Reviewed, UniProtKB/Swiss-Prot Q9VA12 (PSA4L_DROME)

Names and origin

Protein names

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

Gene names

Name:	Prosalpha3T
ORF Names:	CG1736

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	251 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	Nucleus. Ref.1
Tissue specificity	Testis, prominent after meiosis II. After meiosis, predominantly localized to the haploid spermatid nuclei of the 64-cell cysts, remaining during the elongation and condensation of the spermatid nuclei. In mature, motile sperm, expression is seen exclusively in the sperm head. Ref.1
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	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 – 251	251	Proteasome subunit alpha type-4-like		PRO_0000124110
Experimental info
	Sequence conflict	74 – 75	2	CA → WP in AAN63094. Ref.1
	Sequence conflict	133	1	F → L in AAN63094. Ref.1
	Sequence conflict	141 – 142	2	RF → AS in AAN63094. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VA12-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B1AFF83978DB14D3	FASTA	251	28,169
	10 20 30 40 50 60 MARFFDSRTT IFSPEGRLYQ VEYAMEAASQ SGTCVGLLAK NGVLLATERS VDKLMDTSIP 70 80 90 100 110 120 VPRISWLNEN IACCATGNTA DGNVLVNQLR MIAQQYQFNF GEMIPCEQLV TNLCDIKQAY 130 140 150 160 170 180 TQYGGKRPFG VSFLYMGWDC RFGFQLYQSD PSGNYSGWKA TCIGRKSGAA MEMLQKELFS 190 200 210 220 230 240 KGYVSPSVEE AKDVAIKVMG MTLGRDSLTP EKLEIAFVQR YGNTTVFHIL EKNEIHRLIE 250 RNNNLKRRVG S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster." Ma J., Katz E., Belote J.M. Insect Mol. Biol. 11:627-639(2002) [PubMed: 12421421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Testis.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF57116.1. AY147240 Genomic DNA. Translation: AAN63094.1.
RefSeq	NP_651843.1.
UniGene	Dm.25072
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P23638.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9VA12.
Protein family/group databases
MEROPS	T01.973.
Proteomic databases
PRIDE	Q9VA12.
Genome annotation databases
Ensembl	FBtr0085738; FBpp0085100; FBgn0039819; Drosophila melanogaster. [Genome view]
GeneID	43679.
KEGG	dme:Dmel_CG1736.
NMPDR	fig|7227.3.peg.15548.
UCSC	CG1736-RA. d. melanogaster.
Organism-specific databases
CTD	43679.
FlyBase	FBgn0039819. Prosalpha3T.
Phylogenomic databases
HOGENOM	Q9VA12.
OMA	NENIACC.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-014273-MON.
BRENDA	3.4.25.1. 48.
Gene expression databases
GermOnline	CG1736. 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	835221.

Entry information

Entry name

PSA4L_DROME

Accession

Primary (citable) accession number: Q9VA12
Secondary accession number(s): Q8IS89

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project