RPS9M_ARATH
ID RPS9M_ARATH Reviewed; 430 AA.
AC Q8L6Z4; Q67Y07; Q9SMU6;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=30S ribosomal protein S9, mitochondrial {ECO:0000305};
DE Flags: Precursor;
GN Name=RPS9M {ECO:0000303|PubMed:29312411};
GN OrderedLocusNames=At3g49080 {ECO:0000312|Araport:AT3G49080};
GN ORFNames=T2J13.70 {ECO:0000312|EMBL:CAB62001.1};
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;
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH PIA2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=29312411; DOI=10.3389/fpls.2017.02171;
RA Lu C., Yu F., Tian L., Huang X., Tan H., Xie Z., Hao X., Li D., Luan S.,
RA Chen L.;
RT "RPS9M, a mitochondrial ribosomal protein, is essential for central cell
RT maturation and endosperm development in Arabidopsis.";
RL Front. Plant Sci. 8:2171-2171(2017).
CC -!- FUNCTION: Mitochondrial ribosomal protein required for central cell
CC maturation. May work together with PIA2 in controlling female
CC gametophyte development, possibly by regulating the expression of some
CC mitochondrial proteins. {ECO:0000269|PubMed:29312411}.
CC -!- SUBUNIT: Interacts (via C terminus) with PIA2.
CC {ECO:0000269|PubMed:29312411}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:29312411}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, young leaves, flowers and
CC siliques. {ECO:0000269|PubMed:29312411}.
CC -!- DEVELOPMENTAL STAGE: In anthers, expressed throughout the developmental
CC stages, especially in the mature pollen grains. In pistils, expressed
CC in the mature female gametophyte stage and during fertilization.
CC {ECO:0000269|PubMed:29312411}.
CC -!- DISRUPTION PHENOTYPE: Aborted ovule development due to defects in
CC fusion of polar nuclei and central cell maturation.
CC {ECO:0000269|PubMed:29312411}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB62001.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL132967; CAB62001.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE78497.1; -; Genomic_DNA.
DR EMBL; AY140063; AAM98204.1; -; mRNA.
DR EMBL; BT006583; AAP31927.1; -; mRNA.
DR EMBL; AK176622; BAD44385.1; -; mRNA.
DR EMBL; AK176661; BAD44424.1; -; mRNA.
DR PIR; T46121; T46121.
DR RefSeq; NP_190477.2; NM_114767.4.
DR PDB; 6XYW; EM; 3.86 A; Bh=1-430.
DR PDBsum; 6XYW; -.
DR AlphaFoldDB; Q8L6Z4; -.
DR SMR; Q8L6Z4; -.
DR IntAct; Q8L6Z4; 3.
DR STRING; 3702.AT3G49080.1; -.
DR PaxDb; Q8L6Z4; -.
DR PRIDE; Q8L6Z4; -.
DR ProteomicsDB; 228236; -.
DR EnsemblPlants; AT3G49080.1; AT3G49080.1; AT3G49080.
DR GeneID; 824070; -.
DR Gramene; AT3G49080.1; AT3G49080.1; AT3G49080.
DR KEGG; ath:AT3G49080; -.
DR Araport; AT3G49080; -.
DR TAIR; locus:2101373; AT3G49080.
DR eggNOG; KOG1697; Eukaryota.
DR HOGENOM; CLU_046483_5_1_1; -.
DR InParanoid; Q8L6Z4; -.
DR OMA; WEETKRW; -.
DR OrthoDB; 1430790at2759; -.
DR PhylomeDB; Q8L6Z4; -.
DR PRO; PR:Q8L6Z4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L6Z4; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0009559; P:embryo sac central cell differentiation; IMP:TAIR.
DR GO; GO:0048229; P:gametophyte development; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR HAMAP; MF_00532_B; Ribosomal_S9_B; 1.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR000754; Ribosomal_S9.
DR InterPro; IPR023035; Ribosomal_S9_bac/plastid.
DR InterPro; IPR020574; Ribosomal_S9_CS.
DR PANTHER; PTHR21569; PTHR21569; 1.
DR Pfam; PF00380; Ribosomal_S9; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 35..430
FT /note="30S ribosomal protein S9, mitochondrial"
FT /id="PRO_0000443713"
FT REGION 32..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 165
FT /note="V -> G (in Ref. 4; BAD44424)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 430 AA; 47988 MW; F8FE0ADCE3CCCC39 CRC64;
MLSRLFLRHS NLRFVTLVSS KSNSQIFSSF IRPLSTNSSG GGGNGDGNGR NRNDVPWSFT
GVNDDKSGPF SSDDSFGSSG VAGSGLPGGE GKWPEEPKRW NIKEEEEKVV FDTGGEVGQG
IETSRERRGN EWEETKRWDM KEGEEKVVFG GGGDEVDGFG IRGEVKSNEW DVSKPWNLKE
EEEGVVFDTG GEVPFSFENS LEMAEEERVK KELIEKEEKE LLEVIKGPDR AFGDLIAKSG
ITDEMLDSLI ALKDFQGVEG LPPLTEIENL RREKSSKKSS RAEIELQMQE DIAKARVRQV
DETGRAYGTG RRKCSIARVW IQPGEGKFQV NEKEFDVYFP MLDHRAALLR PLAETKTLGR
WDIKCTVKGG GTTGQVGAIQ LGISRALQNW EPDMRTSLRA AGFLTRDSRV VERKKPGKAK
ARKSFQWVKR
