MA656_ARATH
ID MA656_ARATH Reviewed; 608 AA.
AC Q9SIS3; Q0WPU6; Q2V4B4;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=65-kDa microtubule-associated protein 6;
DE Short=AtMAP65-6;
GN Name=MAP65-6; OrderedLocusNames=At2g01910; ORFNames=T23K3.10;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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=15908607; DOI=10.1104/pp.104.052456;
RA Mao T., Jin L., Li H., Liu B., Yuan M.;
RT "Two microtubule-associated proteins of the Arabidopsis MAP65 family
RT function differently on microtubules.";
RL Plant Physiol. 138:654-662(2005).
RN [8]
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 mediates the formation of
CC a mesh-like stable and dense network formed by individual microtubules
CC (MT). Confers MT resistance to high concentration of NaCl.
CC {ECO:0000269|PubMed:15908607}.
CC -!- SUBUNIT: Forms a dimer (By similarity). Binds to polymerized centrally
CC located endocytic MT. {ECO:0000250, ECO:0000269|PubMed:15908607}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm. Mitochondrion.
CC Cytoplasm, cytoskeleton, phragmoplast. Note=Associated with
CC mitochondria. Binds to MT in preprophase band, during anaphase, and in
CC phragmoplast.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIS3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIS3-2; Sequence=VSP_039480;
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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DR EMBL; AC007069; AAD21782.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05516.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05517.1; -; Genomic_DNA.
DR EMBL; AK317525; BAH20190.1; -; mRNA.
DR EMBL; AK228964; BAF00853.1; -; mRNA.
DR PIR; F84430; F84430.
DR RefSeq; NP_001030945.1; NM_001035868.2. [Q9SIS3-2]
DR RefSeq; NP_178300.3; NM_126252.4. [Q9SIS3-1]
DR AlphaFoldDB; Q9SIS3; -.
DR SMR; Q9SIS3; -.
DR STRING; 3702.AT2G01910.1; -.
DR iPTMnet; Q9SIS3; -.
DR PaxDb; Q9SIS3; -.
DR PRIDE; Q9SIS3; -.
DR ProteomicsDB; 238510; -. [Q9SIS3-1]
DR EnsemblPlants; AT2G01910.1; AT2G01910.1; AT2G01910. [Q9SIS3-1]
DR EnsemblPlants; AT2G01910.2; AT2G01910.2; AT2G01910. [Q9SIS3-2]
DR GeneID; 814722; -.
DR Gramene; AT2G01910.1; AT2G01910.1; AT2G01910. [Q9SIS3-1]
DR Gramene; AT2G01910.2; AT2G01910.2; AT2G01910. [Q9SIS3-2]
DR KEGG; ath:AT2G01910; -.
DR Araport; AT2G01910; -.
DR TAIR; locus:2059713; AT2G01910.
DR eggNOG; KOG4302; Eukaryota.
DR InParanoid; Q9SIS3; -.
DR OMA; ERECMEV; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q9SIS3; -.
DR PRO; PR:Q9SIS3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIS3; baseline and differential.
DR Genevisible; Q9SIS3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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: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 Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitochondrion; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..608
FT /note="65-kDa microtubule-associated protein 6"
FT /id="PRO_0000395477"
FT REGION 501..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..186
FT /evidence="ECO:0000255"
FT COILED 368..388
FT /evidence="ECO:0000255"
FT COILED 467..503
FT /evidence="ECO:0000255"
FT COMPBIAS 503..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 419
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 430
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_039480"
FT CONFLICT 128
FT /note="Q -> L (in Ref. 4; BAF00853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 69407 MW; 5AE1314D0D311413 CRC64;
MLEIGSPNAL FFRTNTTCNN LLRELQKIWV EIGETETEKD RMLMELEREC LQIYQRKVDE
AANSKAKLHQ SVASIEAEVA SLMAALGVLN INSPIKLDKG SKSLKEKLAA VTPLVEELRI
QKEERMKQFS DIKAQIEKIS GEISGYSDHL NKAMNISLTL EEQDLTLRNL NEYQTHLRTL
QKEKSDRLNK VLGYVNEVHA LCGVLGVDFS QTVSAVHPSL HRTDQEQSTN ISDSTLEGLE
HMIQKLKTER KSRFQKLKDV VASLFELWNL MDTPQEDRTK FGKVTYVVRS SEANITEPGI
LSTETIEQVS TEVDSLSKLK ASRMKELVMK RRSELEDLCR LTHIQPDTST SAEKSTALID
SGLVDPSELL ANIEMQINKI KDEAQSRKDI MDRIDRWLSA CEEENWLEEY NLDENRYSAG
RGGHVNLKRA ERARVTINKI PGMVDTLIKK TLVWEEDMQK SFLYDGVRLV NILEDYKLTR
KQQEEEKKRY RDQKKRQDLL LTQRESIYGS KPSPRRSSSF RKPNGFNISN GNGSVPPTPR
RGSVGTTTPD VLLTPRSYSG HHRQNGYFKE VRRLSTTPLN YVAMQKEDTV STTYTSIYSS
EPDSPLQG
