ICR5_ARATH
ID ICR5_ARATH Reviewed; 396 AA.
AC Q8VYU8; Q9LFI2;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Interactor of constitutive active ROPs 5;
DE AltName: Full=Protein MICROTUBULE DEPLETION DOMAIN 1;
DE AltName: Full=ROP-interactive partner 3;
GN Name=ICR5; Synonyms=MIDD1, RIP3; OrderedLocusNames=At3g53350;
GN ORFNames=F4P12.50;
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP INTERACTION WITH ARAC11, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825600; DOI=10.1093/mp/ssn051;
RA Li S., Gu Y., Yan A., Lord E., Yang Z.B.;
RT "RIP1 (ROP Interactive Partner 1)/ICR1 marks pollen germination sites and
RT may act in the ROP1 pathway in the control of polarized pollen growth.";
RL Mol. Plant 1:1021-1035(2008).
RN [6]
RP FUNCTION, INTERACTION WITH ARAC4; ARAC11 AND KIN13A, MUTAGENESIS OF ARG-349
RP AND GLN-353, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=20832900; DOI=10.1016/j.ejcb.2010.08.003;
RA Mucha E., Hoefle C., Huckelhoven R., Berken A.;
RT "RIP3 and AtKinesin-13A - a novel interaction linking Rho proteins of
RT plants to microtubules.";
RL Eur. J. Cell Biol. 89:906-916(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20619818; DOI=10.1016/j.cub.2010.05.038;
RA Oda Y., Iida Y., Kondo Y., Fukuda H.;
RT "Wood cell-wall structure requires local 2D-microtubule disassembly by a
RT novel plasma membrane-anchored protein.";
RL Curr. Biol. 20:1197-1202(2010).
RN [8]
RP FUNCTION, INTERACTION WITH ARAC10, AND SUBCELLULAR LOCATION.
RX PubMed=22984069; DOI=10.1126/science.1222597;
RA Oda Y., Fukuda H.;
RT "Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry
RT breaking.";
RL Science 337:1333-1336(2012).
RN [9]
RP INTERACTION WITH KIN13A, FUNCTION, AND SUBUNIT.
RX PubMed=24280391; DOI=10.1105/tpc.113.117853;
RA Oda Y., Fukuda H.;
RT "Rho of plant GTPase signaling regulates the behavior of Arabidopsis
RT kinesin-13A to establish secondary cell wall patterns.";
RL Plant Cell 25:4439-4450(2013).
CC -!- FUNCTION: ROP effector binding specifically activated ROPs and linking
CC them to the microtubule cytoskeleton. Involved in ROP-regulated polar
CC growth. Involved in local disassembly of cortical microtubules when
CC associated with ARAC10 and KIN13A and conversely mediates also the
CC elimination of ARAC10 from the plasma membrane by the cortical
CC microtubules. Accumulates at the plus end of shrinking microtubules.
CC Targets KIN13A to microtubules. {ECO:0000269|PubMed:20619818,
CC ECO:0000269|PubMed:20832900, ECO:0000269|PubMed:22984069,
CC ECO:0000269|PubMed:24280391}.
CC -!- SUBUNIT: Component of the active ARAC10-IRC5-KIN13A complex
CC (PubMed:24280391). Homooligomer. Interacts (via C-terminus) with ARAC4,
CC ARAC10, ARAC11 and (via N-terminus) with KIN13A (via C-terminus), but
CC no interactions with SEC3A. {ECO:0000269|PubMed:19825600,
CC ECO:0000269|PubMed:20832900, ECO:0000269|PubMed:22984069,
CC ECO:0000269|PubMed:24280391}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20619818,
CC ECO:0000269|PubMed:22984069}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20619818, ECO:0000269|PubMed:20832900,
CC ECO:0000269|PubMed:22984069}. Note=In xylem cells, preferentially
CC colocalizes with cortical microtubules located beneath the secondary
CC wall pits (PubMed:20619818). May be associated to the plasma membrane
CC through the interaction with ARAC10 (PubMed:22984069).
CC {ECO:0000269|PubMed:20619818, ECO:0000269|PubMed:22984069}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VYU8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VYU8-2; Sequence=VSP_036032;
CC -!- TISSUE SPECIFICITY: Expressed in xylem cells in the roots and in
CC stamens, petals and pollen. {ECO:0000269|PubMed:20619818}.
CC -!- DOMAIN: The N-terminal part (1-122) is necessary and sufficient for
CC homooligomerization (PubMed:20832900) and for binding to microtubules
CC while the C-terminal domain is anchored to the plasma membrane
CC (PubMed:20619818). {ECO:0000269|PubMed:20619818,
CC ECO:0000269|PubMed:20832900}.
CC -!- SIMILARITY: Belongs to the ICR family. {ECO:0000305}.
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DR EMBL; AL132966; CAB67642.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79072.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79073.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79074.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64278.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64280.1; -; Genomic_DNA.
DR EMBL; AY069906; AAL47457.1; -; mRNA.
DR EMBL; AY113027; AAM47335.1; -; mRNA.
DR EMBL; BX822258; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T45875; T45875.
DR RefSeq; NP_001326318.1; NM_001339615.1. [Q8VYU8-1]
DR RefSeq; NP_001326320.1; NM_001339613.1. [Q8VYU8-1]
DR RefSeq; NP_190903.2; NM_115195.3. [Q8VYU8-1]
DR RefSeq; NP_974423.1; NM_202694.2. [Q8VYU8-2]
DR RefSeq; NP_974424.1; NM_202695.1. [Q8VYU8-2]
DR AlphaFoldDB; Q8VYU8; -.
DR SMR; Q8VYU8; -.
DR BioGRID; 9820; 9.
DR IntAct; Q8VYU8; 7.
DR STRING; 3702.AT3G53350.1; -.
DR PaxDb; Q8VYU8; -.
DR PRIDE; Q8VYU8; -.
DR EnsemblPlants; AT3G53350.1; AT3G53350.1; AT3G53350. [Q8VYU8-1]
DR EnsemblPlants; AT3G53350.2; AT3G53350.2; AT3G53350. [Q8VYU8-2]
DR EnsemblPlants; AT3G53350.3; AT3G53350.3; AT3G53350. [Q8VYU8-2]
DR EnsemblPlants; AT3G53350.5; AT3G53350.5; AT3G53350. [Q8VYU8-1]
DR EnsemblPlants; AT3G53350.7; AT3G53350.7; AT3G53350. [Q8VYU8-1]
DR GeneID; 824503; -.
DR Gramene; AT3G53350.1; AT3G53350.1; AT3G53350. [Q8VYU8-1]
DR Gramene; AT3G53350.2; AT3G53350.2; AT3G53350. [Q8VYU8-2]
DR Gramene; AT3G53350.3; AT3G53350.3; AT3G53350. [Q8VYU8-2]
DR Gramene; AT3G53350.5; AT3G53350.5; AT3G53350. [Q8VYU8-1]
DR Gramene; AT3G53350.7; AT3G53350.7; AT3G53350. [Q8VYU8-1]
DR KEGG; ath:AT3G53350; -.
DR Araport; AT3G53350; -.
DR TAIR; locus:2083951; AT3G53350.
DR eggNOG; ENOG502QT2U; Eukaryota.
DR HOGENOM; CLU_022222_0_0_1; -.
DR InParanoid; Q8VYU8; -.
DR OMA; ARENQIE; -.
DR PhylomeDB; Q8VYU8; -.
DR PRO; PR:Q8VYU8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYU8; baseline and differential.
DR Genevisible; Q8VYU8; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IDA:TAIR.
DR InterPro; IPR029688; ICR.
DR PANTHER; PTHR34224; PTHR34224; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Membrane; Reference proteome.
FT CHAIN 1..396
FT /note="Interactor of constitutive active ROPs 5"
FT /id="PRO_0000356304"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..124
FT /evidence="ECO:0000255"
FT COILED 158..366
FT /evidence="ECO:0000255"
FT VAR_SEQ 65..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036032"
FT MUTAGEN 349
FT /note="R->A: No effect on ROPs binding."
FT /evidence="ECO:0000269|PubMed:20832900"
FT MUTAGEN 353
FT /note="Q->A: Loss of ROPs binding, but no effect on
FT oligomerization."
FT /evidence="ECO:0000269|PubMed:20832900"
FT CONFLICT 120
FT /note="A -> T (in Ref. 3; AAL47457/AAM47335)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="A -> V (in Ref. 4; BX822258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45680 MW; 4A0CE7D68B2C8E70 CRC64;
MQTPKSRPGS LELPQKKSPL PAPKVVRRLK PSGAESDPKT KTISKTQIPK VVADRRSARI
PLNEIQKKRT GRIPELESTI SQLQEELKKA KEELNRSEAL KREAQEEAED AKHQLMDINA
SEDSRIEELR KLSQERDKTW QSELEAMQRQ HGMDSTALSS AINEVQKLKS KLFESESELE
QSKYEVRSLE KLVRQLEEER VNSRDSSSSM EVEELKEAMN LSRQEITQLK SAVEAAETRY
QEEYIQSTLQ IRSAYEQTEA VKSRYSQREA ELTEELNRTK DEIEGLRKEL MEKVKEDEST
GDLKKLESDL MEVRGSLMDK EMELQILRSA MEKKVETANT EAMEAELKRV KIQCEQWRKA
AETAASILNN DEERTDSIET SKMLKKFGVL LKKNHK
