PSRP2_ARATH
ID PSRP2_ARATH Reviewed; 253 AA.
AC Q8VYM4; B9DG26; Q9SUZ0;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=30S ribosomal protein 2, chloroplastic {ECO:0000303|PubMed:12605670};
DE AltName: Full=Chloroplastic small ribosomal subunit protein cS22 {ECO:0000250|UniProtKB:P82277};
DE AltName: Full=Plastid-specific 30S ribosomal protein 2, chloroplastic {ECO:0000303|PubMed:12605670};
DE Short=PSRP-2 {ECO:0000303|PubMed:12605670};
DE Flags: Precursor;
GN Name=PSRP2 {ECO:0000303|PubMed:12605670};
GN OrderedLocusNames=At3g52150 {ECO:0000312|Araport:AT3G52150};
GN ORFNames=F4F15.260 {ECO:0000312|EMBL:CAB41335.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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].
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12605670; DOI=10.1046/j.1432-1033.2003.03359.x;
RA Yamaguchi K., Subramanian A.R.;
RT "Proteomic identification of all plastid-specific ribosomal proteins in
RT higher plant chloroplast 30S ribosomal subunit.";
RL Eur. J. Biochem. 270:190-205(2003).
RN [6]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=21923745; DOI=10.1111/j.1365-313x.2011.04791.x;
RA Tiller N., Weingartner M., Thiele W., Maximova E., Schoettler M.A.,
RA Bock R.;
RT "The plastid-specific ribosomal proteins of Arabidopsis thaliana can be
RT divided into non-essential proteins and genuine ribosomal proteins.";
RL Plant J. 69:302-316(2012).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION BY ABIOTIC STRESSES.
RC STRAIN=cv. Columbia;
RX PubMed=24220572; DOI=10.1016/j.plaphy.2013.10.027;
RA Xu T., Lee K., Gu L., Kim J.I., Kang H.;
RT "Functional characterization of a plastid-specific ribosomal protein PSRP2
RT in Arabidopsis thaliana under abiotic stress conditions.";
RL Plant Physiol. Biochem. 73:405-411(2013).
CC -!- FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a
CC dedicated translation machinery responsible for the synthesis of
CC chloroplast genome-encoded proteins, including proteins of the
CC transcription and translation machinery and components of the
CC photosynthetic apparatus. May have a role in the recruitment of stored
CC chloroplast mRNAs for active protein synthesis (By similarity). Bind
CC single strand DNA (ssDNA) and RNA in vitro. Exhibits RNA chaperone
CC activity. Regulates negatively resistance responses to abiotic stresses
CC during seed germination (e.g. salt, dehydration, and low temperature)
CC and seedling growth (e.g. salt) (PubMed:24220572).
CC {ECO:0000250|UniProtKB:P82277, ECO:0000269|PubMed:24220572}.
CC -!- SUBUNIT: Component of the chloroplast small ribosomal subunit (SSU).
CC Mature 70S chloroplast ribosomes of higher plants consist of a small
CC (30S) and a large (50S) subunit. The 30S small subunit contains 1
CC molecule of ribosomal RNA (16S rRNA) and 24 different proteins. The 50S
CC large subunit contains 3 rRNA molecules (23S, 5S and 4.5S rRNA) and 33
CC different proteins. {ECO:0000250|UniProtKB:P82277}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:21923745, ECO:0000269|PubMed:24220572}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, stems, flower
CC buds, flowers and leaves. {ECO:0000269|PubMed:24220572}.
CC -!- INDUCTION: Down-regulated under cold, salt and dehydration stress
CC conditions. {ECO:0000269|PubMed:24220572}.
CC -!- DISRUPTION PHENOTYPE: No detectable effects on ribosome biogenesis and
CC translation in normal conditions (PubMed:21923745). Better seedling
CC growth under salt stress conditions (PubMed:24220572).
CC {ECO:0000269|PubMed:21923745, ECO:0000269|PubMed:24220572}.
CC -!- SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cS22
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41335.1; Type=Erroneous gene model prediction; Note=The predicted gene At3g52150 has been split into 2 genes: At3g52150 and At3g52155.; Evidence={ECO:0000305};
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DR EMBL; AL049711; CAB41335.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78903.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78904.1; -; Genomic_DNA.
DR EMBL; AY070427; AAL49922.1; -; mRNA.
DR EMBL; AY133746; AAM91680.1; -; mRNA.
DR EMBL; AK316998; BAH19693.1; -; mRNA.
DR PIR; T49094; T49094.
DR RefSeq; NP_001030841.1; NM_001035764.1.
DR RefSeq; NP_566958.3; NM_115074.5.
DR AlphaFoldDB; Q8VYM4; -.
DR SMR; Q8VYM4; -.
DR STRING; 3702.AT3G52150.1; -.
DR iPTMnet; Q8VYM4; -.
DR MetOSite; Q8VYM4; -.
DR PaxDb; Q8VYM4; -.
DR PRIDE; Q8VYM4; -.
DR ProteomicsDB; 249370; -.
DR EnsemblPlants; AT3G52150.1; AT3G52150.1; AT3G52150.
DR EnsemblPlants; AT3G52150.2; AT3G52150.2; AT3G52150.
DR GeneID; 824379; -.
DR Gramene; AT3G52150.1; AT3G52150.1; AT3G52150.
DR Gramene; AT3G52150.2; AT3G52150.2; AT3G52150.
DR KEGG; ath:AT3G52150; -.
DR Araport; AT3G52150; -.
DR TAIR; locus:2083810; AT3G52150.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_15_1_1; -.
DR InParanoid; Q8VYM4; -.
DR OMA; HEINESQ; -.
DR OrthoDB; 1384330at2759; -.
DR PhylomeDB; Q8VYM4; -.
DR PRO; PR:Q8VYM4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYM4; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:1901259; P:chloroplast rRNA processing; IBA:GO_Central.
DR GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0080148; P:negative regulation of response to water deprivation; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:UniProtKB.
DR GO; GO:1900140; P:regulation of seedling development; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 2: Evidence at transcript level;
KW Chaperone; Chloroplast; DNA-binding; Plastid; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW Stress response; Transit peptide.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000250|UniProtKB:P82277"
FT CHAIN 57..253
FT /note="30S ribosomal protein 2, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000441633"
FT DOMAIN 76..154
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 177..253
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT CONFLICT 88
FT /note="T -> S (in Ref. 4; BAH19693)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="I -> V (in Ref. 4; BAH19693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 253 AA; 27748 MW; 1EEB9920BAE71530 CRC64;
MATFLTNVVS IKPTIFSFQS ESFTPLHTRV NVFSSKPFPS LAGTFSRSSR TRFIPYAVTE
TEEKPAALDP SSEAARRVYI GNIPRTVTNE QLTKLVEEHG AVEKVQVMYD KYSGRSRRFG
FATMKSVEDA NAVVEKLNGN TVEGREIKVN ITEKPIASSP DLSVLQSEDS AFVDSPYKVY
VGNLAKTVTK EMLENLFSEK GKVVSAKVSR VPGTSKSTGF GFVTFSSEED VEAAIVALNN
SLLEGQKIRV NKA
