ICR1_ARATH
ID ICR1_ARATH Reviewed; 344 AA.
AC Q8LE98; Q0WP02; Q29Q29;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Interactor of constitutive active ROPs 1;
DE AltName: Full=ROP-interactive partner 1;
GN Name=ICR1; Synonyms=RIP1; OrderedLocusNames=At1g17140;
GN ORFNames=F20D23.32, F20D23_31;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP IDENTIFICATION, FUNCTION, MUTAGENESIS OF 78-GLN--LEU-81; GLN-265;
RP 265-GLN--ALA-270 AND ALA-270, INTERACTION WITH ARAC3; ARAC8; SEC3A; ICR2
RP AND EXO70A1, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=17493810; DOI=10.1016/j.cub.2007.04.038;
RA Lavy M., Bloch D., Hazak O., Gutman I., Poraty L., Sorek N., Sternberg H.,
RA Yalovsky S.;
RT "A Novel ROP/RAC effector links cell polarity, root-meristem maintenance,
RT and vesicle trafficking.";
RL Curr. Biol. 17:947-952(2007).
RN [7]
RP FUNCTION, INTERACTION WITH ARAC11, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF 265-GLN-TRP-266; 340-LYS--LYS-344; LYS-341 AND
RP LYS-344, 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 [8]
RP INTERACTION WITH SEC3A; ARAC4 AND ARAC11.
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY AUXIN, AND SUBCELLULAR LOCATION.
RX PubMed=20098722; DOI=10.1371/journal.pbio.1000282;
RA Hazak O., Bloch D., Poraty L., Sternberg H., Zhang J., Friml J.,
RA Yalovsky S.;
RT "A rho scaffold integrates the secretory system with feedback mechanisms in
RT regulation of auxin distribution.";
RL PLoS Biol. 8:E1000282-E1000282(2010).
CC -!- FUNCTION: Acts as a scaffold, mediating interaction of ROPs with
CC different proteins. Required for primary and adventitious root
CC maintenance, but not for their formation. Promotes the stabilization of
CC ARAC11 on the plasma membrane of the pollen tube initiation site but
CC not the activation of ARAC11. Regulates directionality of polar auxin
CC transport, and is required for the formation of a stable auxin maximum
CC and tip localized auxin gradient during embryogenesis, organogenesis,
CC and meristem activity. Involved in exocytosis and in the recycling of
CC PIN proteins back to the plasma membrane. {ECO:0000269|PubMed:17493810,
CC ECO:0000269|PubMed:19825600, ECO:0000269|PubMed:20098722}.
CC -!- SUBUNIT: Homooligomer. Interacts with ARAC3, ARAC4, ARAC8, ARAC11 and
CC SEC3A, but not with ICR2 or EXO70A1. {ECO:0000269|PubMed:17493810,
CC ECO:0000269|PubMed:19825600, ECO:0000269|PubMed:20832900}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17493810,
CC ECO:0000269|PubMed:20098722}; Peripheral membrane protein. Nucleus
CC {ECO:0000269|PubMed:19825600}. Note=The localization of the ICR1-ROP
CC complexes at the plasma membrane depend on the lipid modifications of
CC the ROPs (PubMed:17493810). Localized in the nuclei in mature pollen,
CC then shifts to the site of germination and stays at the apical cortex
CC of growing pollen tubes (PubMed:19825600).
CC {ECO:0000269|PubMed:17493810, ECO:0000269|PubMed:19825600}.
CC -!- TISSUE SPECIFICITY: Expressed in mature and germinating pollen
CC (PubMed:19825600). Expressed throughout the embryo but not in the
CC hypophysis and quiescent center (QC). In roots, absent from the QC and
CC the stem cells (PubMed:20098722). {ECO:0000269|PubMed:19825600,
CC ECO:0000269|PubMed:20098722}.
CC -!- INDUCTION: Up-regulated by auxin. {ECO:0000269|PubMed:20098722}.
CC -!- DOMAIN: Interactions with ROPs and SEC3A require an intact C-terminal
CC coiled-coil domain.
CC -!- DISRUPTION PHENOTYPE: Plants have cubical adaxial epidermal pavement
CC cells and show a loss of root stem-cell population due to a colapse of
CC the root meristem. Pollen development is also compromised.
CC {ECO:0000269|PubMed:17493810}.
CC -!- SIMILARITY: Belongs to the ICR family. {ECO:0000305}.
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DR EMBL; AC007651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE29547.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29548.1; -; Genomic_DNA.
DR EMBL; AY085543; AAM62767.1; -; mRNA.
DR EMBL; BT024727; ABD59065.1; -; mRNA.
DR EMBL; AK229284; BAF01147.1; -; mRNA.
DR RefSeq; NP_564015.1; NM_101574.3.
DR RefSeq; NP_973848.1; NM_202119.2.
DR AlphaFoldDB; Q8LE98; -.
DR SMR; Q8LE98; -.
DR BioGRID; 23524; 7.
DR STRING; 3702.AT1G17140.1; -.
DR iPTMnet; Q8LE98; -.
DR PaxDb; Q8LE98; -.
DR PRIDE; Q8LE98; -.
DR ProteomicsDB; 228767; -.
DR EnsemblPlants; AT1G17140.1; AT1G17140.1; AT1G17140.
DR EnsemblPlants; AT1G17140.2; AT1G17140.2; AT1G17140.
DR GeneID; 838284; -.
DR Gramene; AT1G17140.1; AT1G17140.1; AT1G17140.
DR Gramene; AT1G17140.2; AT1G17140.2; AT1G17140.
DR KEGG; ath:AT1G17140; -.
DR Araport; AT1G17140; -.
DR TAIR; locus:2020342; AT1G17140.
DR eggNOG; ENOG502QVSP; Eukaryota.
DR HOGENOM; CLU_043733_1_0_1; -.
DR InParanoid; Q8LE98; -.
DR OMA; VMMLVRT; -.
DR OrthoDB; 1223458at2759; -.
DR PhylomeDB; Q8LE98; -.
DR PRO; PR:Q8LE98; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LE98; baseline and differential.
DR Genevisible; Q8LE98; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0090404; C:pollen tube tip; IDA:TAIR.
DR GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR.
DR InterPro; IPR029688; ICR.
DR PANTHER; PTHR34224; PTHR34224; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Membrane; Nucleus; Reference proteome.
FT CHAIN 1..344
FT /note="Interactor of constitutive active ROPs 1"
FT /id="PRO_0000220596"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..108
FT /evidence="ECO:0000255"
FT COILED 145..273
FT /evidence="ECO:0000255"
FT COMPBIAS 12..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 78..81
FT /note="Missing: Loss of oligomerization."
FT /evidence="ECO:0000269|PubMed:17493810"
FT MUTAGEN 265..270
FT /note="Missing: Loss of oligomerization, loss of
FT interaction with ROPs and loss of plasma membrane
FT localization."
FT /evidence="ECO:0000269|PubMed:17493810"
FT MUTAGEN 265
FT /note="Q->P: No visible phenotype; when associated with P-
FT 270."
FT /evidence="ECO:0000269|PubMed:17493810"
FT MUTAGEN 265
FT /note="Q->R: Loss of plasma membrane localization, but
FT stays in the nucleus; when associated with G-266."
FT /evidence="ECO:0000269|PubMed:17493810"
FT MUTAGEN 266
FT /note="W->G: Loss of plasma membrane localization, but
FT stays in the nucleus; when associated with R-265."
FT MUTAGEN 270
FT /note="A->P: No visible phenotype; when associated with P-
FT 265."
FT /evidence="ECO:0000269|PubMed:17493810"
FT MUTAGEN 340..344
FT /note="Missing: No effect on interaction with ROPs but loss
FT of plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:19825600"
FT MUTAGEN 341
FT /note="K->E: Localization greatly shifted to the cytosol;
FT when associated with E-344."
FT /evidence="ECO:0000269|PubMed:19825600"
FT MUTAGEN 344
FT /note="K->E: No effect on the plasma membrane localization,
FT but decreased growth depolarization. Localization greatly
FT shifted to the cytosol; when associated with E-341."
FT /evidence="ECO:0000269|PubMed:19825600"
FT CONFLICT 125
FT /note="I -> V (in Ref. 5; BAF01147)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38358 MW; 84B92E14C9FB2861 CRC64;
MPRPRVSELS QRQAPRLRSS SSTSDSNHSN RLITTDQSFK PGVDRKSPRS GGPNSDPLGQ
KKLGGRISDL ESQLGQAQEE LRLLKEQLAN AEAVKKQAQD ELHKKSKKPN PLARVEESAT
EAERIDRDEI PGDVQKETDV FEVPVEKIAV EEEELRSGND EAEKLVAKED EIKMLKARLY
DMEKEHESLG KENESLKNQL SDSASEISNV KANEDEMVSK VSRIGEELEE SRAKTAHLKE
KLESMEEAKD ALEAEMKKLR VQTEQWRKAA DAAAAVLSGE FEMNGRDRSG STEKYYAGGF
FDPSAGFMDP PGMADDYDDG LGSGKRKSSG MKMFGELWRK KGQK
