R7SL2_ARATH
ID R7SL2_ARATH Reviewed; 263 AA.
AC Q9ZQZ6; E0Y427;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ubiquitin domain-containing protein 7SL RNA2 {ECO:0000305|PubMed:7688456};
DE Short=At7SL-2 {ECO:0000303|PubMed:7688456};
DE AltName: Full=Protein ETERNALLY VEGETATIVE PHASE 1 {ECO:0000303|PubMed:21624980};
GN Name=7SL2 {ECO:0000303|PubMed:7688456};
GN Synonyms=EVE1 {ECO:0000303|PubMed:21624980};
GN OrderedLocusNames=At4g03350 {ECO:0000312|Araport:AT4G03350};
GN ORFNames=F4C21.29 {ECO:0000312|EMBL:AAD14463.1};
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 [GENOMIC DNA].
RX PubMed=7688456; DOI=10.1093/nar/21.15.3581;
RA Marques J.P., Gualberto J.M., Palme K.;
RT "Sequence of the Arabidopsis thaliana 7SL RNA gene.";
RL Nucleic Acids Res. 21:3581-3581(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Kas-2;
RX PubMed=21037570; DOI=10.1038/ng.704;
RA Alcazar R., Garcia A.V., Kronholm I., de Meaux J., Koornneef M.,
RA Parker J.E., Reymond M.;
RT "Natural variation at strubbelig receptor kinase 3 drives immune-triggered
RT incompatibilities between Arabidopsis thaliana accessions.";
RL Nat. Genet. 42:1135-1139(2010).
RN [3]
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 [4]
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 [5]
RP MISCELLANEOUS.
RX PubMed=15960619; DOI=10.1111/j.1365-313x.2005.02430.x;
RA Yukawa Y., Felis M., Englert M., Stojanov M., Matousek J., Beier H.,
RA Sugiura M.;
RT "Plant 7SL RNA genes belong to type 4 of RNA polymerase III- dependent
RT genes that are composed of mixed promoters.";
RL Plant J. 43:97-106(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21624980; DOI=10.1093/jxb/err168;
RA Hwang H.-J., Kim H., Jeong Y.-M., Choi M.Y., Lee S.-Y., Kim S.-G.;
RT "Overexpression of EVE1, a novel ubiquitin family protein, arrests
RT inflorescence stem development in Arabidopsis.";
RL J. Exp. Bot. 62:4571-4581(2011).
CC -!- FUNCTION: Controls phase transition from the vegetative to the
CC reproductive state. Involved in the maintenance of the shoot apical
CC meristem (SAM) thus preventing inflorescence meristem (IM) formation
CC and subsequent inflorescence stem development during flowering.
CC Regulates leaf and organ morphology. {ECO:0000269|PubMed:21624980}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21624980}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, stems, rosettes and
CC flowers (at protein level). {ECO:0000269|PubMed:21624980}.
CC -!- MISCELLANEOUS: Transcribed by RNA polymerase III (pol III).
CC {ECO:0000269|PubMed:15960619}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=X72229; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X72229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GU571158; ADM21180.1; -; Genomic_DNA.
DR EMBL; AC005275; AAD14463.1; -; Genomic_DNA.
DR EMBL; AL161496; CAB77820.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82309.1; -; Genomic_DNA.
DR PIR; E85042; E85042.
DR RefSeq; NP_192244.1; NM_116573.1.
DR AlphaFoldDB; Q9ZQZ6; -.
DR SMR; Q9ZQZ6; -.
DR STRING; 3702.AT4G03350.1; -.
DR PaxDb; Q9ZQZ6; -.
DR PRIDE; Q9ZQZ6; -.
DR ProteomicsDB; 236481; -.
DR EnsemblPlants; AT4G03350.1; AT4G03350.1; AT4G03350.
DR GeneID; 827964; -.
DR Gramene; AT4G03350.1; AT4G03350.1; AT4G03350.
DR KEGG; ath:AT4G03350; -.
DR Araport; AT4G03350; -.
DR TAIR; locus:2125517; AT4G03350.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_085519_1_0_1; -.
DR InParanoid; Q9ZQZ6; -.
DR OrthoDB; 1262441at2759; -.
DR PhylomeDB; Q9ZQZ6; -.
DR PRO; PR:Q9ZQZ6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZQZ6; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 1: Evidence at protein level;
KW Developmental protein; Flowering; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..263
FT /note="Ubiquitin domain-containing protein 7SL RNA2"
FT /id="PRO_0000442013"
FT DOMAIN 1..53
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 184..263
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 52
FT /note="Missing (in Ref. 2; ADM21180)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="L -> H (in Ref. 2; ADM21180)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="T -> A (in Ref. 2; ADM21180)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29791 MW; A6E3A63A7936166C CRC64;
MNVDIDTETG SSFSITIDFG ETVLQIKEKI EKSQGIPVSK QILYLDGKAL EDDLHKIDYM
ILFESLLLRI SPDADPNQSN EQTEQSKQID DKKQEFCGIQ DSSESKKLTR VMARRVHNVY
SSLPAYSLDE LLGPKYSATV TVGGRTNQVV QTTEQASTSG TAKEVLRDSD SPVEKKIKTN
PMKFTVHVKP YQEDTKMIQV EVNADDNVEE LRKELVKMQE RGELNLPHEA FHLVSSELPL
IETKSFKWNR VADGDTIELI REK
