P18053 (PSA4_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-4
EC=3.4.25.1

Alternative name(s):
PROS-Dm29
Proteasome 29 kDa subunit

Gene names

Name:	Pros29
Synonyms:	PROS-29
ORF Names:	CG9327

Organism

Drosophila melanogaster (Fruit fly)

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	264 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 Reference 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 direct assay. Source: FlyBase microtubule associated complex Inferred from direct assay. Source: FlyBase nucleus Inferred from direct assay. Source: FlyBase proteasome core complex, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Pros25	P40301	3	EBI-138951,EBI-98978

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 264	264	Proteasome subunit alpha type-4		PRO_0000124109
Experimental info
	Sequence conflict	68	1	L → R in CAA36555. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P18053 [UniParc]. Last modified December 8, 2000. Version 2. Checksum: E5209BC634008B8B	FASTA	264	29,412
	10 20 30 40 50 60 MARRYDSRTT IFSPEGRLYQ VEYAMEAISH AGTCLGILAE DGILLAAECR STNKLLDSAI 70 80 90 100 110 120 PSEKIYRLND NMVCSVAGIT SDANVLTSEL RLIAQRYQFS YGEVIPCEQL VSHLCDIKQA 130 140 150 160 170 180 YTQYGGKRPF GVSLLYMGWD NKYGYQLYQS DPSGNYGGWK ATCIGNNFGA AISMLKQELA 190 200 210 220 230 240 DKENVKLTLA DAKDLAIKVL SMTLDTTKLT PEKVEMATLQ RVDNKTVYSV LEKPDVEKLI 250 260 EKYTKVQAEA EAAKKEKQAK QPTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Drosophila PROS-29 gene is a new member of the PROS-gene family." Haass C., Pesold-Hurt B., Kloetzel P.-M. Nucleic Acids Res. 18:4018-4018(1990) [PubMed: 2374736] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Oregon-R.
[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. 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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X52319 mRNA. Translation: CAA36555.1. AE013599 Genomic DNA. Translation: AAF46651.1. AY084140 mRNA. Translation: AAL89878.1.
PIR	S10318.
RefSeq	NP_476691.1. NM_057343.4.
3D structure databases
ProteinModelPortal	P18053.
SMR	P18053. Positions 2-240.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19125N.
IntAct	P18053. 5 interactions.
MINT	MINT-996465.
STRING	P18053.
Protein family/group databases
MEROPS	T01.973.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0071522; FBpp0071451; FBgn0261394.
GeneID	37378.
KEGG	dme:Dmel_CG9327.
NMPDR	fig|7227.3.peg.6551.
Organism-specific databases
CTD	37378.
FlyBase	FBgn0261394. Pros29.
Phylogenomic databases
eggNOG	inNOG08920.
GeneTree	EMGT00050000009409.
InParanoid	P18053.
OMA	MARRYDS.
OrthoDB	EOG4V41QM.
PhylomeDB	P18053.
Gene expression databases
Bgee	P18053.
GermOnline	CG9327. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_N. IPR016050. Proteasome_bsu_CS. IPR023332. Proteasome_suA-type. IPR001353. Proteasome_sua/b. [Graphical view]
KO	K02728.
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
SMART	SM00948. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A_1. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	803347.

Entry information

Entry name

PSA4_DROME

Accession

Primary (citable) accession number: P18053
Secondary accession number(s): Q9W2N9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	December 8, 2000
Last modified:	January 25, 2012
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project