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Database: UniProt
Entry: Q9C8N5
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Original site: Q9C8N5 
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   29-OCT-2014, entry version 106.
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; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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. {ECO:0000269|PubMed:17535918,
CC       ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:19321711}.
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.;
CC       Name=1;
CC         IsoId=Q9C8N5-1; Sequence=Displayed;
CC   -!- INDUCTION: By shock H(+) and Al(3+) treatments.
CC       {ECO:0000269|PubMed:17535918}.
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. {ECO:0000269|PubMed:17535918,
CC       ECO:0000269|PubMed:18826429, ECO:0000269|PubMed:19321711}.
CC   -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
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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_103160.4. [Q9C8N5-1]
DR   RefSeq; NP_849746.1; NM_179415.1. [Q9C8N5-1]
DR   UniGene; At.39746; -.
DR   UniGene; At.64018; -.
DR   UniGene; At.74453; -.
DR   ProteinModelPortal; Q9C8N5; -.
DR   SMR; Q9C8N5; 239-272, 286-366.
DR   BioGrid; 25571; 1.
DR   IntAct; Q9C8N5; 1.
DR   PaxDb; Q9C8N5; -.
DR   PRIDE; Q9C8N5; -.
DR   EnsemblPlants; AT1G34370.1; AT1G34370.1; AT1G34370. [Q9C8N5-1]
DR   EnsemblPlants; AT1G34370.2; AT1G34370.2; AT1G34370. [Q9C8N5-1]
DR   GeneID; 840339; -.
DR   KEGG; ath:AT1G34370; -.
DR   TAIR; AT1G34370; -.
DR   eggNOG; NOG266871; -.
DR   HOGENOM; HOG000238514; -.
DR   InParanoid; Q9C8N5; -.
DR   OMA; RICFEES; -.
DR   PhylomeDB; Q9C8N5; -.
DR   ExpressionAtlas; Q9C8N5; baseline and differential.
DR   Genevestigator; Q9C8N5; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR   GO; GO:0010447; P:response to acidic pH; IMP:TAIR.
DR   GO; GO:0010044; P:response to aluminum ion; IMP:TAIR.
DR   GO; GO:0006351; P:transcription, DNA-templated; 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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     354    385       C2H2-type 2; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00042}.
FT   VARIANT      10     10       T -> N (in strain: cv. Est-1).
FT                                {ECO:0000269|PubMed:17535918}.
FT   VARIANT      27     27       C -> G (in strain: cv. Est-1).
FT                                {ECO:0000269|PubMed:17535918}.
FT   VARIANT      60     60       S -> N (in strain: cv. Est-1).
FT                                {ECO:0000269|PubMed:17535918}.
FT   VARIANT     109    109       L -> V (in strain: cv. Est-1).
FT                                {ECO:0000269|PubMed:17535918}.
FT   CONFLICT    400    400       T -> R (in Ref. 5; AAM65531).
FT                                {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
//
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