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TOP6A_ARATH
ID   TOP6A_ARATH             Reviewed;         427 AA.
AC   Q9LZ03;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_03164};
DE            Short=AtTOP6A;
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_03164};
DE   AltName: Full=Meiotic recombination protein SPO11-3;
DE            Short=AtSPO11-3;
DE   AltName: Full=Protein BRASSINOSTEROID INSENSITIVE 5;
DE   AltName: Full=Protein ROOT HAIRLESS 2;
GN   Name=TOP6A {ECO:0000255|HAMAP-Rule:MF_03164}; Synonyms=BIN5, RHL2, SPO11-3;
GN   OrderedLocusNames=At5g02820; ORFNames=F9G14.130;
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 [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH TOP6B.
RX   PubMed=11410368; DOI=10.1016/s0378-1119(01)00496-6;
RA   Hartung F., Puchta H.;
RT   "Molecular characterization of homologues of both subunits A (SPO11) and B
RT   of the archaebacterial topoisomerase 6 in plants.";
RL   Gene 271:81-86(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11157765; DOI=10.1093/emboj/20.3.589;
RA   Grelon M., Vezon D., Gendrot G., Pelletier G.;
RT   "AtSPO11-1 is necessary for efficient meiotic recombination in plants.";
RL   EMBO J. 20:589-600(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12401175; DOI=10.1016/s0960-9822(02)01198-3;
RA   Sugimoto-Shirasu K., Stacey N.J., Corsar J., Roberts K., McCann M.C.;
RT   "DNA topoisomerase VI is essential for endoreduplication in Arabidopsis.";
RL   Curr. Biol. 12:1782-1786(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=12119417; DOI=10.1073/pnas.152337599;
RA   Yin Y., Cheong H., Friedrichsen D., Zhao Y., Hu J., Mora-Garcia S.,
RA   Chory J.;
RT   "A crucial role for the putative Arabidopsis topoisomerase VI in plant
RT   growth and development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10191-10196(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   INTERACTION WITH RHL1.
RX   PubMed=16339310; DOI=10.1073/pnas.0505883102;
RA   Sugimoto-Shirasu K., Roberts G.R., Stacey N.J., McCann M.C., Maxwell A.,
RA   Roberts K.;
RT   "RHL1 is an essential component of the plant DNA topoisomerase VI complex
RT   and is required for ploidy-dependent cell growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18736-18741(2005).
RN   [9]
RP   INTERACTION WITH BIN4.
RX   PubMed=18055605; DOI=10.1105/tpc.107.054833;
RA   Breuer C., Stacey N.J., West C.E., Zhao Y., Chory J., Tsukaya H., Azumi Y.,
RA   Maxwell A., Roberts K., Sugimoto-Shirasu K.;
RT   "BIN4, a novel component of the plant DNA topoisomerase VI complex, is
RT   required for endoreduplication in Arabidopsis.";
RL   Plant Cell 19:3655-3668(2007).
RN   [10]
RP   INTERACTION WITH RHL1.
RX   PubMed=17951446; DOI=10.1105/tpc.107.054361;
RA   Kirik V., Schrader A., Uhrig J.F., Hulskamp M.;
RT   "MIDGET unravels functions of the Arabidopsis topoisomerase VI complex in
RT   DNA endoreduplication, chromatin condensation, and transcriptional
RT   silencing.";
RL   Plant Cell 19:3100-3110(2007).
CC   -!- FUNCTION: Component of the DNA topoisomerase VI involved in chromatin
CC       organization and progression of endoreduplication cycles. Relaxes both
CC       positive and negative superturns and exhibits a strong decatenase
CC       activity. Involved in cell-elongation processes. {ECO:0000255|HAMAP-
CC       Rule:MF_03164, ECO:0000269|PubMed:12119417,
CC       ECO:0000269|PubMed:12401175}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03164};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03164};
CC   -!- SUBUNIT: Homodimer. Heterotetramer of two TOP6A and two TOP6B subunits.
CC       Interacts with BIN4 and RHL1. {ECO:0000255|HAMAP-Rule:MF_03164,
CC       ECO:0000269|PubMed:11410368, ECO:0000269|PubMed:16339310,
CC       ECO:0000269|PubMed:17951446, ECO:0000269|PubMed:18055605}.
CC   -!- INTERACTION:
CC       Q9LZ03; Q5Q0E6: MTOPVIB; NbExp=4; IntAct=EBI-1772104, EBI-16200362;
CC       Q9LZ03; O81242: RHL1; NbExp=2; IntAct=EBI-1772104, EBI-1772159;
CC       Q9LZ03; Q9LZ03: TOP6A; NbExp=3; IntAct=EBI-1772104, EBI-1772104;
CC       Q9LZ03; Q9C5V6: TOP6B; NbExp=7; IntAct=EBI-1772104, EBI-1772132;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03164}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems, flowers and
CC       seedlings. {ECO:0000269|PubMed:11410368}.
CC   -!- DISRUPTION PHENOTYPE: Plants are defective in cell elongation and show
CC       a severe dwarf phenotype. {ECO:0000269|PubMed:12401175}.
CC   -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP-
CC       Rule:MF_03164}.
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DR   EMBL; AJ297842; CAC24689.1; -; mRNA.
DR   EMBL; AF323679; AAL01152.1; -; mRNA.
DR   EMBL; AL162973; CAB86036.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90522.1; -; Genomic_DNA.
DR   EMBL; BT028966; ABI54341.1; -; mRNA.
DR   PIR; T48303; T48303.
DR   RefSeq; NP_195902.1; NM_120360.4.
DR   AlphaFoldDB; Q9LZ03; -.
DR   SMR; Q9LZ03; -.
DR   BioGRID; 16591; 1.
DR   DIP; DIP-40169N; -.
DR   IntAct; Q9LZ03; 3.
DR   STRING; 3702.AT5G02820.1; -.
DR   PaxDb; Q9LZ03; -.
DR   PRIDE; Q9LZ03; -.
DR   ProteomicsDB; 232433; -.
DR   EnsemblPlants; AT5G02820.1; AT5G02820.1; AT5G02820.
DR   GeneID; 831314; -.
DR   Gramene; AT5G02820.1; AT5G02820.1; AT5G02820.
DR   KEGG; ath:AT5G02820; -.
DR   Araport; AT5G02820; -.
DR   TAIR; locus:2151221; AT5G02820.
DR   eggNOG; KOG2795; Eukaryota.
DR   HOGENOM; CLU_037229_1_0_1; -.
DR   InParanoid; Q9LZ03; -.
DR   OMA; NWGEARF; -.
DR   OrthoDB; 1272299at2759; -.
DR   PhylomeDB; Q9LZ03; -.
DR   PRO; PR:Q9LZ03; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LZ03; baseline and differential.
DR   Genevisible; Q9LZ03; AT.
DR   GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; TAS:TAIR.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0009957; P:epidermal cell fate specification; IMP:TAIR.
DR   GO; GO:0042138; P:meiotic DNA double-strand break formation; IBA:GO_Central.
DR   GO; GO:0000706; P:meiotic DNA double-strand break processing; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IBA:GO_Central.
DR   CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00132; Top6A; 1.
DR   InterPro; IPR002815; Spo11/TopoVI_A.
DR   InterPro; IPR013049; Spo11/TopoVI_A_N.
DR   InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR   InterPro; IPR004085; TopoVI_A.
DR   InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10848; PTHR10848; 1.
DR   Pfam; PF04406; TP6A_N; 1.
DR   PRINTS; PR01550; TOP6AFAMILY.
DR   PRINTS; PR01552; TPISMRASE6A.
DR   SUPFAM; SSF56726; SSF56726; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isomerase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Topoisomerase.
FT   CHAIN           1..427
FT                   /note="DNA topoisomerase 6 subunit A"
FT                   /id="PRO_0000346109"
FT   ACT_SITE        170
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03164"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03164"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03164"
SQ   SEQUENCE   427 AA;  47446 MW;  0EA41B8B4BA77441 CRC64;
     MADKKKRKRS KDDEAEELPF KSILESDDVI TELLKSYISS SIKAAAGAGG ASSSSSKPLT
     LADLSLSSSC REVADLSLSS VQTEIETVIV QIARSILAGD GFSFSVPSRA ASNQLYVPEL
     DRIVLKDKST LRPFASVSSV RKTTITTRIL ALIHQLCLRN IHVTKRDLFY TDVKLFQDQT
     QSDAVLDDVS CMLGCTRSSL NVIAAEKGVV VGRLIFSDNG DMIDCTKMGM GGKAIPPNID
     RVGDMQSDAM FILLVEKDAA YMRLAEDRFY NRFPCIIVTA KGQPDVATRL FLRKMKMELK
     LPVLALVDSD PYGLKILSVY GCGSKNMSYD SANLTTPDIK WLGIRPSDLD KYKIPEQCRL
     PMTEQDIKTG KDMLEEDFVK KNPGWVEELN LMVKTKQKAE IQALSSFGFQ YLSEVYLPLK
     LQQQDWL
 
 
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