RL7A_BOVIN
ID RL7A_BOVIN Reviewed; 266 AA.
AC Q2TBQ5; A5D9D0;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=60S ribosomal protein L7a;
GN Name=RPL7A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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. {ECO:0000250|UniProtKB:P62424}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (By similarity).
CC Interacts with CRY1 (By similarity). Interacts with DICER1, AGO2,
CC TARBP2, MOV10 and EIF6; they form a large RNA-induced silencing complex
CC (RISC) (By similarity). {ECO:0000250|UniProtKB:P12970,
CC ECO:0000250|UniProtKB:P62424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62424}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000305}.
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DR EMBL; BT030549; ABQ12989.1; -; mRNA.
DR EMBL; BC109810; AAI09811.1; -; mRNA.
DR RefSeq; NP_001035610.1; NM_001040520.2.
DR AlphaFoldDB; Q2TBQ5; -.
DR SMR; Q2TBQ5; -.
DR IntAct; Q2TBQ5; 1.
DR STRING; 9913.ENSBTAP00000015358; -.
DR PaxDb; Q2TBQ5; -.
DR PeptideAtlas; Q2TBQ5; -.
DR PRIDE; Q2TBQ5; -.
DR Ensembl; ENSBTAT00000015358; ENSBTAP00000015358; ENSBTAG00000011559.
DR GeneID; 513128; -.
DR KEGG; bta:513128; -.
DR CTD; 6130; -.
DR VEuPathDB; HostDB:ENSBTAG00000011559; -.
DR VGNC; VGNC:49957; RPL7A.
DR eggNOG; KOG3166; Eukaryota.
DR GeneTree; ENSGT00940000153294; -.
DR HOGENOM; CLU_055193_0_1_1; -.
DR InParanoid; Q2TBQ5; -.
DR OMA; WLPALCK; -.
DR OrthoDB; 1200503at2759; -.
DR TreeFam; TF300788; -.
DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-BTA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-BTA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-BTA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000011559; Expressed in theca cell and 106 other tissues.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0042788; C:polysomal ribosome; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001921; Ribosomal_L7A/L8.
DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2.
DR InterPro; IPR004037; Ribosomal_L7Ae_CS.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00881; L7ARS6FAMILY.
DR PRINTS; PR00882; RIBOSOMALL7A.
DR SUPFAM; SSF55315; SSF55315; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..266
FT /note="60S ribosomal protein L7a"
FT /id="PRO_0000239925"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT MOD_RES 97
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P62424"
SQ SEQUENCE 266 AA; 30026 MW; 10FB43F221C281DF CRC64;
MPKGKKAKGK KVAPAPAVVK KQEAKKVVNP LFEKRPKNFG IGQDIQPKRD LTRFVKWPRY
IRLQRQRAIL YKRLKVPPAI NQFTQALDRQ TATQLLKLAH KYRPETKQEK KQRLLARAEK
KAAGKGDVPT KRPPVLRAGV NTVTTLVENK KAQLVVIAHD VDPIELVVFL PALCRKMGVP
YCIIKGKARL GRLVHRKTCT TVAFTQVNSE DKSALAKLVE AIRTNYNDRY DEIRRHWGGN
VLGPKSVARI AKLEKAKAKE LATKLG
