RL37_RAT
ID RL37_RAT Reviewed; 97 AA.
AC P61928; P02403; Q99883;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=60S ribosomal protein L37;
GN Name=Rpl37;
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 PRELIMINARY PROTEIN SEQUENCE OF 2-97.
RC TISSUE=Liver;
RX PubMed=6350292; DOI=10.1016/s0021-9258(17)44508-x;
RA Lin A., McNally J., Wool I.G.;
RT "The primary structure of rat liver ribosomal protein L37. Homology with
RT yeast and bacterial ribosomal proteins.";
RL J. Biol. Chem. 258:10664-10671(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-40.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8484768; DOI=10.1006/bbrc.1993.1456;
RA Chan Y.-L., Paz V., Olvera J., Wool I.G.;
RT "The primary structure of L37 -- a rat ribosomal protein with a zinc
RT finger-like motif.";
RL Biochem. Biophys. Res. Commun. 192:590-596(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7588717; DOI=10.1111/j.1432-1033.1995.tb20874.x;
RA Su S., Bird R.C.;
RT "Cell cycle, differentiation and tissue-independent expression of ribosomal
RT protein L37.";
RL Eur. J. Biochem. 232:789-797(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and 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:P61927}.
CC -!- SUBUNIT: Component of the large ribosomal subunit.
CC {ECO:0000250|UniProtKB:P61927}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61927}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL37 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Miscellaneous discrepancy; Note=Differs from that shown extensively.; Evidence={ECO:0000305};
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DR EMBL; X66369; CAA47012.1; -; mRNA.
DR EMBL; S79981; AAP32040.1; -; mRNA.
DR EMBL; BC059132; AAH59132.1; -; mRNA.
DR EMBL; BC069173; AAH69173.1; -; mRNA.
DR PIR; JN0478; R6RT37.
DR RefSeq; NP_112368.1; NM_031106.1.
DR RefSeq; XP_002727261.1; XM_002727215.5.
DR RefSeq; XP_002730083.1; XM_002730037.5.
DR RefSeq; XP_017453151.1; XM_017597662.1.
DR RefSeq; XP_017459577.1; XM_017604088.1.
DR AlphaFoldDB; P61928; -.
DR SMR; P61928; -.
DR STRING; 10116.ENSRNOP00000039155; -.
DR iPTMnet; P61928; -.
DR PhosphoSitePlus; P61928; -.
DR jPOST; P61928; -.
DR PaxDb; P61928; -.
DR PRIDE; P61928; -.
DR Ensembl; ENSRNOT00000045156; ENSRNOP00000049205; ENSRNOG00000033803.
DR Ensembl; ENSRNOT00000046519; ENSRNOP00000039155; ENSRNOG00000034180.
DR GeneID; 100360841; -.
DR GeneID; 81770; -.
DR KEGG; rno:100360841; -.
DR KEGG; rno:81770; -.
DR CTD; 81770; -.
DR RGD; 621204; Rpl37.
DR eggNOG; KOG3475; Eukaryota.
DR GeneTree; ENSGT00390000005254; -.
DR HOGENOM; CLU_150908_0_0_1; -.
DR InParanoid; P61928; -.
DR OMA; RMAYLKH; -.
DR OrthoDB; 1560654at2759; -.
DR PhylomeDB; P61928; -.
DR TreeFam; TF300260; -.
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:P61928; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000033803; Expressed in thymus and 19 other tissues.
DR Genevisible; P61928; RN.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:RGD.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:RGD.
DR GO; GO:0019838; F:growth factor binding; IPI:RGD.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:RGD.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; ISO:RGD.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISO:RGD.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 2.20.25.30; -; 1.
DR HAMAP; MF_00547; Ribosomal_L37e; 1.
DR InterPro; IPR011331; Ribosomal_L37ae/L37e.
DR InterPro; IPR001569; Ribosomal_L37e.
DR InterPro; IPR018267; Ribosomal_L37e_CS.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01907; Ribosomal_L37e; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS01077; RIBOSOMAL_L37E; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8484768"
FT CHAIN 2..97
FT /note="60S ribosomal protein L37"
FT /id="PRO_0000139707"
FT ZN_FING 19..37
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P49166"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61927"
SQ SEQUENCE 97 AA; 11078 MW; F565A11E983027C9 CRC64;
MTKGTSSFGK RRNKTHTLCR RCGSKAYHLQ KSTCGKCGYP AKRKRKYNWS AKAKRRNTTG
TGRMRHLKIV YRRFRHGFRE GTTPKPKRAA VAASSSS
