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 30-NOV-2010, entry version 95. 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; Arthropoda; Hexapoda; Insecta; Pterygota; OC 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 MEDLINE=20196006; 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, AND ALTERNATIVE SPLICING. RX MEDLINE=22426069; PubMed=12537572; 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] (ISOFORM A). RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; 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] (ISOFORM B). 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 MASS RP 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). 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). CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. 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). CC -!- INTERACTION: CC Q9W137:-; NbExp=1; IntAct=EBI-131307, EBI-140332; CC P12881:Pros35; NbExp=1; IntAct=EBI-131307, EBI-183209; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q9V5C6-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9V5C6-2; Sequence=VSP_011805; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Belongs to the peptidase T1A family. 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; AE013599; AAM68801.2; -; Genomic_DNA. DR EMBL; AY069616; AAL39761.1; -; mRNA. DR EMBL; BT014669; AAT27293.1; -; mRNA. DR RefSeq; NP_724834.1; NM_165703.2. DR UniGene; Dm.2041; -. DR ProteinModelPortal; Q9V5C6; -. DR SMR; Q9V5C6; 2-245. DR DIP; DIP-22157N; -. DR IntAct; Q9V5C6; 11. DR MINT; MINT-950398; -. DR STRING; Q9V5C6; -. DR MEROPS; T01.977; -. DR PRIDE; Q9V5C6; -. DR EnsemblMetazoa; FBtr0089998; FBpp0089041; FBgn0023175. DR GeneID; 36018; -. DR KEGG; dme:Dmel_CG1519; -. DR NMPDR; fig|7227.3.peg.4308; -. DR CTD; 36018; -. DR FlyBase; FBgn0023175; Prosalpha7. DR eggNOG; inNOG05444; -. DR InParanoid; Q9V5C6; -. DR OMA; DIPLKHL; -. DR OrthoDB; EOG9DFPV5; -. DR PhylomeDB; Q9V5C6; -. DR BRENDA; 3.4.25.1; 48. DR NextBio; 796366; -. DR Bgee; Q9V5C6; -. DR GermOnline; CG1519; Drosophila melanogaster. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006974; P:response to DNA damage stimulus; IMP:FlyBase. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR000426; Proteasome_asu_CS. 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 PROSITE; PS00388; PROTEASOME_A_1; 1. DR PROSITE; PS51475; PROTEASOME_A_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; KW Nucleus; Phosphoprotein; Protease; Proteasome; Threonine protease. FT CHAIN 1 253 Proteasome subunit alpha type-3. FT /FTId=PRO_0000124097. FT MOD_RES 248 248 Phosphoserine. FT VAR_SEQ 140 157 Missing (in isoform B). FT /FTId=VSP_011805. FT CONFLICT 17 17 P -> A (in Ref. 1; AAB82572). FT CONFLICT 30 30 Missing (in Ref. 1; AAB82572). FT CONFLICT 62 62 D -> H (in Ref. 1; AAB82572). FT CONFLICT 167 167 Missing (in Ref. 1; AAB82572). FT CONFLICT 182 182 M -> T (in Ref. 1; AAB82572). FT CONFLICT 235 253 ARKAGDAANKDEDSDNETH -> DEDTACGQQDEGRRQRQ FT (in Ref. 1; AAB82572). 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 //