MA653_ARATH
ID MA653_ARATH Reviewed; 707 AA.
AC Q9FHM4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=65-kDa microtubule-associated protein 3;
DE Short=AtMAP65-3;
DE AltName: Full=Protein PLEIADE;
GN Name=MAP65-3; Synonyms=PLE; OrderedLocusNames=At5g51600;
GN ORFNames=K17N15.15;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12516862; DOI=10.1023/a:1021236307508;
RA Hussey P.J., Hawkins T.J., Igarashi H., Kaloriti D., Smertenko A.;
RT "The plant cytoskeleton: recent advances in the study of the plant
RT microtubule-associated proteins MAP-65, MAP-190 and the Xenopus MAP215-like
RT protein, MOR1.";
RL Plant Mol. Biol. 50:915-924(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12068111; DOI=10.1104/pp.004184;
RA Soellner R., Glaesser G., Wanner G., Somerville C.R., Juergens G.,
RA Assaad F.F.;
RT "Cytokinesis-defective mutants of Arabidopsis.";
RL Plant Physiol. 129:678-690(2002).
RN [5]
RP FUNCTION, MUTAGENESIS OF ALA-421, AND DISRUPTION PHENOTYPE.
RX PubMed=12226511; DOI=10.1104/pp.004416;
RA Mueller S., Fuchs E., Ovecka M., Wysocka-Diller J., Benfey P.N.,
RA Hauser M.-T.;
RT "Two new loci, PLEIADE and HYADE, implicate organ-specific regulation of
RT cytokinesis in Arabidopsis.";
RL Plant Physiol. 130:312-324(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP MICROTUBULES.
RX PubMed=15028217; DOI=10.1016/j.cub.2004.02.032;
RA Mueller S., Smertenko A., Wagner V., Heinrich M., Hussey P.J.,
RA Hauser M.-T.;
RT "The plant microtubule-associated protein AtMAP65-3/PLE is essential for
RT cytokinetic phragmoplast function.";
RL Curr. Biol. 14:412-417(2004).
RN [7]
RP INTERACTION WITH MICROTUBULES, AND 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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18263774; DOI=10.1105/tpc.107.057422;
RA Caillaud M.-C., Lecomte P., Jammes F., Quentin M., Pagnotta S., Andrio E.,
RA de Almeida Engler J., Marfaing N., Gounon P., Abad P., Favery B.;
RT "MAP65-3 microtubule-associated protein is essential for nematode-induced
RT giant cell ontogenesis in Arabidopsis.";
RL Plant Cell 20:423-437(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19060108; DOI=10.1105/tpc.108.063362;
RA Smertenko A.P., Kaloriti D., Chang H.-Y., Fiserova J., Opatrny Z.,
RA Hussey P.J.;
RT "The C-terminal variable region specifies the dynamic properties of
RT Arabidopsis microtubule-associated protein MAP65 isotypes.";
RL Plant Cell 20:3346-3358(2008).
CC -!- FUNCTION: Microtubule-associated protein that plays a critical role in
CC organizing the mitotic microtubule array during both early and late
CC mitosis in all plant organs. Essential for the cytokinesis, especially
CC in roots, by maintaining the integrity of the overlapped microtubules
CC in the phragmoplast. Required during root morphogenesis. Needed for
CC giant cell development during root knot nematode infection, where
CC cytokinesis is initiated but not completed.
CC {ECO:0000269|PubMed:12068111, ECO:0000269|PubMed:12226511,
CC ECO:0000269|PubMed:15028217, ECO:0000269|PubMed:18263774}.
CC -!- SUBUNIT: Forms a dimer (By similarity). Binds to microtubules (MT)
CC during cell division. Bundles polymerized MT via the formation of 25-nm
CC crossbridges with centrally located endocytic MT, and midline
CC phragmoplast MT. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC phragmoplast. Note=Locates only to the mitotic MT arrays. Present in MT
CC cortical arrays just before mitosis. Associates to MT in preprophase
CC band, during anaphase, and in phragmoplast, including midzone.
CC Distributed diffusely through the cytoplasm during metaphase only. At
CC the end of cytokinesis, present only at the cell periphery, forming a
CC ring around the newly formed cell plate. During root knot nematode
CC infection, targeted to the giant cell mini cell plate.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues enriched in dividing
CC cells, such as the root and shoot apical meristem, foliar primordia,
CC and young leaves, and embryos. {ECO:0000269|PubMed:18263774}.
CC -!- DEVELOPMENTAL STAGE: Present in dividing tissues during all stages of
CC embryonic development. {ECO:0000269|PubMed:18263774}.
CC -!- DISRUPTION PHENOTYPE: Irregular root expansion. Defects in karyokinesis
CC and cytokinesis. Cytokinesis defects before the embryo dermatogen stage
CC and in roots. Embryos with enlarged nuclei, often containing multiple
CC nucleoli. Some abnormal stomata with pores attached to a single side of
CC the mother cell. Long root hairs. In roots, multinucleated cells, cell
CC wall stubs, and synchronized cell divisions in incompletely separated
CC cells. Normal anaphase spindle, but distorted phragmoplast. Abnormal
CC formation of nematode-mediated giant cells leading to impaired
CC maturation of nematode larvae. {ECO:0000269|PubMed:12068111,
CC ECO:0000269|PubMed:12226511, ECO:0000269|PubMed:15028217}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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DR EMBL; AB018109; BAB08676.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96102.1; -; Genomic_DNA.
DR RefSeq; NP_199973.1; NM_124539.4.
DR AlphaFoldDB; Q9FHM4; -.
DR SMR; Q9FHM4; -.
DR BioGRID; 20479; 1.
DR IntAct; Q9FHM4; 1.
DR STRING; 3702.AT5G51600.1; -.
DR iPTMnet; Q9FHM4; -.
DR PaxDb; Q9FHM4; -.
DR PRIDE; Q9FHM4; -.
DR ProteomicsDB; 238581; -.
DR EnsemblPlants; AT5G51600.1; AT5G51600.1; AT5G51600.
DR GeneID; 835234; -.
DR Gramene; AT5G51600.1; AT5G51600.1; AT5G51600.
DR KEGG; ath:AT5G51600; -.
DR Araport; AT5G51600; -.
DR TAIR; locus:2153152; AT5G51600.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_011760_0_0_1; -.
DR InParanoid; Q9FHM4; -.
DR OMA; YYREAPE; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q9FHM4; -.
DR PRO; PR:Q9FHM4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHM4; baseline and differential.
DR Genevisible; Q9FHM4; AT.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0052096; P:formation of syncytium involving giant cell for nutrient acquisition; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0046785; P:microtubule polymerization; IDA:TAIR.
DR GO; GO:0000280; P:nuclear division; IMP:TAIR.
DR GO; GO:0009624; P:response to nematode; IMP:UniProtKB.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..707
FT /note="65-kDa microtubule-associated protein 3"
FT /id="PRO_0000395474"
FT REGION 495..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..84
FT /evidence="ECO:0000255"
FT COILED 157..179
FT /evidence="ECO:0000255"
FT COILED 269..289
FT /evidence="ECO:0000255"
FT COILED 354..374
FT /evidence="ECO:0000255"
FT COILED 464..486
FT /evidence="ECO:0000255"
FT COMPBIAS 538..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 410
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 421
FT /note="Microtubule binding"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MUTAGEN 421
FT /note="A->V: In ple-4; impaired microtubule binding."
FT /evidence="ECO:0000269|PubMed:12226511"
SQ SEQUENCE 707 AA; 80302 MW; 30EAF1E5BCC6BB9A CRC64;
MASVQKDPIL QVETTCGSLL FELQIIWDEV GETETDRDQM LLELERECLE VYRRKVDQAN
RCRAQLRQAI ADAEAQLAAI CSAMGERPVH IRQSDQSVGS LKQELGRILP ELEEMQKRKV
ERRNQFIVVM EQIDSITNDI KGQGELVHSE PLIDETNLSM RKLEELHCQL QVLQKEKIDR
VETIRKHLCT LYSHCSVLGM DFNEVVGQVN PTLSDPEGPR SLSDHTIEKL GAAVQKLMEV
KIQRMQRLQD LATTMLELWN LMDTPIEEQQ EYQHITCNIA ASEHEITEAN SLSEDFIKYV
EAEVVRLDEV KASKMKELVL KKRSELEEIC RKTHLLPVSD SAIDQTIVAI ESGIVDATMV
LEHLEQHISK IKEEALSRKE ILERVEKWLS ACDEESWLEE YNRDDNRYNA GRGAHLTLKR
AEKARNLVTK LPGMVEALAS KTIVWEQENG IEFLYDGIRL LSMLEEYNIL RQEREEEHRR
QRDQKKLQGQ LIAEQEALYG SKPSPSKPLG GKKAPRMSTG GASNRRLSLG AAMHQTPKPN
KKADHRHNDG ALSNGRRGLD IAGLPSRKQS MNPSEMLQSP LVRKPFSPIS TTVVASKANI
ATTTTQQLPK NNAVNEISSF ATPIKNNNIL RNLEEEKMMT MMMQTPKNVA AMIPIPSTPA
TVSVPMHTAP TPFTNNARLM SEKPEVVEYS FEERRLAFML QSECRLV
