REIL1_ARATH
ID REIL1_ARATH Reviewed; 404 AA.
AC Q8H1G5; O49591; Q56ZP6; Q94K64;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cytoplasmic 60S subunit biogenesis factor REI1 homolog 1 {ECO:0000305};
DE AltName: Full=Protein REI1-LIKE 1 {ECO:0000303|PubMed:24038679};
DE AltName: Full=pre-60S factor REI1 homolog 1 {ECO:0000305};
GN Name=REIL1 {ECO:0000303|PubMed:24038679};
GN OrderedLocusNames=At4g31420 {ECO:0000312|Araport:AT4G31420};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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] OF 251-404.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24038679; DOI=10.1104/pp.113.223925;
RA Schmidt S., Dethloff F., Beine-Golovchuk O., Kopka J.;
RT "The REIL1 and REIL2 proteins of Arabidopsis thaliana are required for leaf
RT growth in the cold.";
RL Plant Physiol. 163:1623-1639(2013).
RN [6]
RP SUBUNIT, AND INTERACTION WITH RLP24; RPL24A; RPL24B; EBP1 AND JJJ1.
RX PubMed=24603461; DOI=10.4161/psb.28224;
RA Schmidt S., Dethloff F., Beine-Golovchuk O., Kopka J.;
RT "REIL proteins of Arabidopsis thaliana interact in yeast-2-hybrid assays
RT with homologs of the yeast Rlp24, Rpl24A, Rlp24B, Arx1, and Jjj1
RT proteins.";
RL Plant Signal. Behav. 9:E28224-E28224(2014).
CC -!- FUNCTION: Pre-60S-associated factor involved in the cytoplasmic
CC maturation of the 60S subunit. Involved in the dissociation and
CC recycling of other late pre-60S factors before newly synthesized large
CC ribosomal subunits enter translation (By similarity). Can complement
CC the growth defect of a yeast mutant lacking REI1 (PubMed:24038679).
CC Required for leaf growth under cold temperature conditions
CC (PubMed:24038679). {ECO:0000250|UniProtKB:P38344,
CC ECO:0000269|PubMed:24038679}.
CC -!- SUBUNIT: Can form homodimer. Interacts with RLP24, RPL24A, RPL24B, EBP1
CC and JJJ1. {ECO:0000269|PubMed:24603461}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q8H1G5-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. When grown at 10 degrees Celsius, the double mutant
CC seedlings reil1-1 and reil2-1 show growth arrest at two cotyledon stage
CC and die. {ECO:0000269|PubMed:24038679}.
CC -!- SIMILARITY: Belongs to the REI1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA16545.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79860.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021633; CAA16545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161579; CAB79860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85908.1; -; Genomic_DNA.
DR EMBL; AF370269; AAK44084.1; -; mRNA.
DR EMBL; AY150375; AAN12920.1; -; mRNA.
DR EMBL; AK220917; BAD94371.1; -; mRNA.
DR PIR; T04509; T04509.
DR RefSeq; NP_567875.1; NM_119291.5. [Q8H1G5-1]
DR AlphaFoldDB; Q8H1G5; -.
DR IntAct; Q8H1G5; 3.
DR STRING; 3702.AT4G31420.2; -.
DR iPTMnet; Q8H1G5; -.
DR PaxDb; Q8H1G5; -.
DR PRIDE; Q8H1G5; -.
DR ProteomicsDB; 234914; -. [Q8H1G5-1]
DR EnsemblPlants; AT4G31420.1; AT4G31420.1; AT4G31420. [Q8H1G5-1]
DR GeneID; 829269; -.
DR Gramene; AT4G31420.1; AT4G31420.1; AT4G31420. [Q8H1G5-1]
DR KEGG; ath:AT4G31420; -.
DR Araport; AT4G31420; -.
DR eggNOG; KOG2785; Eukaryota.
DR OMA; WSHIMHA; -.
DR PhylomeDB; Q8H1G5; -.
DR PRO; PR:Q8H1G5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8H1G5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:UniProtKB.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR InterPro; IPR040025; Znf622/Rei1/Reh1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR13182; PTHR13182; 1.
DR Pfam; PF12756; zf-C2H2_2; 1.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Reference proteome; Repeat;
KW Ribosome biogenesis; Zinc; Zinc-finger.
FT CHAIN 1..404
FT /note="Cytoplasmic 60S subunit biogenesis factor REI1
FT homolog 1"
FT /id="PRO_0000435443"
FT ZN_FING 4..28
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 68..92
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 178..201
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255"
FT ZN_FING 229..256
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255"
FT REGION 119..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 48
FT /note="E -> G (in Ref. 3; AAK44084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45998 MW; C4A1CB19DA516AD2 CRC64;
MPGLTCNACN MEFKDEEERN LHYKSDWHRY NLKRKVAGVP GVTEALFEAR QSALAQEKNK
SNEAPMLYTC AICAKGYRSS KAHEQHLQSR SHVLRVSQGT SINGEEDIAI IRQLPRRVQH
RGSIDDDSED EWVEVDSDEE LAAEEASDSL SKLNVNESGS AEDMDDDGDA DKYELDPTCC
LMCDKKHKTL ESCMLHMHKH HGFFIPDIEY LKDPEGLLTY LGLKVKRDFM CLYCNELCRP
FSSLEAVRKH MEAKSHCKLH YGDGDDEEDA ELEEFYDYSS SYVDEAGKQI VVSGETDNTV
ELVGGSELLI TEKSENTTTS KTLGSREFMR YYRQKPRPTS QDSNQIIASL SSRYKSLGLK
TVPSKEETLR MKVRKEMSKR GETMRTKIGV KSNVIRNLPN NVPY
