AUR3_ARATH
ID AUR3_ARATH Reviewed; 288 AA.
AC O64629;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/threonine-protein kinase Aurora-3;
DE Short=AtAur3;
DE EC=2.7.11.1;
DE AltName: Full=Aurora-like kinase 3;
GN Name=AUR3; OrderedLocusNames=At2g45490; ORFNames=F17K2.2;
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, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=16028112; DOI=10.1007/s11103-005-3454-x;
RA Kawabe A., Matsunaga S., Nakagawa K., Kurihara D., Yoneda A., Hasezawa S.,
RA Uchiyama S., Fukui K.;
RT "Characterization of plant Aurora kinases during mitosis.";
RL Plant Mol. Biol. 58:1-13(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15722465; DOI=10.1105/tpc.104.029710;
RA Demidov D., Van Damme D., Geelen D., Blattner F.R., Houben A.;
RT "Identification and dynamics of two classes of aurora-like kinases in
RT Arabidopsis and other plants.";
RL Plant Cell 17:836-848(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [7]
RP FUNCTION, AND INHIBITION BY HESPERADIN.
RX PubMed=17087760; DOI=10.1111/j.1365-313x.2006.02893.x;
RA Kurihara D., Matsunaga S., Kawabe A., Fujimoto S., Noda M., Uchiyama S.,
RA Fukui K.;
RT "Aurora kinase is required for chromosome segregation in tobacco BY-2
RT cells.";
RL Plant J. 48:572-580(2006).
CC -!- FUNCTION: Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and
CC 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph).
CC Colocalizes with phosphorylated histone H3 during mitosis. Associates
CC with cytoskeletal structures that are necessary for cytokinesis and
CC with the microtubule spindle. {ECO:0000269|PubMed:16028112,
CC ECO:0000269|PubMed:17087760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Inhibited by hesperadin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
CC Chromosome. Chromosome, centromere. Note=Cytoplasmic perinuclear region
CC or in dots around the nucleolus and at the nuclear periphery in
CC interphase cells, associated to centromeric regions of condensed
CC chromosomes at metaphase and dispersed along the entire length of the
CC chromosomes during anaphase (PubMed:16028112). Nucleus
CC (PubMed:15722465). {ECO:0000269|PubMed:15722465,
CC ECO:0000269|PubMed:16028112}.
CC -!- TISSUE SPECIFICITY: Abundant in roots, flowers and flower buds, low or
CC absent in expanded leaves, stems and siliques.
CC {ECO:0000269|PubMed:15722465}.
CC -!- INDUCTION: Expression peaks at mitosis. {ECO:0000269|PubMed:15722465}.
CC -!- PTM: Phosphorylation at Thr-176 may regulate activity and degradation
CC of AUR3 in a cell cycle dependent manner. {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression of AUR3 induces mitotic spindle defects,
CC but the distribution of phosphorylation of histone H3 on the chromosome
CC is not affected.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. Aurora subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; AB196735; BAE00021.1; -; Genomic_DNA.
DR EMBL; AJ854185; CAH69534.1; -; mRNA.
DR EMBL; AC003680; AAC06151.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10561.1; -; Genomic_DNA.
DR EMBL; AY074653; AAL69469.1; -; mRNA.
DR PIR; T00862; T00862.
DR RefSeq; NP_182073.1; NM_130111.4.
DR AlphaFoldDB; O64629; -.
DR SMR; O64629; -.
DR STRING; 3702.AT2G45490.1; -.
DR PaxDb; O64629; -.
DR PRIDE; O64629; -.
DR ProteomicsDB; 241106; -.
DR EnsemblPlants; AT2G45490.1; AT2G45490.1; AT2G45490.
DR GeneID; 819157; -.
DR Gramene; AT2G45490.1; AT2G45490.1; AT2G45490.
DR KEGG; ath:AT2G45490; -.
DR Araport; AT2G45490; -.
DR TAIR; locus:2043624; AT2G45490.
DR eggNOG; KOG0580; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; O64629; -.
DR OMA; PYGRQTT; -.
DR OrthoDB; 954262at2759; -.
DR PhylomeDB; O64629; -.
DR PRO; PR:O64629; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64629; baseline and differential.
DR Genevisible; O64629; AT.
DR GO; GO:0032133; C:chromosome passenger complex; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); IDA:TAIR.
DR GO; GO:0044022; F:histone kinase activity (H3-S28 specific); IDA:TAIR.
DR GO; GO:0035174; F:histone serine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007059; P:chromosome segregation; IEA:InterPro.
DR GO; GO:0043987; P:histone H3-S10 phosphorylation; IDA:TAIR.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; IDA:TAIR.
DR GO; GO:0016572; P:histone phosphorylation; IDA:TAIR.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IPI:TAIR.
DR GO; GO:0032465; P:regulation of cytokinesis; IBA:GO_Central.
DR InterPro; IPR030616; Aur.
DR InterPro; IPR030614; AUR3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24350; PTHR24350; 1.
DR PANTHER; PTHR24350:SF29; PTHR24350:SF29; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Centromere; Chromosome; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..288
FT /note="Serine/threonine-protein kinase Aurora-3"
FT /id="PRO_0000270794"
FT DOMAIN 22..273
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q93V58"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q38997"
SQ SEQUENCE 288 AA; 33119 MW; BFB41F3E34795BD8 CRC64;
MSKKSTESDA GNTEKQWSLA DFEIGRPLGK GKFGRVYLAR EAKSKYIVAL KVIFKEQIEK
YKIHHQLRRE MEIQTSLRHP NILRLFGWFH DNERIFLILE YAHGGELYGV LKQNGHLTEQ
QAATYIASLS QALAYCHGKC VIHRDIKPEN LLLDHEGRLK IADFGWSVQS SNKRKTMCGT
LDYLAPEMVE NRDHDYAVDN WTLGILCYEF LYGNPPFEAE SQKDTFKRIL KIDLSFPLTP
NVSEEAKNLI SQLLVKDPSK RLSIEKIMQH PWIVKNADPK GVCASIDI
