MA654_ARATH
ID MA654_ARATH Reviewed; 677 AA.
AC Q9LZY0; F4JD03;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=65-kDa microtubule-associated protein 4;
DE Short=AtMAP65-4;
GN Name=MAP65-4; OrderedLocusNames=At3g60840; ORFNames=T4C21.250;
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 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 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 involved in mitotic spindle
CC formation. {ECO:0000269|PubMed:15557096}.
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:15557096}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15469496,
CC ECO:0000269|PubMed:15557096, ECO:0000269|PubMed:19060108}.
CC Note=Localized specifically to MT that rearranged to form a spindle and
CC the polar sides of the spindle proper. Associates to MT in preprophase
CC band, during anaphase, and in phragmoplast.
CC -!- INDUCTION: Cell cycle-regulated expression with higher levels during
CC mitosis. {ECO:0000269|PubMed:15557096}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82688.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL162295; CAB82688.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80116.2; -; Genomic_DNA.
DR PIR; T47895; T47895.
DR RefSeq; NP_001319808.1; NM_001340060.1.
DR AlphaFoldDB; Q9LZY0; -.
DR SMR; Q9LZY0; -.
DR STRING; 3702.AT3G60840.1; -.
DR PaxDb; Q9LZY0; -.
DR PRIDE; Q9LZY0; -.
DR ProteomicsDB; 238761; -.
DR EnsemblPlants; AT3G60840.1; AT3G60840.1; AT3G60840.
DR GeneID; 825255; -.
DR Gramene; AT3G60840.1; AT3G60840.1; AT3G60840.
DR KEGG; ath:AT3G60840; -.
DR Araport; AT3G60840; -.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_011760_0_0_1; -.
DR InParanoid; Q9LZY0; -.
DR OMA; SKELCLH; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q9LZY0; -.
DR PRO; PR:Q9LZY0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZY0; baseline and differential.
DR Genevisible; Q9LZY0; AT.
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:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..677
FT /note="65-kDa microtubule-associated protein 4"
FT /id="PRO_0000395475"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 49..121
FT /evidence="ECO:0000255"
FT COILED 151..189
FT /evidence="ECO:0000255"
FT COILED 354..383
FT /evidence="ECO:0000255"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 406
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 417
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
SQ SEQUENCE 677 AA; 76939 MW; 26F8747DA32AD036 CRC64;
MIRNSTEQFS RIETTCGLLL RQLQEIWNEM GETEDEKDAS LADIEKECLS VYKRKVEEAS
RGKANLLKEI AVGRAEIAAI GSSMGGQEIH SNSRLGENLK EELENVNVQL DGLRKRKAER
MIRFNEVIDQ LLKLSLQLGN PTDYLKKFAA EETDLSLQRL EELRSQLGEL QNEKSKRLEE
VECLLKTLNS LCSVLGEDFK GMIRGIHSSL VDSNTRDVSR STLDKLDMMI VNLREAKLQR
MQKVQDLAVS LLELWNLLDT PAEEQKIFHN VTCSIALTES EITEANILSV ASIKRVEDEV
IRLSKIKITK IKEVILRKRL ELEEISRKMH MATEVLKSEN FSVEAIESGV KDPEQLLEQI
DSEIAKVKEE ASSRKEILEK VEKWMSACEE ESWLEEYNRD DNRYNAGRGA HLTLKRAEKA
RLLVNKLPGM VEALTAKVTA WENERGNEFL YDGVRVLSML GQYKTVWEEK EHEKQRQRDM
KKLHGQLITE QEALYGSKPS PNKSGKKPLR TPVNAAMNRK LSLGGAMLHQ SLKHEKATLN
SKRTKYYDQN ATSRRDSALP TLSGRRNSEL PGRIRSKNVP VAGKAARSPM LRKPLSPVTS
NILNSPEDHH KDAYTTKERI LTPKTNEEKK RAVPTTPAAS VAMTEATTPF TPAVEKRMDE
EDVIVEYSFE EVRAGFC
