RM21_ARATH
ID RM21_ARATH Reviewed; 270 AA.
AC Q8L9A0; O65556; Q0WRT4; Q9B7N7;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=50S ribosomal protein L21, mitochondrial {ECO:0000303|PubMed:11675010};
DE AltName: Full=Protein NUCLEAR FUSION DEFECTIVE 1 {ECO:0000303|PubMed:16698901};
DE Flags: Precursor;
GN Name=RPL21M {ECO:0000303|PubMed:11675010};
GN Synonyms=NFD1 {ECO:0000303|PubMed:16698901};
GN OrderedLocusNames=At4g30930 {ECO:0000312|Araport:AT4G30930};
GN ORFNames=F6I18.160;
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], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11675010; DOI=10.1016/s0378-1119(01)00613-8;
RA Gallois J.-L., Achard P., Green G., Mache R.;
RT "The Arabidopsis chloroplast ribosomal protein L21 is encoded by a nuclear
RT gene of mitochondrial origin.";
RL Gene 274:179-185(2001).
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 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 [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16698901; DOI=10.1104/pp.106.079319;
RA Portereiko M.F., Sandaklie-Nikolova L., Lloyd A., Dever C.A., Otsuga D.,
RA Drews G.N.;
RT "NUCLEAR FUSION DEFECTIVE1 encodes the Arabidopsis RPL21M protein and is
RT required for karyogamy during female gametophyte development and
RT fertilization.";
RL Plant Physiol. 141:957-965(2006).
CC -!- FUNCTION: This protein binds to 23S ribosomal RNA in the presence of
CC protein L20 (By similarity). Required for karyogamy during female
CC gametophyte development, when the two polar nuclei fuse to form the
CC diploid central cell nucleus, and during double fertilization of the
CC egg cell and the central cell (PubMed:16698901). {ECO:0000250,
CC ECO:0000269|PubMed:16698901}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16698901}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, stems, leaves,
CC flowers, pistils and siliques. {ECO:0000269|PubMed:11675010,
CC ECO:0000269|PubMed:16698901}.
CC -!- DISRUPTION PHENOTYPE: Failure of fusion of the polar nuclei during
CC megagametogenesis and abnormal double fertilization; fails to undergo
CC fusion of the outer nuclear membranes. {ECO:0000269|PubMed:16698901}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL21 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18200.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g30930 has been split into 2 genes: At4g30930 and At4g30935.; Evidence={ECO:0000305};
CC Sequence=CAB79811.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g30930 has been split into 2 genes: At4g30930 and At4g30935.; Evidence={ECO:0000305};
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DR EMBL; AJ278909; CAC27453.1; -; Genomic_DNA.
DR EMBL; AL022198; CAA18200.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161578; CAB79811.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85831.1; -; Genomic_DNA.
DR EMBL; BT005870; AAO64805.1; -; mRNA.
DR EMBL; AK228212; BAF00165.1; -; mRNA.
DR EMBL; AY088563; AAM66095.1; -; mRNA.
DR EMBL; AB493710; BAH30548.1; -; mRNA.
DR PIR; B85362; B85362.
DR RefSeq; NP_567861.1; NM_119240.4.
DR PDB; 6XYW; EM; 3.86 A; Ar=1-270.
DR PDBsum; 6XYW; -.
DR AlphaFoldDB; Q8L9A0; -.
DR SMR; Q8L9A0; -.
DR BioGRID; 14504; 5.
DR IntAct; Q8L9A0; 2.
DR STRING; 3702.AT4G30930.1; -.
DR iPTMnet; Q8L9A0; -.
DR PaxDb; Q8L9A0; -.
DR PRIDE; Q8L9A0; -.
DR ProteomicsDB; 228176; -.
DR EnsemblPlants; AT4G30930.1; AT4G30930.1; AT4G30930.
DR GeneID; 829217; -.
DR Gramene; AT4G30930.1; AT4G30930.1; AT4G30930.
DR KEGG; ath:AT4G30930; -.
DR Araport; AT4G30930; -.
DR TAIR; locus:2126699; AT4G30930.
DR eggNOG; KOG1686; Eukaryota.
DR HOGENOM; CLU_061463_4_0_1; -.
DR InParanoid; Q8L9A0; -.
DR OMA; DRCFSSN; -.
DR OrthoDB; 1586807at2759; -.
DR PhylomeDB; Q8L9A0; -.
DR PRO; PR:Q8L9A0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8L9A0; baseline and differential.
DR Genevisible; Q8L9A0; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IMP:TAIR.
DR GO; GO:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0000741; P:karyogamy; IMP:TAIR.
DR GO; GO:0010197; P:polar nucleus fusion; IMP:UniProtKB.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR HAMAP; MF_01363; Ribosomal_L21; 1.
DR InterPro; IPR036164; L21-like_sf.
DR InterPro; IPR028909; L21p-like.
DR InterPro; IPR001787; Ribosomal_L21.
DR InterPro; IPR018258; Ribosomal_L21_CS.
DR PANTHER; PTHR21349; PTHR21349; 1.
DR Pfam; PF00829; Ribosomal_L21p; 1.
DR SUPFAM; SSF141091; SSF141091; 1.
DR TIGRFAMs; TIGR00061; L21; 1.
DR PROSITE; PS01169; RIBOSOMAL_L21; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Fertilization; Karyogamy;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transit peptide.
FT TRANSIT 1..68
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 69..270
FT /note="50S ribosomal protein L21, mitochondrial"
FT /id="PRO_0000030482"
FT REGION 68..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 30908 MW; C83E96E95666ABF9 CRC64;
MASLRCFREL SRRATTVFSI NQTRSISSFH GIEFSGTSIS HGTVIPNRSL TRNLPWYSHW
YRSQDRCFSS NTKDTDEDEE SSEGEDDDEE EGEDFEDSAD MEVEREYSPA EKVEEAEEIG
YKVMGPLKPS ERLFKPYEPV FAIVQIGSHQ FKVSNGDSIF TEKLKFCDIN DKLELTKVLL
LGSASQTIIG RPILPDATVH AVVEEHALDE KVLIFKKKRR KNYRRTRGHR QELTKLRITD
IQGIEKPEPK IVHKPSKEAV TEQTKAELVA
