MA655_ARATH
ID MA655_ARATH Reviewed; 550 AA.
AC Q9ZVJ3; F4ITW9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=65-kDa microtubule-associated protein 5;
DE Short=AtMAP65-5;
GN Name=MAP65-5; OrderedLocusNames=At2g38720; ORFNames=T6A23.8;
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=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 [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 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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15557096; DOI=10.1104/pp.104.051623;
RA Van Damme D., Van Poucke K., Boutant E., Ritzenthaler C., Inze D.,
RA Geelen D.;
RT "In vivo dynamics and differential microtubule-binding activities of MAP65
RT proteins.";
RL Plant Physiol. 136:3956-3967(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18667529; DOI=10.1091/mbc.e08-04-0341;
RA Gaillard J., Neumann E., Van Damme D., Stoppin-Mellet V., Ebel C.,
RA Barbier E., Geelen D., Vantard M.;
RT "Two microtubule-associated proteins of Arabidopsis MAP65s promote
RT antiparallel microtubule bundling.";
RL Mol. Biol. Cell 19:4534-4544(2008).
RN [7]
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 bundle and stabilize
CC adjacent microtubules (MT) of the cell cortex. Confers MT resistance to
CC the drug oryzalin. Promotes the formation of a planar network of
CC antiparallel microtubules. {ECO:0000269|PubMed:15557096,
CC ECO:0000269|PubMed:18667529}.
CC -!- SUBUNIT: Forms a dimer (By similarity). Binds to MT, mostly with
CC coaligned MT, both between parallel or antiparallel, forming thick
CC bundles. Bundles polymerized MT via the formation of 25-nm crossbridges
CC with cortical MT. {ECO:0000250, ECO:0000269|PubMed:15557096,
CC ECO:0000269|PubMed:18667529}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cytoplasm,
CC cytoskeleton, spindle. Cytoplasm, cytoskeleton, phragmoplast.
CC Cytoplasm, cell cortex. Cell junction, plasmodesma. Note=Present in MT
CC cortical arrays. Binds the preprophase band and the prophase spindle
CC microtubule during prophase. Binds MT during anaphase. Associates also
CC with phragmoplast; binds MT of young emerging phragmoplasts but don't
CC binds along MT when the disk-shaped phragmoplasts transform into a
CC ring-shaped, centrifugally expanding structure. At this time,
CC accumulates in the cell plate and associates with the surface of the
CC separated nuclei. Later traverses the newly formed cross wall, probably
CC in association with plasmodesma.
CC -!- INDUCTION: Expressed throughout the cell cycle.
CC {ECO:0000269|PubMed:15557096}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC67346.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005499; AAC67346.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09577.2; -; Genomic_DNA.
DR PIR; E84808; E84808.
DR RefSeq; NP_001318376.1; NM_001336724.1.
DR AlphaFoldDB; Q9ZVJ3; -.
DR SMR; Q9ZVJ3; -.
DR STRING; 3702.AT2G38720.1; -.
DR PRIDE; Q9ZVJ3; -.
DR ProteomicsDB; 238551; -.
DR EnsemblPlants; AT2G38720.1; AT2G38720.1; AT2G38720.
DR GeneID; 818454; -.
DR Gramene; AT2G38720.1; AT2G38720.1; AT2G38720.
DR KEGG; ath:AT2G38720; -.
DR Araport; AT2G38720; -.
DR eggNOG; KOG4302; Eukaryota.
DR InParanoid; Q9ZVJ3; -.
DR OMA; AQIKCIN; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q9ZVJ3; -.
DR PRO; PR:Q9ZVJ3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZVJ3; baseline and differential.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..550
FT /note="65-kDa microtubule-associated protein 5"
FT /id="PRO_0000395476"
FT REGION 471..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..174
FT /evidence="ECO:0000255"
FT COILED 288..310
FT /evidence="ECO:0000255"
FT COMPBIAS 471..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 401
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 412
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 62653 MW; B73640A1BD445A80 CRC64;
MSPSSTTTCT SLLEELQMIW DEIGESYNER DKMLLELEQE CLDIYNKKVE KTRKFRAELQ
RSLAQAEAEI ASLMSALGEK VSFAKKEGSL KEQISSVKPV LEDLLMKKDR RRKELSETLN
QIAEITSNIA GNDYTVSSGS EVDESDLTQR KLDELRADLQ DLRNEKAVRL QKVNSYISAV
HELSEILSFD FSKALNSVHS SLTEFSKTHS KSISNDTLAR FTELVKSLKA EKHERLLKLQ
GLGRSMQELW NLMETPMDER RRFDHCSSLL SSLPDDALKK GCLSLDIIRE AEDEVRRLNS
LKSSKMKELV FKRQCELEEI CRGNHMDINS DAARKSLVEL IESGDGDLSD ILASIDGQIE
KAREEALSRK EILDKVDKWR HAKEEETWLD DYEKDENRFS AVRGAHKNLK RAEKARSLIS
KIPAMVDVLT TKVKAWEKER GVPFLCDKQP LLQTLEDDIV IRAQREEEKR QFREQKRLQG
QLATEKEAKY GSKSAKKKPL GQSLNTDNVT KTPIGRRIGN TPGRSVTSGG KDYRGNAVIP
LNYVALQKDD
