R7SL1_ARATH
ID R7SL1_ARATH Reviewed; 275 AA.
AC Q9ZT95;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Ubiquitin domain-containing protein 7SL RNA1 {ECO:0000305|PubMed:7688456};
DE Short=At7SL-1 {ECO:0000303|PubMed:7688456};
GN Name=7SL1 {ECO:0000303|PubMed:7688456};
GN OrderedLocusNames=At4g02970 {ECO:0000312|Araport:AT4G02970};
GN ORFNames=T4I9.15 {ECO:0000312|EMBL:AAC79109.1},
GN T4I9.17 {ECO:0000312|EMBL:CAB77782.1};
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] (ISOFORM 1).
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 [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 [3]
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 [4]
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ZQZ6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZT95-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZT95-2; Sequence=VSP_059158;
CC -!- MISCELLANEOUS: Transcribed by RNA polymerase III (pol III).
CC {ECO:0000269|PubMed:15960619}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; X72228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF069442; AAC79109.1; -; Genomic_DNA.
DR EMBL; AL161495; CAB77782.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82255.1; -; Genomic_DNA.
DR PIR; T01396; T01396.
DR RefSeq; NP_192206.1; NM_116531.1. [Q9ZT95-2]
DR AlphaFoldDB; Q9ZT95; -.
DR SMR; Q9ZT95; -.
DR PaxDb; Q9ZT95; -.
DR PeptideAtlas; Q9ZT95; -.
DR PRIDE; Q9ZT95; -.
DR EnsemblPlants; AT4G02970.1; AT4G02970.1; AT4G02970. [Q9ZT95-2]
DR GeneID; 828121; -.
DR Gramene; AT4G02970.1; AT4G02970.1; AT4G02970. [Q9ZT95-2]
DR KEGG; ath:AT4G02970; -.
DR Araport; AT4G02970; -.
DR TAIR; locus:2139375; AT4G02970.
DR HOGENOM; CLU_085519_1_0_1; -.
DR InParanoid; Q9ZT95; -.
DR OrthoDB; 1262441at2759; -.
DR PhylomeDB; Q9ZT95; -.
DR PRO; PR:Q9ZT95; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZT95; baseline.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 3: Inferred from homology;
KW Alternative splicing; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..275
FT /note="Ubiquitin domain-containing protein 7SL RNA1"
FT /id="PRO_0000442012"
FT DOMAIN 1..53
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 185..263
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 74..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 235..274
FT /note="VSSELPLTETKSFKWNRVADGDTIEIIRRLVPFCSLLFSH -> LGLGSSET
FT CPHQNRSEEPNQCPTILMSPHGLQAIV (in isoform 2)"
FT /id="VSP_059158"
SQ SEQUENCE 275 AA; 31245 MW; 3D5E2DF017E0EE6A CRC64;
MNVYIDTETG SSFSITIDFG ETVLEIKEKI EKSQGIPVSK QILYLDGKAL EDDLHKIDYM
ILFESRLLLR ISPDADPNQS NEQTEQSKQI DDKKQEFCGI QDSSESKKIT RVMARRVHNI
YSSLPAYSLD ELLGPKYSAT VAVGGRTNQV VQPTEQASTS GTAKEVLRDS DSPVEKKIKT
NPMKFTVHVK PYQEDTRMIH VEVNADDNVE ELRKELVKMQ ERGELNLPHE AFHLVSSELP
LTETKSFKWN RVADGDTIEI IRRLVPFCSL LFSHT
