Reviewed, UniProtKB/Swiss-Prot P40301 (PSA2_DROME)

Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-2
    EC=3.4.25.1
Alternative name(s):
    Proteasome 25 kDa subunit
    PROS-Dm25

Gene names

Name:	Pros25
Synonyms:	PROS-25
ORF Names:	CG5266

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell proliferation Inferred from mutant phenotype. Source: FlyBase mitotic spindle elongation Inferred from mutant phenotype. Source: FlyBase ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 234	234	Proteasome subunit alpha type-2		PRO_0000124083

Sequences

	Sequence		Length	Mass (Da)
	P40301-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: BC6F98060BD9D7C2	FASTA	234	25,907
	10 20 30 40 50 60 MATERYSFSL TTFSPSGKLV QLEYALAAVS GGAPSVGIIA SNGVVIATEN KHKSPLYEQH 70 80 90 100 110 120 SVHRVEMIYN HIGMVYSGMG PDYRLLVKQA RKIAQTYYLT YKEPIPVSQL VQRVATLMQE 130 140 150 160 170 180 YTQSGGVRPF GVSLLICGWD NDRPYLYQSD PSGAYFAWKA TAMGKNAVNG KTFLEKRYSE 190 200 210 220 230 DLELDDAVHT AILTLKEGFE GKMTADNIEI GICDQNGFQR LDPASIKDYL ASIP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and genomic organization of the Drosophila proteasome PROS-Dm25 gene." Seelig A., Troxell M., Kloetzel P.-M. Biochim. Biophys. Acta 1174:215-217(1993) [PubMed: 8357840] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Canton-S.
[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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X70304 Genomic DNA. Translation: CAA49783.1. AE014297 Genomic DNA. Translation: AAF54814.1. AY069280 mRNA. Translation: AAL39425.1.
PIR	S36116.
RefSeq	NP_524328.1.
UniGene	Dm.2198
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P23639.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:20541N.
IntAct	P40301. 24 interactions.
STRING	P40301.
Protein family/group databases
MEROPS	T01.972.
Proteomic databases
PRIDE	P40301.
Genome annotation databases
Ensembl	FBtr0082590; FBpp0082062; FBgn0086134; Drosophila melanogaster. [Genome view]
GeneID	41531.
KEGG	dme:Dmel_CG5266.
NMPDR	fig|7227.3.peg.12441.
Organism-specific databases
CTD	41531.
FlyBase	FBgn0086134. Pros25.
Phylogenomic databases
HOGENOM	P40301.
OMA	HIALLTL.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-011276-MON.
BRENDA	3.4.25.1. 48.
Gene expression databases
GermOnline	CG5266. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	824277.

Entry information

Entry name

PSA2_DROME

Accession

Primary (citable) accession number: P40301
Secondary accession number(s): Q9VG71

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project