TPX2_ARATH
ID TPX2_ARATH Reviewed; 790 AA.
AC F4I2H7; F4I2H9; Q3EDJ2; Q56XS5; Q9ZWA0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protein TPX2;
DE Short=AtTPX2;
DE AltName: Full=Targeting protein for XKLP2;
GN Name=TPX2; OrderedLocusNames=At1g03780; ORFNames=F11M21.29;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP 231-LYS-ARG-232; LEU-500; LEU-506; 673-LYS-ARG-674 AND 733-LYS-ARG-734,
RP DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=18941054; DOI=10.1105/tpc.107.056796;
RA Vos J.W., Pieuchot L., Evrard J.L., Janski N., Bergdoll M., de Ronde D.,
RA Perez L.H., Sardon T., Vernos I., Schmit A.C.;
RT "The plant TPX2 protein regulates prospindle assembly before nuclear
RT envelope breakdown.";
RL Plant Cell 20:2783-2797(2008).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AUR1.
RX PubMed=22150830; DOI=10.1111/j.1469-8137.2011.03989.x;
RA Petrovska B., Cenklova V., Pochylova Z., Kourova H., Doskocilova A.,
RA Plihal O., Binarova L., Binarova P.;
RT "Plant Aurora kinases play a role in maintenance of primary meristems and
RT control of endoreduplication.";
RL New Phytol. 193:590-604(2012).
RN [6]
RP FUNCTION.
RX PubMed=24006426; DOI=10.1093/jxb/ert271;
RA Petrovska B., Jerabkova H., Kohoutova L., Cenklova V., Pochylova Z.,
RA Gelova Z., Kocarova G., Vachova L., Kurejova M., Tomastikova E.,
RA Binarova P.;
RT "Overexpressed TPX2 causes ectopic formation of microtubular arrays in the
RT nuclei of acentrosomal plant cells.";
RL J. Exp. Bot. 64:4575-4587(2013).
CC -!- FUNCTION: Regulates prospindle assembly during late prophase and at the
CC onset of mitosis, before nuclear envelope breakdown (NEB). Is exported
CC from the nucleus shortly before NEB and organized into two polar
CC crescents. After NEB, is progressively associated with the forming
CC spindle. Probably mediates AUR1 activation and localization to spindle
CC microtubules. Has a microtubule binding capability and is able to
CC trigger microtubule assembly induced by RanGTP in a heterologous
CC system. Not involved in phragmoplast assembly, nuclear envelope
CC reformation, and cortical microtubule assembly at the onset of G1
CC (PubMed:18941054). Involved in the formation of specific nuclear and
CC perinuclear microtubular arrays in the nuclei of acentrosomal plant
CC cells. Fungi and plants have acentrosomal microtubule arrays because
CC they lack centrosomes. They use other microtubule organizing center
CC (MTOC) structures to organize their microtubules. May function through
CC interaction with importin (PubMed:24006426).
CC {ECO:0000269|PubMed:18941054, ECO:0000269|PubMed:24006426}.
CC -!- SUBUNIT: Interacts with AUR1. {ECO:0000269|PubMed:22150830}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Located in the
CC nucleoplasm during interphase until late G2, in the perinuclear region
CC during early prophase, and at the spindle during mitosis. Localized on
CC a specific subset of phragmoplast microtubules in early telophase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4I2H7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4I2H7-2; Sequence=VSP_044615, VSP_044616;
CC Name=3;
CC IsoId=F4I2H7-3; Sequence=VSP_044609, VSP_044610, VSP_044611,
CC VSP_044612, VSP_044613, VSP_044614;
CC -!- DOMAIN: The N-terminal part of the protein is required for the
CC interaction with AUR1. Two regions (220-463 and 684-758) seem involved
CC in the targeting to the microtubule cytoskeleton.
CC {ECO:0000269|PubMed:18941054}.
CC -!- DISRUPTION PHENOTYPE: Lethal when homozygous.
CC {ECO:0000269|PubMed:18941054}.
CC -!- MISCELLANEOUS: TPX2 over-expressing cells display formation of nuclear
CC and perinuclear microtubular arrays which are not specific for the
CC transition to mitosis and occur independently of AUR1 kinase.
CC {ECO:0000269|PubMed:24006426}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10690.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003027; AAD10690.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27611.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27612.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27613.1; -; Genomic_DNA.
DR EMBL; AK221598; BAD95139.1; -; mRNA.
DR PIR; C86168; C86168.
DR RefSeq; NP_001184902.1; NM_001197973.1. [F4I2H7-1]
DR RefSeq; NP_171874.3; NM_100257.3. [F4I2H7-3]
DR RefSeq; NP_973754.2; NM_202025.3. [F4I2H7-2]
DR AlphaFoldDB; F4I2H7; -.
DR SMR; F4I2H7; -.
DR BioGRID; 24377; 1.
DR STRING; 3702.AT1G03780.3; -.
DR PaxDb; F4I2H7; -.
DR PRIDE; F4I2H7; -.
DR ProteomicsDB; 232506; -. [F4I2H7-1]
DR EnsemblPlants; AT1G03780.1; AT1G03780.1; AT1G03780. [F4I2H7-3]
DR EnsemblPlants; AT1G03780.2; AT1G03780.2; AT1G03780. [F4I2H7-2]
DR EnsemblPlants; AT1G03780.3; AT1G03780.3; AT1G03780. [F4I2H7-1]
DR GeneID; 839140; -.
DR Gramene; AT1G03780.1; AT1G03780.1; AT1G03780. [F4I2H7-3]
DR Gramene; AT1G03780.2; AT1G03780.2; AT1G03780. [F4I2H7-2]
DR Gramene; AT1G03780.3; AT1G03780.3; AT1G03780. [F4I2H7-1]
DR KEGG; ath:AT1G03780; -.
DR Araport; AT1G03780; -.
DR TAIR; locus:2024132; AT1G03780.
DR eggNOG; ENOG502QVQS; Eukaryota.
DR InParanoid; F4I2H7; -.
DR OMA; SEFDNMV; -.
DR OrthoDB; 1390734at2759; -.
DR PRO; PR:F4I2H7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I2H7; baseline and differential.
DR Genevisible; F4I2H7; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005880; C:nuclear microtubule; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IMP:UniProtKB.
DR GO; GO:0005819; C:spindle; IMP:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:TAIR.
DR InterPro; IPR027329; TPX2_C.
DR InterPro; IPR027330; TPX2_central_dom.
DR InterPro; IPR009675; TPX2_fam.
DR PANTHER; PTHR14326; PTHR14326; 1.
DR Pfam; PF06886; TPX2; 1.
DR Pfam; PF12214; TPX2_importin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..790
FT /note="Protein TPX2"
FT /id="PRO_0000420703"
FT REGION 101..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..619
FT /evidence="ECO:0000255"
FT COILED 656..698
FT /evidence="ECO:0000255"
FT COMPBIAS 118..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 362..382
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044609"
FT VAR_SEQ 506..532
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044610"
FT VAR_SEQ 572
FT /note="V -> VKREMVLINLTCSNSQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044611"
FT VAR_SEQ 664
FT /note="K -> KVSILFSHFSKQKNASITSEIDESILFWNQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044612"
FT VAR_SEQ 686..691
FT /note="EEERAL -> CNISNA (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044613"
FT VAR_SEQ 692..790
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_044614"
FT VAR_SEQ 755..758
FT /note="VHCL -> GQMR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044615"
FT VAR_SEQ 759..790
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044616"
FT MUTAGEN 231..232
FT /note="KR->NG: Loss of nuclear targeting."
FT /evidence="ECO:0000269|PubMed:18941054"
FT MUTAGEN 500
FT /note="L->S: Loss of export from the nucleus; when
FT associated with H-506."
FT /evidence="ECO:0000269|PubMed:18941054"
FT MUTAGEN 506
FT /note="L->H: Loss of export from the nucleus; when
FT associated with S-500."
FT /evidence="ECO:0000269|PubMed:18941054"
FT MUTAGEN 673..674
FT /note="KR->NG: Loss of nuclear targeting."
FT /evidence="ECO:0000269|PubMed:18941054"
FT MUTAGEN 733..734
FT /note="KR->NG: No effect on nuclear targeting."
FT /evidence="ECO:0000269|PubMed:18941054"
SQ SEQUENCE 790 AA; 90083 MW; 11BDAD2288B217DA CRC64;
MEATAEESVS TLVTTMVDET YEFLAPRWFD FVNGETEDES RRAELWFQSA LSCAPSPSVP
RIKARRSFKV EAMCNFNEAE EETLKDKEPL EPVVPIVSLQ SQPSQAKKAE VAPSKASTVK
PSRISSKDAE VNNKTVDASD PTTEPIEDKE NIAPACTPKP PMQFSLGAKS VDLKKQQTAR
KIASLLKNPS TLRPKNQSQA KGSHQKSVKG ETNLNNIAST TNLIQENQAI KRQKLDDGKS
RQILNPKPAT LLHKTRNGLV NTGFNLCPSV TKHTPKENRK VYVREQIAPF VSTAELMKKF
QTSTRDLFVQ NRPKLTLTRP KEPEFVTSQR ARPLRVKSSA ELEEEMLAKI PKFKARPVNK
KILAAPALPA PQRSTPHLPE FQEFHLQTMA RANQHAETSS IASTEVSKQH NDQKHHLTEP
KSPVLQTMLR ARPTIAKTTA ELEQEELEKA PKFKAKPLNK KIFESKGEMG IFCNTKKHIT
IPQEFHFATD ERISRPESVL DIFDKLSLNS ESCHEKPLPR NTAPNPFNLK TEERGAEKEK
KFYMELMYKK LGDVKARVPK ANPYPYTTDY PVVPPKPEPK QCTQPEPFQL ESLVRHEEEM
RREREERRRM ETEEAQKRLF KAQPVIKEDP IPVPEKVRMP LTEIQEFNLH VEHRAVERAD
FDHKIKEKEN QYKRYREESE AAKMVEEERA LKQMRKTMVP HARPVPNFNK PFLPQKSNKG
TTKAKSPNLR VIKRTERRTM MARPTISAAT SASAVHCLMY PGSSFNKLKK KTVLTNIVHC
LMYPDSSLLN
