MDP60_ARATH
ID MDP60_ARATH Reviewed; 488 AA.
AC Q5XVC4; A0A178VFR0; Q9C7U3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Microtubule-destabilizing protein 60 {ECO:0000303|PubMed:29167353, ECO:0000303|PubMed:31638649};
GN Name=MDP60 {ECO:0000303|PubMed:29167353, ECO:0000303|PubMed:31638649};
GN OrderedLocusNames=At3g01015 {ECO:0000312|Araport:AT3G01015};
GN ORFNames=EL3N.1 {ECO:0000312|EMBL:AAG51320.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY ETHYLENE AND LIGHT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=29167353; DOI=10.1104/pp.17.01109;
RA Ma Q., Wang X., Sun J., Mao T.;
RT "Coordinated regulation of hypocotyl cell elongation by light and ethylene
RT through a microtubule destabilizing protein.";
RL Plant Physiol. 176:678-690(2018).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SUBMERGENCE AND ETHYLENE.
RC STRAIN=cv. Columbia, cv. En-2, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=31638649; DOI=10.1093/jxb/erz453;
RA Wang X., Ma Q., Wang R., Wang P., Liu Y., Mao T.;
RT "Submergence stress-induced hypocotyl elongation through ethylene
RT signaling-mediated regulation of cortical microtubules in Arabidopsis.";
RL J. Exp. Bot. 71:1067-1077(2020).
CC -!- FUNCTION: Binds directly to microtubules (PubMed:29167353).
CC Microtubule-destabilizing protein involved in the PIF3-dependent
CC positive regulation of hypocotyl cell elongation via the modulation of
CC cortical microtubules dynamic in response to light and ethylene
CC signaling (PubMed:29167353, PubMed:31638649). Promotes submergence-
CC induced and ethylene-dependent underwater hypocotyl elongation
CC (PubMed:31638649). {ECO:0000269|PubMed:29167353,
CC ECO:0000269|PubMed:31638649}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:29167353}. Note=Associated with microtubules.
CC {ECO:0000269|PubMed:29167353}.
CC -!- INDUCTION: Induced by ethylene (ACC) via PIF3 binding to its promoter
CC and subsequent transcription regulation (PubMed:29167353). Accumulates
CC upon submergence through ethylene signaling (PubMed:31638649).
CC Repressed by aminoethoxyvinyl-Gly (AVG), an inhibitor of ethylene
CC biosynthesis (PubMed:29167353, PubMed:31638649). Higher levels in
CC light-grown hypocotyls (PubMed:29167353). {ECO:0000269|PubMed:29167353,
CC ECO:0000269|PubMed:31638649}.
CC -!- DISRUPTION PHENOTYPE: Reduced hypocotyls length in light conditions and
CC in response to ethylene due to reduced cell elongation and associated
CC with the disruption of cortical microtubules (PubMed:29167353).
CC Suppressed effects of submergence on hypocotyl elongation and cortical
CC microtubule reorganization (PubMed:31638649).
CC {ECO:0000269|PubMed:29167353, ECO:0000269|PubMed:31638649}.
CC -!- SIMILARITY: Belongs to the TPX2 family. {ECO:0000305}.
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DR EMBL; AC067753; AAG51320.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73594.1; -; Genomic_DNA.
DR EMBL; AY735598; AAU44468.1; -; mRNA.
DR EMBL; DQ056582; AAY78731.1; -; mRNA.
DR RefSeq; NP_186749.2; NM_110965.4.
DR AlphaFoldDB; Q5XVC4; -.
DR SMR; Q5XVC4; -.
DR STRING; 3702.AT3G01015.1; -.
DR PaxDb; Q5XVC4; -.
DR PRIDE; Q5XVC4; -.
DR ProteomicsDB; 175096; -.
DR EnsemblPlants; AT3G01015.1; AT3G01015.1; AT3G01015.
DR GeneID; 821318; -.
DR Gramene; AT3G01015.1; AT3G01015.1; AT3G01015.
DR KEGG; ath:AT3G01015; -.
DR Araport; AT3G01015; -.
DR TAIR; locus:2831117; AT3G01015.
DR eggNOG; ENOG502QWA1; Eukaryota.
DR HOGENOM; CLU_042597_0_0_1; -.
DR InParanoid; Q5XVC4; -.
DR OMA; YIEQYKM; -.
DR OrthoDB; 1167097at2759; -.
DR PhylomeDB; Q5XVC4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q5XVC4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005880; C:nuclear microtubule; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IMP:TAIR.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IEA:InterPro.
DR GO; GO:1905421; P:regulation of plant organ morphogenesis; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR GO; GO:1990785; P:response to water-immersion restraint stress; IMP:UniProtKB.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB.
DR InterPro; IPR027329; TPX2_C.
DR InterPro; IPR009675; TPX2_fam.
DR PANTHER; PTHR14326; PTHR14326; 1.
DR Pfam; PF06886; TPX2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Developmental protein; Microtubule;
KW Reference proteome.
FT CHAIN 1..488
FT /note="Microtubule-destabilizing protein 60"
FT /id="PRO_0000454771"
FT REGION 25..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 13
FT /note="T -> A (in Ref. 1; AAG51320)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="S -> P (in Ref. 1; AAG51320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56173 MW; 9F5844DD77063428 CRC64;
MESTNLKNAK HETLVMDPIS FQSKAQEVSR FSENSNPNFV SHSTPLEKSS KSSAQKNPKW
KPNPVPAVFS PRNRIRERRF VVVKKNSRKE KNDSASVDCK CGAKTISNMK KCVCIAYETL
RASQEEFFNN RRESVSEIGE SSQNLEDGNE QVEFGDSDET RVSLMKRRRE KVLEEARMSI
PEFGKVMHLV KAFEKLTCFP LSKVTSKEEE DQIKQPLKWE LPGMSQPKCS ESETDQFTWS
SSFYPSSGLI LTATNLGLEQ PHASVSSSWD NSVSSLNSNG GRRGRRNSFE SSASMGSRRS
TKKQIKVTSL KPFKLRTEER GRMKEEEFAK KLHEMTLEKA KKRIPIAQGL PWTTDEPENL
VKPHVKDITI PVDLKLHSDI RAVERAEFDY QVTEKINLVE QYKTERERQQ KLAEEEEIRR
LRKELVPKAQ PMPYFDRPFI PKRSNKHPTV PRDPKFNIPQ HKKIRCCSTS SWSDTGSYMS
DLLYQQDL
