EB1A_ARATH
ID EB1A_ARATH Reviewed; 276 AA.
AC Q7XJ60; Q9STU4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1A;
DE AltName: Full=APC-binding protein EB1A;
DE AltName: Full=End-binding protein 1A;
DE Short=AtEB1A;
DE AltName: Full=Protein ATEB1 homolog 2;
DE Short=AtEB1H2;
GN Name=EB1A; OrderedLocusNames=At3g47690; ORFNames=T23J7.20;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14557818; DOI=10.1038/ncb1057;
RA Chan J., Calder G.M., Doonan J.H., Lloyd C.W.;
RT "EB1 reveals mobile microtubule nucleation sites in Arabidopsis.";
RL Nat. Cell Biol. 5:967-971(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15879559; DOI=10.1105/tpc.105.032615;
RA Chan J., Calder G., Fox S., Lloyd C.;
RT "Localization of the microtubule end binding protein EB1 reveals
RT alternative pathways of spindle development in Arabidopsis suspension
RT cells.";
RL Plant Cell 17:1737-1748(2005).
RN [7]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18281505; DOI=10.1105/tpc.107.056846;
RA Bisgrove S.R., Lee Y.R., Liu B., Peters N.T., Kropf D.L.;
RT "The microtubule plus-end binding protein EB1 functions in root responses
RT to touch and gravity signals in Arabidopsis.";
RL Plant Cell 20:396-410(2008).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TOBAMOVIRUS MOVEMENT PROTEIN.
RX PubMed=18408045; DOI=10.1104/pp.108.117481;
RA Brandner K., Sambade A., Boutant E., Didier P., Mely Y., Ritzenthaler C.,
RA Heinlein M.;
RT "Tobacco mosaic virus movement protein interacts with green fluorescent
RT protein-tagged microtubule end-binding protein 1.";
RL Plant Physiol. 147:611-623(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19706794; DOI=10.1105/tpc.109.069716;
RA Chan J., Sambade A., Calder G., Lloyd C.;
RT "Arabidopsis cortical microtubules are initiated along, as well as
RT branching from, existing microtubules.";
RL Plant Cell 21:2298-2306(2009).
RN [10]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20067996; DOI=10.1242/jcs.062703;
RA Komaki S., Abe T., Coutuer S., Inze D., Russinova E., Hashimoto T.;
RT "Nuclear-localized subtype of end-binding 1 protein regulates spindle
RT organization in Arabidopsis.";
RL J. Cell Sci. 123:451-459(2010).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. May be involved in anchoring
CC microtubules to their nucleation sites and/or functioning as a
CC reservoir for distribution to the growing end. In plants, microtubule
CC minus ends are not necessarily severed from the nucleation site and
CC transported to the plus end of a microtubule as part of the recycling
CC process. May play a role in endomembrane organization during polarized
CC growth of plant cells. Interacts with the tobamovirus movement protein
CC (MP) and may play a role in the association of MP with the microtubule
CC system during infection. {ECO:0000269|PubMed:14557818,
CC ECO:0000269|PubMed:20067996}.
CC -!- SUBUNIT: Homodimer and heterodimer with EB1B. Interacts with
CC tobamovirus movement protein. {ECO:0000269|PubMed:18408045,
CC ECO:0000269|PubMed:20067996}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole. Cytoplasm,
CC cytoskeleton, phragmoplast. Note=Localizes both to the plus ends of
CC microtubules and to the sites of nucleation during division and
CC interphase.
CC -!- TISSUE SPECIFICITY: Highly expressed in guard cells of leaf stomata,
CC pollen grains and pollen tubes. Expressed in young roots.
CC {ECO:0000269|PubMed:20067996}.
CC -!- DOMAIN: Composed of two functionally independent domains. The N-
CC terminal domain forms a hydrophobic cleft involved in microtubule
CC binding and the C-terminal is involved in protein binding. In
CC Arabidopsis thaliana, EB1A and EB1B possess an acidic C-terminal tail
CC that has autoinhibitory function, but EB1C has a tail region with
CC patches of basic amino acid residues required for nuclear targeting.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18281505, ECO:0000269|PubMed:20067996}.
CC -!- MISCELLANEOUS: Plant microtubules behave differently from those of
CC other eukaryotes in mitosis: they lack centrosomes and spindles are
CC barrel-shaped with unfocused poles and no astral microtubules.
CC {ECO:0000305|PubMed:18281505}.
CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41852.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049746; CAB41852.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78319.1; -; Genomic_DNA.
DR EMBL; BT009707; AAP88341.1; -; mRNA.
DR EMBL; AK227867; BAE99843.1; -; mRNA.
DR PIR; T07708; T07708.
DR RefSeq; NP_190353.3; NM_114637.4.
DR AlphaFoldDB; Q7XJ60; -.
DR SMR; Q7XJ60; -.
DR BioGRID; 9243; 3.
DR STRING; 3702.AT3G47690.1; -.
DR PaxDb; Q7XJ60; -.
DR PRIDE; Q7XJ60; -.
DR ProteomicsDB; 222044; -.
DR DNASU; 823923; -.
DR EnsemblPlants; AT3G47690.1; AT3G47690.1; AT3G47690.
DR GeneID; 823923; -.
DR Gramene; AT3G47690.1; AT3G47690.1; AT3G47690.
DR KEGG; ath:AT3G47690; -.
DR Araport; AT3G47690; -.
DR TAIR; locus:2100417; AT3G47690.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_0_1_1; -.
DR InParanoid; Q7XJ60; -.
DR OMA; ICQEKES; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q7XJ60; -.
DR PRO; PR:Q7XJ60; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7XJ60; baseline and differential.
DR GO; GO:0010005; C:cortical microtubule, transverse to long axis; IDA:TAIR.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IDA:TAIR.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR GO; GO:0005876; C:spindle microtubule; IDA:TAIR.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0001578; P:microtubule bundle formation; IGI:TAIR.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR GO; GO:0009652; P:thigmotropism; IMP:TAIR.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR004953; EB1_C.
DR InterPro; IPR036133; EB1_C_sf.
DR InterPro; IPR027328; MAPRE.
DR PANTHER; PTHR10623; PTHR10623; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF03271; EB1; 1.
DR SUPFAM; SSF140612; SSF140612; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51230; EB1_C; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Host-virus interaction;
KW Microtubule; Mitosis; Reference proteome.
FT CHAIN 1..276
FT /note="Microtubule-associated protein RP/EB family member
FT 1A"
FT /id="PRO_0000418410"
FT DOMAIN 13..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 173..243
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 124..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 31080 MW; B1BC78E0ACA00839 CRC64;
MATNIGMMDS AYFVGRNEIL TWINDRLHLN LSRVEEAASG AVQCQMLDMT FPGVVPMHKV
NFDAKNEYDM IQNYKVLQDV FNKLKITKPL EINRLVKGRP LDNLEFLQWL KRFCDSINGG
IMNENYNPVE RRSRNGKERS VKGSNKIPKS LQTNNNHPPP NSSSVGLSKA SGPKSAKAAE
VQALSKELVD LKISTDLLEK ERDFYFSKLR DVEILCQTPE LDDLPIVVAV KKILYATDAN
ESALEDAQEY LNQSLGVEDD EAEGNGEQLE EEKTQA
