EB1C_ARATH
ID EB1C_ARATH Reviewed; 329 AA.
AC Q9FGQ6;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Microtubule-associated protein RP/EB family member 1C;
DE AltName: Full=APC-binding protein EB1C;
DE AltName: Full=End-binding protein 1C;
DE Short=AtEB1C;
DE AltName: Full=Protein ATEB1 homolog 1;
DE Short=AtEB1H1;
GN Name=EB1C; OrderedLocusNames=At5g67270; ORFNames=K3G17.3;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19825573; DOI=10.1093/mp/ssn026;
RA Cheung A.Y., Duan Q.H., Costa S.S., de Graaf B.H., Di Stilio V.S.,
RA Feijo J., Wu H.M.;
RT "The dynamic pollen tube cytoskeleton: live cell studies using actin-
RT binding and microtubule-binding reporter proteins.";
RL Mol. Plant 1:686-702(2008).
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 289-LYS--LYS-291 AND 309-ARG--ARG-311, 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).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21873565; DOI=10.1105/tpc.110.078204;
RA Ho C.M., Hotta T., Guo F., Roberson R.W., Lee Y.R., Liu B.;
RT "Interaction of antiparallel microtubules in the phragmoplast is mediated
RT by the microtubule-associated protein MAP65-3 in Arabidopsis.";
RL Plant Cell 23:2909-2923(2011).
CC -!- FUNCTION: Plant-specific EB1 subtype that functions preferentially at
CC early stages of plant mitosis by regulating spindle positioning and
CC chromosome segregation. Accumulates in the prophase nucleus and is
CC required to maintain spindle bipolarity during premetaphase and/or
CC metaphase and for efficient segregation of chromosomes at anaphase. May
CC play a role in the dynamics of microtubule network in elongating pollen
CC tubes. {ECO:0000269|PubMed:19825573, ECO:0000269|PubMed:20067996}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20067996}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Cytoplasm, cytoskeleton, phragmoplast. Note=During mitosis, accumulates
CC in the prophase nucleus, and after the nuclear envelope disintegration
CC is associated with whole spindle microtubules, plus end of
CC microtubules, phragmoplast and finally is actively recruited to the
CC nucleus. Localizes in the microtubule network in elongating pollen
CC tubes.
CC -!- TISSUE SPECIFICITY: Highly expressed in the root and shoot meristems,
CC in guard cells of leaf stomata, pollen grains and pollen tubes.
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 seedlings show increased sensitivity to oryzalin, a
CC microtubule-destabilizing agent. conditions.
CC {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}.
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DR EMBL; AB025614; BAB09646.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98323.1; -; Genomic_DNA.
DR EMBL; AK175495; BAD43258.1; -; mRNA.
DR EMBL; BT028930; ABI49477.1; -; mRNA.
DR EMBL; AY087775; AAM65311.1; -; mRNA.
DR RefSeq; NP_201528.1; NM_126127.4.
DR AlphaFoldDB; Q9FGQ6; -.
DR SMR; Q9FGQ6; -.
DR BioGRID; 22104; 3.
DR STRING; 3702.AT5G67270.1; -.
DR iPTMnet; Q9FGQ6; -.
DR PaxDb; Q9FGQ6; -.
DR PRIDE; Q9FGQ6; -.
DR ProteomicsDB; 224713; -.
DR EnsemblPlants; AT5G67270.1; AT5G67270.1; AT5G67270.
DR GeneID; 836862; -.
DR Gramene; AT5G67270.1; AT5G67270.1; AT5G67270.
DR KEGG; ath:AT5G67270; -.
DR Araport; AT5G67270; -.
DR TAIR; locus:2157177; AT5G67270.
DR eggNOG; KOG3000; Eukaryota.
DR HOGENOM; CLU_041744_0_1_1; -.
DR InParanoid; Q9FGQ6; -.
DR OMA; EQCGTGG; -.
DR OrthoDB; 1237523at2759; -.
DR PhylomeDB; Q9FGQ6; -.
DR PRO; PR:Q9FGQ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGQ6; baseline and differential.
DR Genevisible; Q9FGQ6; AT.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
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:0008017; F:microtubule binding; ISS: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:0030865; P:cortical cytoskeleton organization; ISS: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 Nucleus; Reference proteome.
FT CHAIN 1..329
FT /note="Microtubule-associated protein RP/EB family member
FT 1C"
FT /id="PRO_0000418412"
FT DOMAIN 13..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 193..263
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576"
FT REGION 130..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..311
FT /note="Required for nuclear localization"
FT COMPBIAS 142..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 289..291
FT /note="KRK->AAA: Loss of targeting to nucleus."
FT /evidence="ECO:0000269|PubMed:20067996"
FT MUTAGEN 309..311
FT /note="RQR->AQA: Loss of targeting to nucleus."
FT /evidence="ECO:0000269|PubMed:20067996"
SQ SEQUENCE 329 AA; 36386 MW; 27115C5E35F619E2 CRC64;
MATNIGMMDS AYFVGRSEIL AWINSTLQLN LSKVEEACSG AVHCQLMDSV HPGTVPMHKV
NFDAKSEYEM IQNYKVLQDV FNKLKITKHI EVSKLVKGRP LDNLEFMQWM KKYCDSVNGG
QHNYHALERR EASKGGKEAT KRAAATQQSG KSSSSSAPPR PSSSNGTRKH EPQSNNTGTH
HSSTGNHHHS SKPSAKQSKP VPAYDEKITE LKLYIDSLEK ERDFYFSKLR DVEILCQNPD
TEHLPLVGSI KRILYAADGE DVGAAETQTL SPIAEGSEER RNSVTESQKR KLIVNLDVDV
AAITTLSPRQ RLSDASDVKC SGSSPLLTC
