RL7_RAT
ID RL7_RAT Reviewed; 260 AA.
AC P05426;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=60S ribosomal protein L7;
GN Name=Rpl7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-252, AND PROTEIN SEQUENCE OF 253-258.
RX PubMed=3624274; DOI=10.1016/s0021-9258(18)45258-1;
RA Lin A., Chan Y.-L., McNally J., Peleg D., Meyuhas O., Wool I.G.;
RT "The primary structure of rat ribosomal protein L7. The presence near the
RT amino terminus of L7 of five tandem repeats of a sequence of 12 amino
RT acids.";
RL J. Biol. Chem. 262:12665-12671(1987).
RN [2]
RP SEQUENCE REVISION TO 253-260.
RX PubMed=7654221; DOI=10.1006/bbrc.1995.2233;
RA Chan Y.-L., Olvera J., Wool I.G.;
RT "The primary structures of rat ribosomal proteins: the characterization of
RT the cDNAs for S21 and L39, corrections in the sequences of L7 and L18a, and
RT the identification of L33.";
RL Biochem. Biophys. Res. Commun. 213:1042-1050(1995).
RN [3]
RP PROTEIN SEQUENCE OF 1-8 AND 161-168, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
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; M17422; AAA42075.1; -; mRNA.
DR PIR; JC4230; R5RTL7.
DR AlphaFoldDB; P05426; -.
DR SMR; P05426; -.
DR IntAct; P05426; 3.
DR MINT; P05426; -.
DR STRING; 10116.ENSRNOP00000009431; -.
DR iPTMnet; P05426; -.
DR PhosphoSitePlus; P05426; -.
DR jPOST; P05426; -.
DR PaxDb; P05426; -.
DR PRIDE; P05426; -.
DR UCSC; RGD:735169; rat.
DR RGD; 735169; Rpl7.
DR eggNOG; KOG3184; Eukaryota.
DR InParanoid; P05426; -.
DR PhylomeDB; P05426; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-RNO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-RNO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P05426; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031672; C:A band; IDA:RGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR GO; GO:0005840; C:ribosome; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008097; F:5S rRNA binding; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding.
FT CHAIN 1..260
FT /note="60S ribosomal protein L7"
FT /id="PRO_0000104635"
FT REPEAT 7..18
FT /note="1"
FT REPEAT 19..30
FT /note="2"
FT REPEAT 31..42
FT /note="3"
FT REPEAT 43..54
FT /note="4"
FT REPEAT 55..66
FT /note="5"
FT REGION 7..66
FT /note="5 X 12 AA tandem repeats"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 29
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
FT MOD_RES 139
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14148"
FT MOD_RES 151
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18124"
SQ SEQUENCE 260 AA; 30329 MW; 893802C48A79CEF1 CRC64;
MEAVPEKKKK VAAALGTLKK KKVPAVPETL KKKRRNFAEL KVKRLRKKFA LKTLRKARRK
LIYEKAKHYH KEYRQMYRTE IRMARMARKA GNFYVPAEPK LAFVIRIRGI NGVSPKVRKV
LQLLRLRQIF NGTFVKLNKA SVNMLRIVEP YIAWGYPNLK SVNELIYKRG YGKINKKRIA
LTDNSLVARS LGKFGIICME DLIHEIYTVG KRFKEANNFL WPFKLSSPRG GMKKKTTHFV
EGGDAGNRED QINRLIRRMN
