RHON1_ARATH
ID RHON1_ARATH Reviewed; 401 AA.
AC Q94K75; A8MQM6; Q8LFT8; Q9LNC8;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Rho-N domain-containing protein 1, chloroplastic;
DE Flags: Precursor;
GN Name=RHON1; OrderedLocusNames=At1g06190; ORFNames=F9P14.5;
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] (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 1).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNE,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22735703; DOI=10.1093/nar/gks613;
RA Stoppel R., Manavski N., Schein A., Schuster G., Teubner M.,
RA Schmitz-Linneweber C., Meurer J.;
RT "RHON1 is a novel ribonucleic acid-binding protein that supports RNase E
RT function in the Arabidopsis chloroplast.";
RL Nucleic Acids Res. 40:8593-8606(2012).
CC -!- FUNCTION: Binds to and supports processing of specific plastid RNAs.
CC Associates via its C-terminal Rho-N domain to single stranded regions
CC of 16S and 23S rRNAs or to rbcL mRNAs. May be involved in targeting
CC transcripts to RNases such as RNE or RNase J.
CC {ECO:0000269|PubMed:22735703}.
CC -!- SUBUNIT: Homodimer or homomultimer. Part of a chloroplastic
CC degradosome-like complex. Interacts with RNE.
CC {ECO:0000269|PubMed:22735703}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:22735703}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94K75-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94K75-2; Sequence=VSP_045660, VSP_045661;
CC -!- DISRUPTION PHENOTYPE: Smaller and albinotic phenotype. Increased number
CC and decreased size of chloroplasts. Seedling lethal when homozygous.
CC {ECO:0000269|PubMed:22735703}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC025290; AAF80216.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE27956.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27957.1; -; Genomic_DNA.
DR EMBL; AF370238; AAK44053.1; -; mRNA.
DR EMBL; AY062959; AAL33805.1; -; mRNA.
DR EMBL; AY084647; AAM61210.1; -; mRNA.
DR PIR; E86197; E86197.
DR RefSeq; NP_001077466.1; NM_001083997.1. [Q94K75-2]
DR RefSeq; NP_563761.1; NM_100500.4. [Q94K75-1]
DR AlphaFoldDB; Q94K75; -.
DR SMR; Q94K75; -.
DR BioGRID; 22370; 1.
DR STRING; 3702.AT1G06190.1; -.
DR iPTMnet; Q94K75; -.
DR PaxDb; Q94K75; -.
DR PRIDE; Q94K75; -.
DR ProteomicsDB; 236250; -. [Q94K75-1]
DR EnsemblPlants; AT1G06190.1; AT1G06190.1; AT1G06190. [Q94K75-1]
DR EnsemblPlants; AT1G06190.2; AT1G06190.2; AT1G06190. [Q94K75-2]
DR GeneID; 837128; -.
DR Gramene; AT1G06190.1; AT1G06190.1; AT1G06190. [Q94K75-1]
DR Gramene; AT1G06190.2; AT1G06190.2; AT1G06190. [Q94K75-2]
DR KEGG; ath:AT1G06190; -.
DR Araport; AT1G06190; -.
DR TAIR; locus:2038560; AT1G06190.
DR eggNOG; ENOG502T2MX; Eukaryota.
DR HOGENOM; CLU_062947_0_0_1; -.
DR InParanoid; Q94K75; -.
DR OMA; YSEHRIC; -.
DR PhylomeDB; Q94K75; -.
DR PRO; PR:Q94K75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q94K75; baseline and differential.
DR Genevisible; Q94K75; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0019843; F:rRNA binding; IDA:TAIR.
DR GO; GO:0010239; P:chloroplast mRNA processing; IMP:TAIR.
DR GO; GO:1901259; P:chloroplast rRNA processing; IMP:TAIR.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:InterPro.
DR InterPro; IPR011112; Rho_N.
DR Pfam; PF07498; Rho_N; 1.
DR SMART; SM00959; Rho_N; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Coiled coil; Plastid;
KW Reference proteome; RNA-binding; Transit peptide.
FT TRANSIT 1..63
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 64..401
FT /note="Rho-N domain-containing protein 1, chloroplastic"
FT /id="PRO_0000421382"
FT REGION 73..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 339..371
FT /evidence="ECO:0000255"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 276..289
FT /note="EPEHEPAYEHEHEP -> DLSMMLMKIVMKLRKKP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045660"
FT VAR_SEQ 290..401
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_045661"
FT CONFLICT 129
FT /note="R -> I (in Ref. 4; AAM61210)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="S -> L (in Ref. 4; AAM61210)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="E -> D (in Ref. 4; AAM61210)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="E -> K (in Ref. 4; AAM61210)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="G -> S (in Ref. 4; AAM61210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 44530 MW; 00678B72E5107856 CRC64;
MAMSGTFHLT SDYVPGYTLS DSRCFFNSAV SRRTLAILPC SSCLDHKNGR LKSVPNRSSF
VCRASSGGYR RNPDFSRLNK HGYRGNNRQS GGREDFDIEN SDMLSSRNGP LFNLSSSPKF
QATSSPGPRE KEIVELFRKV QAQLRARAAA KKEEKKIEEA SKGQGKESET VDSLLKLLRK
HSGEQSKRQV SKFSSQGEVQ GDTVDKQDRT GNLVTSGNKD NNASSFTRPT SSFRRKSPVP
RSQSPPAYSS EATFDQSSSY SVTWTQKKDT VELHDEPEHE PAYEHEHEPE NESEPGPVTT
MLEPDSELKP ESSSFYQEEE DDDVTFDVLS QDDGILDVLS DDDESLDDAD EDSDEAEEEA
VKDLSELKLV ELRGIAKSRG LKGLSKMKKA ELVELLGSDS S
