HLL_ARATH
ID HLL_ARATH Reviewed; 196 AA.
AC Q84JG5; Q8LC24; Q8W1X5; Q9LNP8;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=50S ribosomal protein HLL, mitochondrial;
DE AltName: Full=Protein HUELLENLOS;
DE Flags: Precursor;
GN Name=HLL; OrderedLocusNames=At1g17560; ORFNames=F1L3.27;
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], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11752383; DOI=10.2307/3871530;
RA Skinner D.J., Baker S.C., Meister R.J., Broadhvest J., Schneitz K.,
RA Gasser C.S.;
RT "The Arabidopsis HUELLENLOS gene, which is essential for normal ovule
RT development, encodes a mitochondrial ribosomal protein.";
RL Plant Cell 13:2719-2730(2001).
RN [2]
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 [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].
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9636071; DOI=10.1242/dev.125.14.2555;
RA Schneitz K., Baker S.C., Gasser C.S., Redweik A.;
RT "Pattern formation and growth during floral organogenesis: HUELLENLOS and
RT AINTEGUMENTA are required for the formation of the proximal region of the
RT ovule primordium in Arabidopsis thaliana.";
RL Development 125:2555-2563(1998).
RN [7]
RP FUNCTION, AND INDUCTION BY BRASSINOSTEROID.
RX PubMed=22914576; DOI=10.1093/mp/sss070;
RA Huang H.-Y., Jiang W.-B., Hu Y.-W., Wu P., Zhu J.-Y., Liang W.-Q.,
RA Wang Z.-Y., Lin W.-H.;
RT "BR signal influences Arabidopsis ovule and seed number through regulating
RT related genes expression by BZR1.";
RL Mol. Plant 6:456-469(2013).
CC -!- FUNCTION: Binds to 23S rRNA in mitochondrion (By similarity). Required
CC for the formation of the proximal region of the ovule primordium during
CC floral organogenesis, thus participating in patterning and growth of
CC ovule. Also regulates the initiation and/or maintenance of integument
CC and embryo sac ontogenesis. Prevents inappropriate cell death in the
CC young ovule. {ECO:0000250, ECO:0000269|PubMed:11752383,
CC ECO:0000269|PubMed:22914576, ECO:0000269|PubMed:9636071}.
CC -!- SUBUNIT: Part of the mitochondrial 50S ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11752383}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in pistils and inflorescences,
CC including floral organs and meristems, and, to a lower extent, in
CC leaves. {ECO:0000269|PubMed:11752383}.
CC -!- INDUCTION: By brassinosteroid (BR), repressed by the BR biosynthesis
CC inhibitor brassinazole (BRZ). {ECO:0000269|PubMed:22914576}.
CC -!- DISRUPTION PHENOTYPE: Female-sterility due to abnormal gynoecium and
CC ovule growth and development with highly reduced integuments and
CC collapsed cells in the distal regions of the ovule primordia. Slight
CC reduction in the rate of growth and size of the pistil.
CC {ECO:0000269|PubMed:11752383, ECO:0000269|PubMed:9636071}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL14 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79479.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM63894.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF402992; AAL60451.1; -; Genomic_DNA.
DR EMBL; AC022492; AAF79479.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE29606.1; -; Genomic_DNA.
DR EMBL; BT004292; AAO42290.1; -; mRNA.
DR EMBL; BT005522; AAO63942.1; -; mRNA.
DR EMBL; AY086846; AAM63894.1; ALT_INIT; mRNA.
DR RefSeq; NP_173200.1; NM_101619.2.
DR AlphaFoldDB; Q84JG5; -.
DR SMR; Q84JG5; -.
DR STRING; 3702.AT1G17560.1; -.
DR PaxDb; Q84JG5; -.
DR PRIDE; Q84JG5; -.
DR ProteomicsDB; 230227; -.
DR EnsemblPlants; AT1G17560.1; AT1G17560.1; AT1G17560.
DR GeneID; 838332; -.
DR Gramene; AT1G17560.1; AT1G17560.1; AT1G17560.
DR KEGG; ath:AT1G17560; -.
DR Araport; AT1G17560; -.
DR TAIR; locus:2007913; AT1G17560.
DR eggNOG; KOG0901; Eukaryota.
DR HOGENOM; CLU_095071_1_1_1; -.
DR InParanoid; Q84JG5; -.
DR OrthoDB; 1547267at2759; -.
DR PRO; PR:Q84JG5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84JG5; baseline and differential.
DR Genevisible; Q84JG5; AT.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0009553; P:embryo sac development; IMP:UniProtKB.
DR GO; GO:0080060; P:integument development; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:0048481; P:plant ovule development; IMP:UniProtKB.
DR GO; GO:0009741; P:response to brassinosteroid; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1.
DR InterPro; IPR036853; Ribosomal_L14_sf.
DR InterPro; IPR000218; Ribosomal_L14P.
DR InterPro; IPR019972; Ribosomal_L14P_CS.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SMART; SM01374; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Transit peptide.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 63..196
FT /note="50S ribosomal protein HLL, mitochondrial"
FT /id="PRO_0000429331"
FT REGION 148..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1
FT /note="M -> I (in Ref. 5; AAM63894)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="I -> V (in Ref. 1; AAL60451 and 5; AAM63894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 21160 MW; B96F686EB74F9476 CRC64;
MATALASKLS KGRSLLGGLC NAFSGLMNSS SNGMMNGSIL SQQQHRTFIQ MGTILKCVDN
SCAKEVMCIQ SLRGKKGARL GDIIVGSVKE ANPIVQKKVK KDAIPKGKVK KGMVVYGVVV
RAAMPKGRAD GSQVKFDDNA IVVVGIKEKK GQNNSHGSKR KMEYNQPTGT RVFGPVPHEM
RLRKQLKILS LAQHIV
