MA659_ARATH
ID MA659_ARATH Reviewed; 549 AA.
AC Q4PSA3; Q9LVB1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=65-kDa microtubule-associated protein 9;
DE Short=AtMAP65-9;
GN Name=MAP65-9; OrderedLocusNames=At5g62250; ORFNames=MMI9.8;
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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- SUBUNIT: Forms dimer. Binds to microtubules (MT) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97189.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019235; BAA97189.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97586.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68950.1; -; Genomic_DNA.
DR EMBL; DQ056733; AAY78877.1; -; mRNA.
DR RefSeq; NP_001318863.1; NM_001345543.1.
DR RefSeq; NP_201031.1; NM_125619.2.
DR AlphaFoldDB; Q4PSA3; -.
DR SMR; Q4PSA3; -.
DR STRING; 3702.AT5G62250.1; -.
DR iPTMnet; Q4PSA3; -.
DR PaxDb; Q4PSA3; -.
DR PRIDE; Q4PSA3; -.
DR ProteomicsDB; 238278; -.
DR EnsemblPlants; AT5G62250.1; AT5G62250.1; AT5G62250.
DR EnsemblPlants; AT5G62250.2; AT5G62250.2; AT5G62250.
DR GeneID; 836346; -.
DR Gramene; AT5G62250.1; AT5G62250.1; AT5G62250.
DR Gramene; AT5G62250.2; AT5G62250.2; AT5G62250.
DR KEGG; ath:AT5G62250; -.
DR Araport; AT5G62250; -.
DR TAIR; locus:2167978; AT5G62250.
DR eggNOG; KOG4302; Eukaryota.
DR HOGENOM; CLU_011760_1_1_1; -.
DR InParanoid; Q4PSA3; -.
DR OMA; QIEYRAG; -.
DR OrthoDB; 272248at2759; -.
DR PhylomeDB; Q4PSA3; -.
DR PRO; PR:Q4PSA3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q4PSA3; baseline and differential.
DR Genevisible; Q4PSA3; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..549
FT /note="65-kDa microtubule-associated protein 9"
FT /id="PRO_0000395480"
FT REGION 474..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..123
FT /evidence="ECO:0000255"
FT COILED 160..199
FT /evidence="ECO:0000255"
FT COILED 459..492
FT /evidence="ECO:0000255"
FT COMPBIAS 474..494
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 412
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT SITE 423
FT /note="Microtubule binding"
FT /evidence="ECO:0000250"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FLP0"
SQ SEQUENCE 549 AA; 63869 MW; 116F52062055A5FB CRC64;
MSKSQIESTW SSLLQELEII WKEVGETETE REKILIEIEE ECREVYNRKI EKVKEEKIRI
KQEIADSEAR VIDICSVMEE PPILGRHHQS DQQSGNGRSL KDELVKILQK LEEMEKRKSE
RKIQFIQVID DIRCVREEIN GESDDETCSS DFSADESDLS LRKLEELHRE LYTLQEQKRN
RVKQIQDNIR TLESLCSVLG LNFRETVTKI HPSLVDTEGS RSISNETLDK LASSVQQWHE
TKIQRMQELQ DLVTTMLEFW NLMDTPAEEQ QKFMDVSCNI AATVSEITKP NSLSIDLLEE
VKAELCRLEE LKWSKMKELV LKKRSELEEI CRRTHIVLEE EDIAVENVIK AIESGDVNPE
NILEQIEYRA GKVKEEALSR KEILEKADKW LNACEEENWL EEYNQDENRY NAGKGSHLIL
KRAEKARALV NKLPAMVEAL ASKITIWESE KEYEFLFDGN RLLSMLEEYT ELREEKEQER
RRKRDLKKHQ GQVTSEQDKG SVTKPQSAKK GLKVSTNKRF VSSPHTPQTD SPHSAKSNQS
FSTPLSRHG
