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 01-MAY-2013, entry version 94.
DE RecName: Full=Protein SENSITIVE TO PROTON RHIZOTOXICITY 1;
DE AltName: Full=Zinc finger protein STOP1;
GN Name=STOP1; OrderedLocusNames=At1g34370; ORFNames=F7P12.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
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.,
RA Kobayashi Y., Ikka T., Hirayama T., Shinozaki K., Kobayashi M.;
RT "Zinc finger protein STOP1 is critical for proton tolerance in
RT Arabidopsis 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.,
RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA 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.,
RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RG The Arabidopsis Information Resource (TAIR);
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA Hayashizaki Y., 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
RT proteins 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
RT ALMT families function independently to confer Arabidopsis aluminum
RT 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
RT and aluminum toxicities.";
RL Plant Physiol. 150:281-294(2009).
CC -!- FUNCTION: Probable transcription factor. Plays a critical role in
CC tolerance to major stress factors in acid soils such as proton
CC H(+) and aluminum ion Al(3+). Required for the expression of genes
CC in response to acidic stress (e.g. ALMT1 and MATE), and Al-
CC activated citrate exudation.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences;
CC Name=1;
CC IsoId=Q9C8N5-1; Sequence=Displayed;
CC -!- INDUCTION: By shock H(+) and Al(3+) treatments.
CC -!- DISRUPTION PHENOTYPE: Hypersensitive to H(+) and Al(3+)
CC rhizotoxicity, reduced induction of genes such as ALMT1 and MATE
CC in response to acidic stress, and impaired Al-activated citrate
CC exudation.
CC -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
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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 IPI; IPI00542277; -.
DR PIR; A86468; A86468.
DR RefSeq; NP_174697.1; NM_103160.4.
DR RefSeq; NP_849746.1; NM_179415.1.
DR UniGene; At.39746; -.
DR UniGene; At.64018; -.
DR UniGene; At.74453; -.
DR ProteinModelPortal; Q9C8N5; -.
DR SMR; Q9C8N5; 243-270, 285-391.
DR IntAct; Q9C8N5; 1.
DR PaxDb; Q9C8N5; -.
DR PRIDE; Q9C8N5; -.
DR EnsemblPlants; AT1G34370.1; AT1G34370.1; AT1G34370.
DR EnsemblPlants; AT1G34370.2; AT1G34370.2; AT1G34370.
DR GeneID; 840339; -.
DR KEGG; ath:AT1G34370; -.
DR TAIR; At1g34370; -.
DR eggNOG; NOG266871; -.
DR HOGENOM; HOG000238514; -.
DR InParanoid; Q9C8N5; -.
DR OMA; KEHKKFQ; -.
DR PhylomeDB; Q9C8N5; -.
DR ProtClustDB; CLSN2679604; -.
DR ArrayExpress; Q9C8N5; -.
DR Genevestigator; Q9C8N5; -.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010447; P:response to acidity; IMP:TAIR.
DR GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 3.30.160.60; -; 1.
DR InterPro; IPR007087; Znf_C2H2.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
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; Complete proteome; Metal-binding; Nucleus;
KW Polymorphism; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 499 Protein SENSITIVE TO PROTON RHIZOTOXICITY
FT 1.
FT /FTId=PRO_0000380136.
FT ZN_FING 244 266 C2H2-type 1.
FT ZN_FING 354 385 C2H2-type 2; atypical.
FT VARIANT 10 10 T -> N (in strain: cv. Est-1).
FT VARIANT 27 27 C -> G (in strain: cv. Est-1).
FT VARIANT 60 60 S -> N (in strain: cv. Est-1).
FT VARIANT 109 109 L -> V (in strain: cv. Est-1).
FT CONFLICT 400 400 T -> R (in Ref. 5; AAM65531).
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
//
