RSSA1_ARATH
ID RSSA1_ARATH Reviewed; 298 AA.
AC Q08682; Q93V81;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 3.
DT 25-MAY-2022, entry version 166.
DE RecName: Full=40S ribosomal protein Sa-1;
DE AltName: Full=Laminin receptor homolog;
DE AltName: Full=p40;
GN Name=RPSaA; OrderedLocusNames=At1g72370; ORFNames=T10D10.16;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8208855; DOI=10.1104/pp.103.1.299;
RA Axelos M., Bardet C., Lescure B.;
RT "An Arabidopsis cDNA encoding a 33-kilodalton laminin receptor homolog.";
RL Plant Physiol. 103:299-300(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8051176; DOI=10.1016/s0021-9258(17)32055-0;
RA Garcia-Hernandez M., Davies E., Staswick P.E.;
RT "Arabidopsis p40 homologue. A novel acidic protein associated with the 40 S
RT subunit of ribosomes.";
RL J. Biol. Chem. 269:20744-20749(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Scheer I., Axelos M., Pont-Lezica R.F.;
RT "Characterization of a ribosomal p40 homologue gene showing the same
RT pattern of expression as the elongation factor-1 alpha in Arabidopsis
RT thaliana.";
RL Plant Physiol. Biochem. 34:501-508(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9426609; DOI=10.1023/a:1005956601270;
RA Scheer I., Ludevid M.D., Regad F.F., Lescure B., Pont-Lezica R.F.;
RT "Expression of a gene encoding a ribosomal p40 protein and identification
RT of an active promoter site.";
RL Plant Mol. Biol. 35:905-913(1997).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11598216; DOI=10.1104/pp.010265;
RA Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R.,
RA Delseny M., Bailey-Serres J.;
RT "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis
RT genome.";
RL Plant Physiol. 127:398-415(2001).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (25S, 5.8S and 5S). Interacts with ribosomal protein S21.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q08682-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
CC -!- CAUTION: Was originally thought to be a laminin receptor.
CC {ECO:0000305}.
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DR EMBL; X69056; CAA48794.1; -; mRNA.
DR EMBL; U01955; AAA53425.1; -; mRNA.
DR EMBL; X89366; CAA61547.1; -; Genomic_DNA.
DR EMBL; Y10379; CAA71407.1; -; Genomic_DNA.
DR EMBL; AC016529; AAG52587.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35313.1; -; Genomic_DNA.
DR EMBL; AY054211; AAL06872.1; -; mRNA.
DR EMBL; AY058885; AAL24271.1; -; mRNA.
DR EMBL; AY065096; AAL38272.1; -; mRNA.
DR EMBL; AY079041; AAL79591.1; -; mRNA.
DR EMBL; AY114561; AAM47880.1; -; mRNA.
DR EMBL; AY136324; AAM96990.1; -; mRNA.
DR EMBL; BT000421; AAN15740.1; -; mRNA.
DR EMBL; AY087976; AAM65523.1; -; mRNA.
DR PIR; F96747; F96747.
DR PIR; S71247; S71247.
DR RefSeq; NP_177381.1; NM_105896.4. [Q08682-1]
DR AlphaFoldDB; Q08682; -.
DR SMR; Q08682; -.
DR BioGRID; 28789; 10.
DR IntAct; Q08682; 2.
DR MINT; Q08682; -.
DR STRING; 3702.AT1G72370.1; -.
DR iPTMnet; Q08682; -.
DR MetOSite; Q08682; -.
DR PaxDb; Q08682; -.
DR PRIDE; Q08682; -.
DR EnsemblPlants; AT1G72370.1; AT1G72370.1; AT1G72370. [Q08682-1]
DR GeneID; 843569; -.
DR Gramene; AT1G72370.1; AT1G72370.1; AT1G72370. [Q08682-1]
DR KEGG; ath:AT1G72370; -.
DR Araport; AT1G72370; -.
DR TAIR; locus:2193997; AT1G72370.
DR eggNOG; KOG0830; Eukaryota.
DR InParanoid; Q08682; -.
DR OMA; WEGDAEW; -.
DR PhylomeDB; Q08682; -.
DR PRO; PR:Q08682; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q08682; baseline and differential.
DR Genevisible; Q08682; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0042788; C:polysomal ribosome; IDA:CAFA.
DR GO; GO:0015935; C:small ribosomal subunit; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..298
FT /note="40S ribosomal protein Sa-1"
FT /id="PRO_0000134346"
FT REGION 252..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 11..12
FT /note="QL -> HV (in Ref. 1, 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="P -> L (in Ref. 1; CAA48794)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..213
FT /note="EE -> DY (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32291 MW; E5C1A846A30161B6 CRC64;
MATNGSASSA QLSQKEADVR MMCAAEVHLG TKNCNYQMER YVFKRRNDGI YIFNLGKTWE
KLQMAARVIV AIENPQDIIV QSARPYGQRA VLKFAQYTGA NAIAGRHTPG TFTNQMQTSF
SEPRLLILTD PRTDHQPIKE GALGNIPIIA FCDTDSPMRF VDIGIPANNK GKHSIGCLFW
LLARMVLQMR GTIAAGQKWD VMVDLFFYRE PEETKPEDED EAGPQAEYGA LPAPEYGMVG
GDQWTTAQIP DAAWPGEGQA PISAAPAAAS WSDSAAAPAD GGWEAAAPPS GAPAAGWE
