P19889 (RLA0_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S acidic ribosomal protein P0

Alternative name(s):
Apurinic-apyrimidinic endonuclease
DNA-(apurinic or apyrimidinic site) lyase
EC=4.2.99.18

Gene names

Name:	RpLP0
Synonyms:	AP3, Ape, RpP0
ORF Names:	CG7490

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ribosomal protein P0 is the functional equivalent of E.coli protein L10.
Catalytic activity	The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
Subunit structure	P0 forms a pentameric complex by interaction with dimers of P1 and P2 By similarity.
Subcellular location	Cytoplasm. Nucleus.
Developmental stage	All stages of development. A larger transcript is restricted to the embryonic and early larval stages.
Sequence similarities	Belongs to the ribosomal protein L10P family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Molecular function	Lyase Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW ribosome biogenesis Inferred from electronic annotation. Source: InterPro translational elongation Inferred from electronic annotation. Source: InterPro
Cellular_component	lipid particle Inferred from direct assay PubMed 16543254. Source: FlyBase nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell ribosome Inferred from direct assay PubMed 16889426. Source: FlyBase
Molecular_function	DNA-(apurinic or apyrimidinic site) lyase activity Inferred from electronic annotation. Source: EC structural constituent of ribosome Inferred from direct assay PubMed 16889426. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 317	317	60S acidic ribosomal protein P0		PRO_0000154769
Amino acid modifications
	Modified residue	302	1	Phosphoserine Ref.8
	Modified residue	304	1	Phosphoserine; by CK1 Potential

Sequences

	Sequence		Length	Mass (Da)
	P19889 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 36E9DD5DD8CF7E1F	FASTA	317	34,202
	10 20 30 40 50 60 MVRENKAAWK AQYFIKVVEL FDEFPKCFIV GADNVGSKQM QNIRTSLRGL AVVLMGKNTM 70 80 90 100 110 120 MRKAIRGHLE NNPQLEKLLP HIKGNVGFVF TKGDLAEVRD KLLESKVRAP ARPGAIAPLH 130 140 150 160 170 180 VIIPAQNTGL GPEKTSFFQA LSIPTKISKG TIEIINDVPI LKPGDKVGAS EATLLNMLNI 190 200 210 220 230 240 SPFSYGLIVN QVYDSGSIFS PEILDIKPED LRAKFQQGVA NLAAVCLSVG YPTIASAPHS 250 260 270 280 290 300 IANGFKNLLA IAATTEVEFK EATTIKEYIK DPSKFAAAAS ASAAPAAGGA TEKKEEAKKP 310 ESESEEEDDD MGFGLFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Antibody to a human DNA repair protein allows for cloning of a Drosophila cDNA that encodes an apurinic endonuclease." Kelley M.R., Venugopal S., Harless J., Deutsch W.A. Mol. Cell. Biol. 9:965-973(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[6]	"Drosophila AP3, a presumptive DNA repair protein, is homologous to human ribosomal associated protein P0." Grabowski D.T., Deutsch W.A., Derda D., Kelley M.R. Nucleic Acids Res. 19:4297-4297(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SIMILARITY TO RIBOSOMAL PROTEIN P0.
[7]	"Drosophila ribosomal protein PO contains apurinic/apyrimidinic endonuclease activity." Yacoub A., Kelley M.R., Deutsch W.A. Nucleic Acids Res. 24:4298-4303(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DNA REPAIR ACTIVITY.
[8]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M25772 mRNA. Translation: AAA53372.1. AE014296 Genomic DNA. Translation: AAF51807.1. AY075528 mRNA. Translation: AAL68335.1. BT021447 mRNA. Translation: AAX33595.1.
PIR	R5FFP0. A30223.
RefSeq	NP_001262202.1. NM_001275273.1. NP_524211.1. NM_079487.4.
UniGene	Dm.7933.
3D structure databases
ProteinModelPortal	P19889.
SMR	P19889. Positions 2-259.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-21968N.
IntAct	P19889. 2 interactions.
MINT	MINT-235412.
Proteomic databases
PaxDb	P19889.
PRIDE	P19889.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0078481; FBpp0078134; FBgn0000100. FBtr0334113; FBpp0306232; FBgn0000100.
GeneID	40451.
KEGG	dme:Dmel_CG7490.
Organism-specific databases
CTD	6175.
FlyBase	FBgn0000100. RpLP0.
Phylogenomic databases
eggNOG	COG0244.
GeneTree	ENSGT00390000017839.
InParanoid	P19889.
KO	K02941.
OMA	AYMHAFN.
OrthoDB	EOG4J6Q6N.
PhylomeDB	P19889.
Gene expression databases
Bgee	P19889.
GermOnline	CG7490. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001813. Ribosomal_60S. IPR001790. Ribosomal_L10/acidic_P0. [Graphical view]
Pfam	PF00428. Ribosomal_60s. 1 hit. PF00466. Ribosomal_L10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	40451.
NextBio	818852.

Entry information

Entry name

RLA0_DROME

Accession

Primary (citable) accession number: P19889
Secondary accession number(s): Q5BHX7, Q9VNV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 128 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project