ID   RIN1_ARATH              Reviewed;         458 AA.
AC   Q9FMR9;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=RuvB-like protein 1;
DE            EC=3.6.4.12;
DE   AltName: Full=49 kDa TATA box-binding protein-interacting protein homolog;
DE            Short=AtTIP49a;
DE   AltName: Full=Ruv DNA-helicase-like protein;
GN   Name=RIN1; Synonyms=RVB1, TIP49a; OrderedLocusNames=At5g22330;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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;
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].
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   [5]
RP   INTERACTION WITH RPM1 AND RPP5, AND DISRUPTION PHENOTYPE.
RX   PubMed=12062092; DOI=10.1016/s1534-5807(02)00174-0;
RA   Holt B.F. III, Boyes D.C., Ellerstroem M., Siefers N., Wiig A.,
RA   Kauffman S., Grant M.R., Dangl J.L.;
RT   "An evolutionarily conserved mediator of plant disease resistance gene
RT   function is required for normal Arabidopsis development.";
RL   Dev. Cell 2:807-817(2002).
RN   [6]
RP   INTERACTION WITH FLX; FES1 AND FRI.
RX   PubMed=21282526; DOI=10.1105/tpc.110.075911;
RA   Choi K., Kim J., Hwang H.J., Kim S., Park C., Kim S.Y., Lee I.;
RT   "The FRIGIDA complex activates transcription of FLC, a strong flowering
RT   repressor in Arabidopsis, by recruiting chromatin modification factors.";
RL   Plant Cell 23:289-303(2011).
CC   -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC       complex which is involved in transcriptional regulation, DNA
CC       replication and probably DNA repair. Component of the NuA4 histone
CC       acetyltransferase complex which is involved in transcriptional
CC       activation of select genes principally by acetylation of nucleosomal
CC       histones H4 and H2A. Has single-stranded DNA-stimulated ATPase and ATP-
CC       dependent DNA helicase (3' to 5') activity suggesting a role in nuclear
CC       processes such as recombination and transcription (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with FRI, and with FLX and FES1, two component of
CC       the transcription activator complex FRI-C. Interacts with the disease
CC       resistance genes RPM1 and RPP5. {ECO:0000269|PubMed:12062092,
CC       ECO:0000269|PubMed:21282526}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Gametophyte lethality.
CC       {ECO:0000269|PubMed:12062092}.
CC   -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
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DR   EMBL; AB007651; BAB08331.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93012.1; -; Genomic_DNA.
DR   EMBL; BT000923; AAN41323.1; -; mRNA.
DR   EMBL; AY084606; AAM61170.1; -; mRNA.
DR   RefSeq; NP_197625.1; NM_122138.3.
DR   AlphaFoldDB; Q9FMR9; -.
DR   SMR; Q9FMR9; -.
DR   BioGRID; 17568; 101.
DR   IntAct; Q9FMR9; 1.
DR   STRING; 3702.AT5G22330.1; -.
DR   PaxDb; Q9FMR9; -.
DR   PRIDE; Q9FMR9; -.
DR   ProteomicsDB; 237004; -.
DR   EnsemblPlants; AT5G22330.1; AT5G22330.1; AT5G22330.
DR   GeneID; 832293; -.
DR   Gramene; AT5G22330.1; AT5G22330.1; AT5G22330.
DR   KEGG; ath:AT5G22330; -.
DR   Araport; AT5G22330; -.
DR   TAIR; locus:2176302; AT5G22330.
DR   eggNOG; KOG1942; Eukaryota.
DR   HOGENOM; CLU_028311_1_1_1; -.
DR   InParanoid; Q9FMR9; -.
DR   OMA; VIYVEAN; -.
DR   OrthoDB; 752343at2759; -.
DR   PhylomeDB; Q9FMR9; -.
DR   PRO; PR:Q9FMR9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMR9; baseline and differential.
DR   Genevisible; Q9FMR9; AT.
DR   GO; GO:0031011; C:Ino80 complex; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0097255; C:R2TP complex; IBA:GO_Central.
DR   GO; GO:0000812; C:Swr1 complex; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR   GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR   GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR   GO; GO:0048507; P:meristem development; IMP:TAIR.
DR   GO; GO:1900150; P:regulation of defense response to fungus; IMP:TAIR.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.40.50.360; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR027238; RuvB-like.
DR   InterPro; IPR041048; RuvB-like_C.
DR   InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR   InterPro; IPR010339; TIP49_P-loop.
DR   PANTHER; PTHR11093; PTHR11093; 1.
DR   Pfam; PF06068; TIP49; 1.
DR   Pfam; PF17856; TIP49_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Developmental protein; Differentiation; Flowering; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..458
FT                   /note="RuvB-like protein 1"
FT                   /id="PRO_0000423730"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   458 AA;  50323 MW;  7DA33A99AFFA365F CRC64;
     MEKVKIEEIQ STAKKQRIAT HTHIKGLGLE PTGIPIKLAA GFVGQLEARE AAGLVVDMIK
     QKKMAGKALL LAGPPGTGKT ALALGISQEL GSKVPFCPMV GSEVYSSEVK KTEVLMENFR
     RAIGLRIKET KEVYEGEVTE LSPEETESLT GGYGKSISHV VITLKTVKGT KHLKLDPTIY
     DALIKEKVAV GDVIYIEANS GAVKRVGRSD AFATEFDLEA EEYVPLPKGE VHKKKEIVQD
     VTLQDLDAAN ARPQGGQDIL SLMGQMMKPR KTEITDKLRQ EINKVVNRYI DEGVAELVPG
     VLFIDEVHML DMECFSYLNR ALESSLSPIV IFATNRGVCN VRGTDMPSPH GVPIDLLDRL
     VIIRTQIYDP SEMIQIIAIR AQVEELTVDE ECLVLLGEIG QRTSLRHAVQ LLSPASIVAK
     MNGRDNICKA DIEEVTSLYL DAKSSAKLLH EQQEKYIS