EB1B_ARATH
ID EB1B_ARATH Reviewed; 293 AA.
AC Q9FJJ5; Q8GYG7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1B;
DE AltName: Full=APC-binding protein EB1B;
DE AltName: Full=End-binding protein 1;
DE Short=AtEB1;
DE AltName: Full=End-binding protein 1B;
DE Short=AtEB1B;
DE AltName: Full=Protein ATEB1 homolog 2;
DE Short=ATEB1H2;
GN Name=EB1B; OrderedLocusNames=At5g62500; ORFNames=K19B1.11;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14614826; DOI=10.1016/j.cub.2003.10.033;
RA Mathur J., Mathur N., Kernebeck B., Srinivas B.P., Huelskamp M.;
RT "A novel localization pattern for an EB1-like protein links microtubule
RT dynamics to endomembrane organization.";
RL Curr. Biol. 13:1991-1997(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18042620; DOI=10.1242/jcs.024950;
RA Kirik V., Herrmann U., Parupalli C., Sedbrook J.C., Ehrhardt D.W.,
RA Huelskamp M.;
RT "CLASP localizes in two discrete patterns on cortical microtubules and is
RT required for cell morphogenesis and cell division in Arabidopsis.";
RL J. Cell Sci. 120:4416-4425(2007).
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 FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP TYR-212 AND ILE-219, AND DISRUPTION 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. {ECO:0000269|PubMed:14614826,
CC ECO:0000269|PubMed:20067996}.
CC -!- SUBUNIT: Homodimer and heterodimer with EB1A.
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, but root growth is affected in response to gravity or touch
CC stimuli. conditions. {ECO:0000269|PubMed:18281505,
CC 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=BAC42296.1; Type=Frameshift; 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; AB015469; BAB11500.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97615.1; -; Genomic_DNA.
DR EMBL; AK117640; BAC42296.1; ALT_FRAME; mRNA.
DR EMBL; AY084598; AAM61163.1; -; mRNA.
DR RefSeq; NP_201056.1; NM_125644.3.
DR AlphaFoldDB; Q9FJJ5; -.
DR SMR; Q9FJJ5; -.
DR BioGRID; 21614; 4.
DR STRING; 3702.AT5G62500.1; -.
DR PaxDb; Q9FJJ5; -.
DR PRIDE; Q9FJJ5; -.
DR ProteomicsDB; 222013; -.
DR EnsemblPlants; AT5G62500.1; AT5G62500.1; AT5G62500.
DR GeneID; 836370; -.
DR Gramene; AT5G62500.1; AT5G62500.1; AT5G62500.
DR KEGG; ath:AT5G62500; -.
DR Araport; AT5G62500; -.
DR TAIR; locus:2154149; AT5G62500.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_0_1_1; -.
DR InParanoid; Q9FJJ5; -.
DR OMA; VQHAKEM; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q9FJJ5; -.
DR PRO; PR:Q9FJJ5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJJ5; baseline and differential.
DR Genevisible; Q9FJJ5; AT.
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:0005874; C:microtubule; HDA:TAIR.
DR GO; GO:0005815; C:microtubule organizing center; IDA:TAIR.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0005819; C:spindle; HDA:TAIR.
DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
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:0009958; P:positive gravitropism; IMP: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; Microtubule; Mitosis;
KW Reference proteome.
FT CHAIN 1..293
FT /note="Microtubule-associated protein RP/EB family member
FT 1B"
FT /id="PRO_0000418411"
FT DOMAIN 13..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 180..250
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 124..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..293
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..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 212
FT /note="Y->A: Loss of homodimerization; when associated with
FT A-219."
FT /evidence="ECO:0000269|PubMed:20067996"
FT MUTAGEN 219
FT /note="I->A: Loss of homodimerization; when associated with
FT A-211."
FT /evidence="ECO:0000269|PubMed:20067996"
SQ SEQUENCE 293 AA; 32931 MW; 967FB67D666E86F3 CRC64;
MATNIGMMDS AYFVGRNEIL SWINDRLHLN LSRIEEAASG AVQCQMLDMT FPGVVPMHKV
NFEAKNEYEM IQNYKVMQEV FTKLKITKPL EVNRLVKGRP LDNLEFLQWL KRFCDSINGG
IMNENYNPVE RRSRGGREKS VKGSSKISKS LQTNNMHHPP VATSNKPAGP KQAKSHGIGG
GSNSSAEVQA LSKEVEDLKV SVDLLEKERD FYFSKLRDIE ILCQTPELDD LPIVVAVKKI
LYATDANESV LEEAQECLNQ SLGLEGYEEE GKEEEEEEEE EEEEAAAAAE TQT
