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Microtubule-associated protein RP/EB family member 1C (APC-binding protein EB1C) (End-binding protein 1C) (AtEB1C) (Protein ATEB1 homolog 1) (AtEB1H1)

 EB1C_ARATH              Reviewed;         329 AA.
Q9FGQ6;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-JUL-2017, entry version 99.
RecName: Full=Microtubule-associated protein RP/EB family member 1C;
AltName: Full=APC-binding protein EB1C;
AltName: Full=End-binding protein 1C;
Short=AtEB1C;
AltName: Full=Protein ATEB1 homolog 1;
Short=AtEB1H1;
Name=EB1C; OrderedLocusNames=At5g67270; ORFNames=K3G17.3;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19825573; DOI=10.1093/mp/ssn026;
Cheung A.Y., Duan Q.H., Costa S.S., de Graaf B.H., Di Stilio V.S.,
Feijo J., Wu H.M.;
"The dynamic pollen tube cytoskeleton: live cell studies using actin-
binding and microtubule-binding reporter proteins.";
Mol. Plant 1:686-702(2008).
[7]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=18281505; DOI=10.1105/tpc.107.056846;
Bisgrove S.R., Lee Y.R., Liu B., Peters N.T., Kropf D.L.;
"The microtubule plus-end binding protein EB1 functions in root
responses to touch and gravity signals in Arabidopsis.";
Plant Cell 20:396-410(2008).
[8]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
MUTAGENESIS OF 289-LYS--LYS-291 AND 309-ARG--ARG-311, AND DISRUPTION
PHENOTYPE.
PubMed=20067996; DOI=10.1242/jcs.062703;
Komaki S., Abe T., Coutuer S., Inze D., Russinova E., Hashimoto T.;
"Nuclear-localized subtype of end-binding 1 protein regulates spindle
organization in Arabidopsis.";
J. Cell Sci. 123:451-459(2010).
[9]
SUBCELLULAR LOCATION.
PubMed=21873565; DOI=10.1105/tpc.110.078204;
Ho C.M., Hotta T., Guo F., Roberson R.W., Lee Y.R., Liu B.;
"Interaction of antiparallel microtubules in the phragmoplast is
mediated by the microtubule-associated protein MAP65-3 in
Arabidopsis.";
Plant Cell 23:2909-2923(2011).
-!- FUNCTION: Plant-specific EB1 subtype that functions preferentially
at early stages of plant mitosis by regulating spindle positioning
and chromosome segregation. Accumulates in the prophase nucleus
and is required to maintain spindle bipolarity during premetaphase
and/or metaphase and for efficient segregation of chromosomes at
anaphase. May play a role in the dynamics of microtubule network
in elongating pollen tubes. {ECO:0000269|PubMed:19825573,
ECO:0000269|PubMed:20067996}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20067996}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
Cytoplasm, cytoskeleton, phragmoplast. Note=During mitosis,
accumulates in the prophase nucleus, and after the nuclear
envelope disintegration is associated with whole spindle
microtubules, plus end of microtubules, phragmoplast and finally
is actively recruited to the nucleus. Localizes in the microtubule
network in elongating pollen tubes.
-!- TISSUE SPECIFICITY: Highly expressed in the root and shoot
meristems, in guard cells of leaf stomata, pollen grains and
pollen tubes. {ECO:0000269|PubMed:20067996}.
-!- DOMAIN: Composed of two functionally independent domains. The N-
terminal domain forms a hydrophobic cleft involved in microtubule
binding and the C-terminal is involved in protein binding. In
Arabidopsis thaliana, EB1A and EB1B possess an acidic C-terminal
tail that has autoinhibitory function, but EB1C has a tail region
with patches of basic amino acid residues required for nuclear
targeting.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but seedlings show increased sensitivity to oryzalin,
a microtubule-destabilizing agent. conditions.
{ECO:0000269|PubMed:18281505, ECO:0000269|PubMed:20067996}.
-!- MISCELLANEOUS: Plant microtubules behave differently from those of
other eukaryotes in mitosis: they lack centrosomes and spindles
are barrel-shaped with unfocused poles and no astral microtubules.
{ECO:0000305|PubMed:18281505}.
-!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB025614; BAB09646.1; -; Genomic_DNA.
EMBL; CP002688; AED98323.1; -; Genomic_DNA.
EMBL; AK175495; BAD43258.1; -; mRNA.
EMBL; BT028930; ABI49477.1; -; mRNA.
EMBL; AY087775; AAM65311.1; -; mRNA.
RefSeq; NP_201528.1; NM_126127.4.
UniGene; At.28817; -.
ProteinModelPortal; Q9FGQ6; -.
SMR; Q9FGQ6; -.
BioGrid; 22104; 3.
STRING; 3702.AT5G67270.1; -.
iPTMnet; Q9FGQ6; -.
PaxDb; Q9FGQ6; -.
EnsemblPlants; AT5G67270.1; AT5G67270.1; AT5G67270.
GeneID; 836862; -.
Gramene; AT5G67270.1; AT5G67270.1; AT5G67270.
KEGG; ath:AT5G67270; -.
Araport; AT5G67270; -.
TAIR; locus:2157177; AT5G67270.
eggNOG; KOG3000; Eukaryota.
eggNOG; COG5217; LUCA.
HOGENOM; HOG000198048; -.
InParanoid; Q9FGQ6; -.
KO; K10436; -.
OMA; CQVFDSI; -.
OrthoDB; EOG09360IOF; -.
PhylomeDB; Q9FGQ6; -.
PRO; PR:Q9FGQ6; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FGQ6; baseline and differential.
Genevisible; Q9FGQ6; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005730; C:nucleolus; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0005819; C:spindle; IDA:TAIR.
GO; GO:0008017; F:microtubule binding; ISS:TAIR.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030865; P:cortical cytoskeleton organization; ISS:TAIR.
GO; GO:0009652; P:thigmotropism; IMP:TAIR.
Gene3D; 1.10.418.10; -; 1.
InterPro; IPR001715; CH-domain.
InterPro; IPR004953; EB1_C.
InterPro; IPR027328; MAPRE.
PANTHER; PTHR10623; PTHR10623; 1.
Pfam; PF00307; CH; 1.
Pfam; PF03271; EB1; 1.
SUPFAM; SSF140612; SSF140612; 1.
SUPFAM; SSF47576; SSF47576; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS51230; EB1_C; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton;
Microtubule; Mitosis; Nucleus; Reference proteome.
CHAIN 1 329 Microtubule-associated protein RP/EB
family member 1C.
/FTId=PRO_0000418412.
DOMAIN 13 115 Calponin-homology. {ECO:0000255|PROSITE-
ProRule:PRU00044}.
DOMAIN 193 263 EB1 C-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00576}.
REGION 289 311 Required for nuclear localization.
MUTAGEN 289 291 KRK->AAA: Loss of targeting to nucleus.
{ECO:0000269|PubMed:20067996}.
MUTAGEN 309 311 RQR->AQA: Loss of targeting to nucleus.
{ECO:0000269|PubMed:20067996}.
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


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