MA652_ARATH
ID MA652_ARATH Reviewed; 578 AA.
AC Q8LEG3; Q9SZ16;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=65-kDa microtubule-associated protein 2;
DE Short=AtMAP65-2;
GN Name=MAP65-2; OrderedLocusNames=At4g26760; ORFNames=F10M23.100;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19002591; DOI=10.1007/s11103-008-9426-1;
RA Li H., Zeng X., Liu Z.-Q., Meng Q.-T., Yuan M., Mao T.-L.;
RT "Arabidopsis microtubule-associated protein AtMAP65-2 acts as a microtubule
RT stabilizer.";
RL Plant Mol. Biol. 69:313-324(2009).
CC -!- FUNCTION: Microtubule-associated protein that stabilize microtubules
CC (MT). Involved in the regulation of MT organization and dynamics.
CC Confers MT resistance to the drug propyzamide and cold conditions.
CC {ECO:0000269|PubMed:19002591}.
CC -!- SUBUNIT: Forms a dimer (By similarity). Binds to microtubules (MT).
CC Bundles polymerized MT via the formation of 25-nm crossbridges with
CC centrally located endocytic MT. {ECO:0000250,
CC ECO:0000269|PubMed:19002591}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm. Cytoplasm,
CC cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast.
CC Note=During interphase, binds cortical microtubules. In M-phase,
CC locates to the preprophase band. Decorates entire mitotic spindle
CC during cell division. During the anaphase to telophase transition,
CC accumulates in the midline where oppositely oriented phragmoplast MTs
CC overlap. In the phragmoplast, colocalizes completely with the MTs.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79531.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL035440; CAB36522.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79531.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85249.1; -; Genomic_DNA.
DR EMBL; AY085430; AAM62657.1; -; mRNA.
DR EMBL; BT030366; ABO38779.1; -; mRNA.
DR PIR; T04799; T04799.
DR RefSeq; NP_567756.1; NM_118810.4.
DR AlphaFoldDB; Q8LEG3; -.
DR SMR; Q8LEG3; -.
DR BioGRID; 14070; 1.
DR STRING; 3702.AT4G26760.1; -.
DR iPTMnet; Q8LEG3; -.
DR PaxDb; Q8LEG3; -.
DR PRIDE; Q8LEG3; -.
DR ProteomicsDB; 238840; -.
DR EnsemblPlants; AT4G26760.1; AT4G26760.1; AT4G26760.
DR GeneID; 828783; -.
DR Gramene; AT4G26760.1; AT4G26760.1; AT4G26760.
DR KEGG; ath:AT4G26760; -.
DR Araport; AT4G26760; -.
DR TAIR; locus:2116267; AT4G26760.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_011760_1_0_1; -.
DR InParanoid; Q8LEG3; -.
DR OMA; KSYIDIP; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q8LEG3; -.
DR PRO; PR:Q8LEG3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8LEG3; baseline and differential.
DR Genevisible; Q8LEG3; AT.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0072686; C:mitotic spindle; IDA:TAIR.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA: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; IDA:TAIR.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IGI:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048528; P:post-embryonic root development; IGI:TAIR.
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..578
FT /note="65-kDa microtubule-associated protein 2"
FT /id="PRO_0000395473"
FT REGION 473..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 64..84
FT /evidence="ECO:0000255"
FT COILED 151..184
FT /evidence="ECO:0000255"
FT COILED 235..257
FT /evidence="ECO:0000255"
FT COILED 290..312
FT /evidence="ECO:0000255"
FT COILED 461..489
FT /evidence="ECO:0000255"
FT COMPBIAS 473..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 409
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 420
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
SQ SEQUENCE 578 AA; 65205 MW; A8544528EFB6C2DE CRC64;
MAVTEAENPL LGEITCGTLL QKLQEIWDEV GESDEERDKL LLQIEEECLN VYKKKVELAA
KSRAELLQTL SDATVELSNL TTALGEKSYI DIPDKTSGTI KEQLSAIAPA LEQLWQQKEE
RVRAFSDVQS QIQKICEEIA GGLNNGPHVV DETDLSLKRL DDFQRKLQEL QKEKSDRLQK
VLEFVSTVHD LCAVLRLDFL STVTEVHPSL DEANGVQTKS ISNETLARLA KTVLTLKEDK
MQRLKKLQEL ATQLTDLWNL MDTSDEEREL FDHVTSNISA SVHEVTASGA LALDLIEQAE
VEVDRLDQLK SSRMKEIAFK KQSELEEIYA RAHIEIKPEV VRERIMSLID AGNTEPTELL
ADMDSQIAKA KEEAFSRKEI LDRVEKWMSA CEEESWLEDY NRDQNRYSAS RGAHLNLKRA
EKARILVSKI TAMVDTLIAK TRAWEEENSM SFEYDGVPLL AMLDEYTMLR QEREDEKRRL
KEQKKQQEQP HTDQESAFGS KPSPARPVSA KKPVGTRVNG GGLNETPMRR LSMNSNQNGS
KSKRDSLNKI ASPSNIVANT KDDAASPVSR ADPVMASP
