ID PSA3_DROME Reviewed; 253 AA. AC Q9V5C6; O17313; Q8MKU6; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 29-OCT-2014, entry version 128. DE RecName: Full=Proteasome subunit alpha type-3; DE EC=3.4.25.1; DE AltName: Full=20S proteasome subunit alpha-7; GN Name=Prosalpha7; ORFNames=CG1519; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Belote J.M., Smyth K.A., Katz E., Miller M.; RT "Cloning of the Drosophila melanogaster alpha7 proteasome subunit RT gene."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] 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., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA 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., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA 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., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] 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., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Testis; RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., RA Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Embryo; RX PubMed=18327897; DOI=10.1021/pr700696a; RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; RT "Phosphoproteome analysis of Drosophila melanogaster embryos."; RL J. Proteome Res. 7:1675-1682(2008). RN [7] RP INTERACTION WITH NTC. RX PubMed=21529711; DOI=10.1016/j.cell.2011.03.021; RA Bader M., Benjamin S., Wapinski O.L., Smith D.M., Goldberg A.L., RA Steller H.; RT "A conserved F box regulatory complex controls proteasome activity in RT Drosophila."; RL Cell 145:371-382(2011). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex CC which is characterized by its ability to cleave peptides with Arg, CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. The proteasome has an ATP-dependent proteolytic CC activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000255|PROSITE-ProRule:PRU00808}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and CC two 19S regulatory subunits. The 20S proteasome core is composed CC of 28 subunits that are arranged in four stacked rings, resulting CC in a barrel-shaped structure. The two end rings are each formed by CC seven alpha subunits, and the two central rings are each formed by CC seven beta subunits. The catalytic chamber with the active sites CC is on the inside of the barrel (By similarity). Interacts with CC ntc. {ECO:0000250, ECO:0000269|PubMed:21529711}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1A family. CC {ECO:0000255|PROSITE-ProRule:PRU00808}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF025793; AAB82572.1; -; Genomic_DNA. DR EMBL; AE013599; AAF58889.1; -; Genomic_DNA. DR EMBL; AY069616; AAL39761.1; -; mRNA. DR EMBL; BT014669; AAT27293.1; -; mRNA. DR RefSeq; NP_724834.1; NM_165703.3. DR UniGene; Dm.2041; -. DR ProteinModelPortal; Q9V5C6; -. DR SMR; Q9V5C6; 2-237. DR BioGrid; 61847; 46. DR DIP; DIP-22157N; -. DR IntAct; Q9V5C6; 8. DR MINT; MINT-950398; -. DR MEROPS; T01.977; -. DR PaxDb; Q9V5C6; -. DR PRIDE; Q9V5C6; -. DR EnsemblMetazoa; FBtr0089998; FBpp0089041; FBgn0023175. DR GeneID; 36018; -. DR KEGG; dme:Dmel_CG1519; -. DR CTD; 36018; -. DR FlyBase; FBgn0023175; Prosalpha7. DR eggNOG; COG0638; -. DR GeneTree; ENSGT00550000074912; -. DR InParanoid; Q9V5C6; -. DR KO; K02727; -. DR OMA; VPDGRHF; -. DR OrthoDB; EOG73JKW6; -. DR PhylomeDB; Q9V5C6; -. DR Reactome; REACT_180649; Activation of NF-kappaB in B cells. DR Reactome; REACT_180655; ER-Phagosome pathway. DR Reactome; REACT_180671; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; REACT_180708; Antigen processing: Ubiquitination & Proteasome degradation. DR Reactome; REACT_181662; Separation of Sister Chromatids. DR Reactome; REACT_184330; Asymmetric localization of PCP proteins. DR Reactome; REACT_211248; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; REACT_215026; degradation of AXIN. DR Reactome; REACT_218589; Orc1 removal from chromatin. DR Reactome; REACT_225883; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; REACT_92044; APC/C:Cdc20 mediated degradation of Securin. DR GenomeRNAi; 36018; -. DR NextBio; 796366; -. DR PRO; PR:Q9V5C6; -. DR Bgee; Q9V5C6; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0005839; C:proteasome core complex; IDA:FlyBase. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR023332; Proteasome_suA-type. DR InterPro; IPR001353; Proteasome_sua/b. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; KW Protease; Proteasome; Reference proteome; Threonine protease. FT CHAIN 1 253 Proteasome subunit alpha type-3. FT /FTId=PRO_0000124097. FT MOD_RES 248 248 Phosphoserine. FT {ECO:0000269|PubMed:18327897}. FT CONFLICT 17 17 P -> A (in Ref. 1; AAB82572). FT {ECO:0000305}. FT CONFLICT 30 30 Missing (in Ref. 1; AAB82572). FT {ECO:0000305}. FT CONFLICT 62 62 D -> H (in Ref. 1; AAB82572). FT {ECO:0000305}. FT CONFLICT 140 157 Missing (in Ref. 5; AAT27293). FT {ECO:0000305}. FT CONFLICT 167 167 Missing (in Ref. 1; AAB82572). FT {ECO:0000305}. FT CONFLICT 182 182 M -> T (in Ref. 1; AAB82572). FT {ECO:0000305}. FT CONFLICT 235 253 ARKAGDAANKDEDSDNETH -> DEDTACGQQDEGRRQRQ FT (in Ref. 1; AAB82572). {ECO:0000305}. SQ SEQUENCE 253 AA; 27675 MW; 7B19D8DA350E2B7E CRC64; MSTIGTGYDL SASQFSPDGR VFQIDYASKA VEKSGTVIGI RGKDAVVLAV EKIITSKLYE PDAGGRIFTI EKNIGMAVAG LVADGNFVAD IARQEAANYR QQFEQAIPLK HLCHRVAGYV HAYTLYSAVR PFGLSIILAS WDEVEGPQLY KIEPSGSSFG YFACASGKAK QLAKTEMEKL KMDMRTDELV ESAGEIIYKV HDELKDKDFR FEMGLVGRVT GGLHLINPSE LTEKARKAGD AANKDEDSDN ETH //