPGMTDGR ICFEESFSPM NFDTCNFGGF HEFPRLMFDD SESSFQMLIA
NACGFSPRNV GESVSDTSL
