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RL32_DROME
ID   RL32_DROME              Reviewed;         134 AA.
AC   P04359; A4V3M7; B7Z0S1; O01386; Q8IMJ6; Q9VAB2;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=60S ribosomal protein L32;
DE   AltName: Full=Ribosomal protein 49;
GN   Name=RpL32; Synonyms=M(3)99D, rp49; ORFNames=CG7939;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6087289; DOI=10.1093/nar/12.13.5495;
RA   O'Connell P., Rosbash M.;
RT   "Sequence, structure, and codon preference of the Drosophila ribosomal
RT   protein 49 gene.";
RL   Nucleic Acids Res. 12:5495-5513(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC   STRAIN=Canton-S;
RA   McMahill M.S., Danielson P.D., Fogleman J.C.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M66;
RX   PubMed=9479691; DOI=10.1006/mpev.1997.0438;
RA   Ramos-Onsins S., Segarra C., Rozas J., Aguade M.;
RT   "Molecular and chromosomal phylogeny in the obscura group of Drosophila
RT   inferred from sequences of the rp49 gene region.";
RL   Mol. Phylogenet. Evol. 9:33-41(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
RX   PubMed=23636399; DOI=10.1038/nature12104;
RA   Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA   Wilson D.N., Beckmann R.;
RT   "Structures of the human and Drosophila 80S ribosome.";
RL   Nature 497:80-85(2013).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000312|FlyBase:FBgn0002626}; Synonyms=B, D
CC       {ECO:0000312|FlyBase:FBgn0002626};
CC         IsoId=P04359-1; Sequence=Displayed;
CC       Name=C {ECO:0000312|FlyBase:FBgn0002626};
CC         IsoId=P04359-2; Sequence=VSP_058151;
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family.
CC       {ECO:0000305}.
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DR   EMBL; X00848; CAA25404.1; -; Genomic_DNA.
DR   EMBL; U92431; AAB51389.1; -; mRNA.
DR   EMBL; Y13939; CAA74278.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF57001.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14210.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN14211.1; -; Genomic_DNA.
DR   EMBL; AE014297; ACL83583.1; -; Genomic_DNA.
DR   EMBL; AY070656; AAL48127.1; -; mRNA.
DR   EMBL; BT011442; AAR99100.1; -; mRNA.
DR   PIR; A02830; R5FF49.
DR   RefSeq; NP_001138127.1; NM_001144655.3. [P04359-1]
DR   RefSeq; NP_524582.1; NM_079843.4. [P04359-1]
DR   RefSeq; NP_733339.1; NM_170460.2. [P04359-2]
DR   RefSeq; NP_733340.1; NM_170461.3. [P04359-1]
DR   PDB; 4V6W; EM; 6.00 A; Ce=1-134.
DR   PDB; 6XU6; EM; 3.50 A; Ce=1-132.
DR   PDB; 6XU7; EM; 4.90 A; Ce=1-132.
DR   PDB; 6XU8; EM; 3.00 A; Ce=1-132.
DR   PDBsum; 4V6W; -.
DR   PDBsum; 6XU6; -.
DR   PDBsum; 6XU7; -.
DR   PDBsum; 6XU8; -.
DR   AlphaFoldDB; P04359; -.
DR   SMR; P04359; -.
DR   BioGRID; 68429; 93.
DR   IntAct; P04359; 13.
DR   STRING; 7227.FBpp0084959; -.
DR   PaxDb; P04359; -.
DR   PRIDE; P04359; -.
DR   DNASU; 43573; -.
DR   EnsemblMetazoa; FBtr0085592; FBpp0084958; FBgn0002626. [P04359-1]
DR   EnsemblMetazoa; FBtr0085593; FBpp0084959; FBgn0002626. [P04359-2]
DR   EnsemblMetazoa; FBtr0085594; FBpp0084960; FBgn0002626. [P04359-1]
DR   EnsemblMetazoa; FBtr0114555; FBpp0113047; FBgn0002626. [P04359-1]
DR   GeneID; 43573; -.
DR   KEGG; dme:Dmel_CG7939; -.
DR   CTD; 6161; -.
DR   FlyBase; FBgn0002626; RpL32.
DR   VEuPathDB; VectorBase:FBgn0002626; -.
DR   eggNOG; KOG0878; Eukaryota.
DR   GeneTree; ENSGT00940000158890; -.
DR   HOGENOM; CLU_071479_4_1_1; -.
DR   InParanoid; P04359; -.
DR   OMA; HPSGYEE; -.
DR   PhylomeDB; P04359; -.
DR   Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   SignaLink; P04359; -.
DR   BioGRID-ORCS; 43573; 1 hit in 1 CRISPR screen.
DR   ChiTaRS; RpL32; fly.
DR   GenomeRNAi; 43573; -.
DR   PRO; PR:P04359; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002626; Expressed in adult Malpighian tubule (Drosophila) and 25 other tissues.
DR   ExpressionAtlas; P04359; baseline and differential.
DR   Genevisible; P04359; DM.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR   GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
DR   CDD; cd00513; Ribosomal_L32_L32e; 1.
DR   InterPro; IPR001515; Ribosomal_L32e.
DR   InterPro; IPR018263; Ribosomal_L32e_CS.
DR   InterPro; IPR036351; Ribosomal_L32e_sf.
DR   PANTHER; PTHR23413; PTHR23413; 1.
DR   Pfam; PF01655; Ribosomal_L32e; 1.
DR   SMART; SM01393; Ribosomal_L32e; 1.
DR   SUPFAM; SSF52042; SSF52042; 1.
DR   PROSITE; PS00580; RIBOSOMAL_L32E; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..134
FT                   /note="60S ribosomal protein L32"
FT                   /id="PRO_0000131128"
FT   VAR_SEQ         1
FT                   /note="M -> MDTAQEASPTCFKM (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058151"
FT   CONFLICT        18
FT                   /note="H -> D (in Ref. 1; CAA25404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        45
FT                   /note="R -> G (in Ref. 1; CAA25404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92..107
FT                   /note="RVYCGEIAHGVSSKKR -> PRLLREMPTASPPRS (in Ref. 1;
FT                   CAA25404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="V -> I (in Ref. 1; CAA25404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119..134
FT                   /note="VRLTNPNGRLRSQENE -> LRSPTPTVACVSRRTR (in Ref. 1;
FT                   CAA25404)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   134 AA;  16020 MW;  AC00FA7EEEE46D9A CRC64;
     MTIRPAYRPK IVKKRTKHFI RHQSDRYAKL SHKWRKPKGI DNRVRRRFKG QYLMPNIGYG
     SNKRTRHMLP TGFKKFLVHN VRELEVLLMQ NRVYCGEIAH GVSSKKRKEI VERAKQLSVR
     LTNPNGRLRS QENE
 
 
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