RL7_PONAB
ID RL7_PONAB Reviewed; 247 AA.
AC Q5R9R4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=60S ribosomal protein L7;
GN Name=RPL7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. Binds to G-rich structures in 28S rRNA and in
CC mRNAs. Plays a regulatory role in the translation apparatus; inhibits
CC cell-free translation of mRNAs. {ECO:0000250|UniProtKB:P18124}.
CC -!- SUBUNIT: Component of the large ribosomal subunit. Homodimer. Interacts
CC with DHX33. {ECO:0000250|UniProtKB:P18124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P18124}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000305}.
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DR EMBL; CR859318; CAH91496.1; -; mRNA.
DR RefSeq; NP_001125880.1; NM_001132408.2.
DR RefSeq; XP_009242140.1; XM_009243865.1.
DR AlphaFoldDB; Q5R9R4; -.
DR SMR; Q5R9R4; -.
DR STRING; 9601.ENSPPYP00000020944; -.
DR Ensembl; ENSPPYT00000021782; ENSPPYP00000020944; ENSPPYG00000018671.
DR GeneID; 100172811; -.
DR KEGG; pon:100172811; -.
DR CTD; 6129; -.
DR eggNOG; KOG3184; Eukaryota.
DR GeneTree; ENSGT00950000182878; -.
DR HOGENOM; CLU_055156_0_2_1; -.
DR InParanoid; Q5R9R4; -.
DR OMA; TKKTNHF; -.
DR OrthoDB; 1544778at2759; -.
DR TreeFam; TF300740; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:InterPro.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 2.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR012988; Ribosomal_L30_N.
DR InterPro; IPR039699; Ribosomal_L7/L30.
DR InterPro; IPR005998; Ribosomal_L7_euk.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR PANTHER; PTHR11524; PTHR11524; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR Pfam; PF08079; Ribosomal_L30_N; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR TIGRFAMs; TIGR01310; uL30_euk; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding.
FT CHAIN 1..247
FT /note="60S ribosomal protein L7"
FT /id="PRO_0000265738"
FT REPEAT 7..17
FT /note="1"
FT REPEAT 18..29
FT /note="2"
FT REPEAT 30..41
FT /note="3"
FT REPEAT 42..53
FT /note="4"
FT REGION 7..53
FT /note="4 X 12 AA tandem repeats"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 16
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 126
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14148"
FT MOD_RES 138
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
SQ SEQUENCE 247 AA; 29097 MW; 5F17F5CFB1ADC2FD CRC64;
MEGVEEKKKV PAVPETLKKK RRNFAELKIK RLRKKFAQKM LRKARRKLIY EKAKHYHKEY
RQMYRTEIRM ARMARKAGNF YVPAEPKLAF VIRIRGINGV SPKVRKVLQL LRLRQIFNGT
FVKLNKASIN MLRIVEPYIA WGYPNLKSVN ELIYKRGYGK INKKRIALTD NALIARSLGK
YGIICMEDLI HEIYTVGKRF KEANNFLWPF KLSSPRGGMK KKTTHFVEGG DAGNREDQIN
RLIRRMN