ID   RL35_RAT                Reviewed;         123 AA.
AC   P17078;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=60S ribosomal protein L35;
GN   Name=Rpl35;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=2322279; DOI=10.1016/0006-291x(90)90675-d;
RA   Suzuki K., Olvera J., Wool I.G.;
RT   "The primary structure of rat ribosomal protein L35.";
RL   Biochem. Biophys. Res. Commun. 167:1377-1382(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:P42766}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit.
CC       {ECO:0000250|UniProtKB:P42766}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42766}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC       {ECO:0000305}.
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DR   EMBL; X51705; CAA36001.1; -; mRNA.
DR   EMBL; BC058499; AAH58499.1; -; mRNA.
DR   PIR; A34571; R5RT35.
DR   RefSeq; NP_997676.1; NM_212511.2.
DR   AlphaFoldDB; P17078; -.
DR   SMR; P17078; -.
DR   IntAct; P17078; 7.
DR   STRING; 10116.ENSRNOP00000019162; -.
DR   iPTMnet; P17078; -.
DR   PhosphoSitePlus; P17078; -.
DR   jPOST; P17078; -.
DR   PaxDb; P17078; -.
DR   PRIDE; P17078; -.
DR   GeneID; 296709; -.
DR   KEGG; rno:296709; -.
DR   UCSC; RGD:1303007; rat.
DR   CTD; 11224; -.
DR   RGD; 1303007; Rpl35.
DR   VEuPathDB; HostDB:ENSRNOG00000014272; -.
DR   eggNOG; KOG3436; Eukaryota.
DR   HOGENOM; CLU_110381_1_1_1; -.
DR   InParanoid; P17078; -.
DR   OMA; VMNQKAR; -.
DR   OrthoDB; 1468839at2759; -.
DR   PhylomeDB; P17078; -.
DR   TreeFam; TF314951; -.
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:P17078; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000014272; Expressed in ovary and 20 other tissues.
DR   Genevisible; P17078; RN.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:RGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR   GO; GO:0071493; P:cellular response to UV-B; 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:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 1.10.287.310; -; 1.
DR   HAMAP; MF_00374; Ribosomal_L29; 1.
DR   InterPro; IPR001854; Ribosomal_L29/L35.
DR   InterPro; IPR036049; Ribosomal_L29/L35_sf.
DR   InterPro; IPR018254; Ribosomal_L29_CS.
DR   InterPro; IPR045059; RL35.
DR   PANTHER; PTHR45722; PTHR45722; 1.
DR   Pfam; PF00831; Ribosomal_L29; 1.
DR   SUPFAM; SSF46561; SSF46561; 1.
DR   TIGRFAMs; TIGR00012; L29; 1.
DR   PROSITE; PS00579; RIBOSOMAL_L29; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN           1..123
FT                   /note="60S ribosomal protein L35"
FT                   /id="PRO_0000130535"
FT   REGION          100..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42766"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P42766"
FT   MOD_RES         43
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P42766"
FT   CROSSLNK        25
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P42766"
SQ   SEQUENCE   123 AA;  14553 MW;  67B76951361674EB CRC64;
     MAKIKARDLR GKKKEELLKQ LDDLKVELSQ LRVAKVTGGA ASKLSKIRVV RKSIARVLTV
     INQTQKENLR KFYKGKKYKP LDLRPKKTRA MRRRLTKHEE KLKTKKQQRK ERLYPLRKYA
     VKA