ICR3_ARATH
ID ICR3_ARATH Reviewed; 564 AA.
AC Q9LSS5; Q0WQ47;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Interactor of constitutive active ROPs 3;
DE AltName: Full=ROP-interactive partner 5;
GN Name=ICR3; Synonyms=RIP5; OrderedLocusNames=At5g60210; ORFNames=F15L12.15;
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] OF 22-564.
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=15010618; DOI=10.1023/b:plan.0000019063.18097.62;
RA Hu W., Wang Y., Bowers C., Ma H.;
RT "Isolation, sequence analysis, and expression studies of florally expressed
RT cDNAs in Arabidopsis.";
RL Plant Mol. Biol. 53:545-563(2003).
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).
CC -!- FUNCTION: Acts as a scaffold, mediating interaction of ROPs with
CC different proteins. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARAC11 in vitro. {ECO:0000269|PubMed:19825600}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:15010618}.
CC -!- SIMILARITY: Belongs to the ICR family. {ECO:0000305}.
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DR EMBL; AB026632; BAA97502.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97293.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97294.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70940.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70941.1; -; Genomic_DNA.
DR EMBL; AK228858; BAF00752.1; -; mRNA.
DR RefSeq; NP_001190579.1; NM_001203650.2.
DR RefSeq; NP_001318845.1; NM_001345401.1.
DR RefSeq; NP_001332510.1; NM_001345403.1.
DR RefSeq; NP_200829.5; NM_125414.6.
DR AlphaFoldDB; Q9LSS5; -.
DR SMR; Q9LSS5; -.
DR BioGRID; 21387; 1.
DR STRING; 3702.AT5G60210.1; -.
DR iPTMnet; Q9LSS5; -.
DR PaxDb; Q9LSS5; -.
DR PRIDE; Q9LSS5; -.
DR EnsemblPlants; AT5G60210.1; AT5G60210.1; AT5G60210.
DR EnsemblPlants; AT5G60210.2; AT5G60210.2; AT5G60210.
DR EnsemblPlants; AT5G60210.4; AT5G60210.4; AT5G60210.
DR EnsemblPlants; AT5G60210.6; AT5G60210.6; AT5G60210.
DR GeneID; 836143; -.
DR Gramene; AT5G60210.1; AT5G60210.1; AT5G60210.
DR Gramene; AT5G60210.2; AT5G60210.2; AT5G60210.
DR Gramene; AT5G60210.4; AT5G60210.4; AT5G60210.
DR Gramene; AT5G60210.6; AT5G60210.6; AT5G60210.
DR KEGG; ath:AT5G60210; -.
DR Araport; AT5G60210; -.
DR TAIR; locus:2144040; AT5G60210.
DR eggNOG; ENOG502QT2U; Eukaryota.
DR HOGENOM; CLU_022222_0_0_1; -.
DR InParanoid; Q9LSS5; -.
DR OMA; KESKEQC; -.
DR PhylomeDB; Q9LSS5; -.
DR PRO; PR:Q9LSS5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSS5; baseline and differential.
DR Genevisible; Q9LSS5; AT.
DR InterPro; IPR029688; ICR.
DR PANTHER; PTHR34224; PTHR34224; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..564
FT /note="Interactor of constitutive active ROPs 3"
FT /id="PRO_0000356303"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 70..133
FT /evidence="ECO:0000255"
FT COILED 231..514
FT /evidence="ECO:0000255"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZQC5"
SQ SEQUENCE 564 AA; 63712 MW; 18A9F64BA991F2C9 CRC64;
MQTQKARNGS PDVPKKVSPR AARPLKIAAL EPESSSSPIS ATNRTPKDKS PNVLNRRSPR
SPVSEKKRPS RITELELLVS QLQEELKKAK DQISVSETSK KQAEQEAEES RKQLQEVSSK
LEESQNQFVE TSALEEETDK TGSLVFQSVS QECDWEFSAT AGERAGLAAV AHEIRQLKLQ
IEMVASSEAG HVKQAELYNS EVQLLRGNLM DTLFHVENFR NQLKDCEISE AETEALATET
LRQLENAKKA VEELKSDGTK AVESYKKMAV ELEQSKSRMV WLEALVNKLQ NNPADLENHE
ILLKDYESLR RGESNEMDEE VSSLRCEVER LRAALEASDK KDQEGNVEAS SRLRIQAELQ
SELKIAKSEI DELKARLMDK ETELQFISEE RDNFSMKLMK NQKEIDVEAE LKKLREAIEN
LKADLMDKET ELQIVSDENE TLKSDIHKSE TDVQDAFLKL GIAMEEADKS SKKAVRVTEQ
LEATQASNSE METELRKLKV QSNQWRKAAE AATAMLSAGN NGKFAENYNQ TNSPYSEDID
DELTKKKNGN VLKKIGVLWK KPQK
