ID   PSA1_DROME              Reviewed;         279 AA.
AC   P12881; Q8SZ22; Q9VL23;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   24-JAN-2024, entry version 207.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=PROS-Dm35;
DE   AltName: Full=Proteasome 35 kDa subunit;
GN   Name=Prosalpha6; Synonyms=PROS-35, Pros35; ORFNames=CG4904;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 4-18 AND 194-206.
RC   STRAIN=Oregon-R;
RX   PubMed=2477245; DOI=10.1002/j.1460-2075.1989.tb08366.x;
RA   Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.;
RT   "The PROS-35 gene encodes the 35 kd protein subunit of Drosophila
RT   melanogaster proteasome.";
RL   EMBO J. 8:2373-2379(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oregon-R;
RX   PubMed=1374331; DOI=10.1111/j.1432-1033.1992.tb16872.x;
RA   Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H.,
RA   Kloetzel P.-M.;
RT   "Molecular characterization of the genomic regions of the Drosophila alpha-
RT   type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35.";
RL   Eur. J. Biochem. 205:1043-1051(1992).
RN   [3]
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., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., 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., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., 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., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
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., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
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., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   INTERACTION WITH PI31.
RX   PubMed=23622245; DOI=10.1016/j.cell.2013.03.040;
RA   Cho-Park P.F., Steller H.;
RT   "Proteasome regulation by ADP-ribosylation.";
RL   Cell 153:614-627(2013).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC       is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC       Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC       pH. The proteasome has an ATP-dependent proteolytic activity.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is composed of 28
CC       subunits that are arranged in four stacked rings, resulting in a
CC       barrel-shaped structure. The two end rings are each formed by seven
CC       alpha subunits, and the two central rings are each formed by seven beta
CC       subunits. The catalytic chamber with the active sites is on the inside
CC       of the barrel (By similarity). Interacts with PI31. {ECO:0000250,
CC       ECO:0000269|PubMed:23622245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; X15497; CAA33520.1; -; mRNA.
DR   EMBL; X62285; CAA44173.1; -; Genomic_DNA.
DR   EMBL; AE014134; AAF52875.1; -; Genomic_DNA.
DR   EMBL; AY071178; AAL48800.1; -; mRNA.
DR   PIR; S23450; SNFF5K.
DR   RefSeq; NP_001285798.1; NM_001298869.1.
DR   RefSeq; NP_523532.1; NM_078808.4.
DR   AlphaFoldDB; P12881; -.
DR   SMR; P12881; -.
DR   BioGRID; 60450; 54.
DR   DIP; DIP-22159N; -.
DR   IntAct; P12881; 15.
DR   MINT; P12881; -.
DR   STRING; 7227.FBpp0310201; -.
DR   PaxDb; 7227-FBpp0079538; -.
DR   EnsemblMetazoa; FBtr0079948; FBpp0079538; FBgn0250843.
DR   EnsemblMetazoa; FBtr0343606; FBpp0310201; FBgn0250843.
DR   GeneID; 34359; -.
DR   KEGG; dme:Dmel_CG4904; -.
DR   AGR; FB:FBgn0250843; -.
DR   CTD; 34359; -.
DR   FlyBase; FBgn0250843; Prosalpha6.
DR   VEuPathDB; VectorBase:FBgn0250843; -.
DR   eggNOG; KOG0863; Eukaryota.
DR   GeneTree; ENSGT00550000074855; -.
DR   HOGENOM; CLU_035750_8_0_1; -.
DR   InParanoid; P12881; -.
DR   OMA; NTQVYGK; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; P12881; -.
DR   Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DME-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DME-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-DME-202424; Downstream TCR signaling.
DR   Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
DR   Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT.
DR   Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
DR   Reactome; R-DME-216167; Nuclear CI is degraded.
DR   Reactome; R-DME-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-DME-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DME-432395; Degradation of TIM.
DR   Reactome; R-DME-432524; Degradation of PER.
DR   Reactome; R-DME-432626; Circadian Clock pathway.
DR   Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-DME-4641257; Degradation of AXIN.
DR   Reactome; R-DME-4641258; Degradation of DVL.
DR   Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DME-538864; Degradation of CRY.
DR   Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-DME-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-DME-5632684; Hedgehog 'on' state.
DR   Reactome; R-DME-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-DME-5689603; UCH proteinases.
DR   Reactome; R-DME-5689880; Ub-specific processing proteases.
DR   Reactome; R-DME-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-DME-68949; Orc1 removal from chromatin.
DR   Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DME-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DME-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DME-8951664; Neddylation.
DR   Reactome; R-DME-9020702; Interleukin-1 signaling.
DR   Reactome; R-DME-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DME-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   BioGRID-ORCS; 34359; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 34359; -.
DR   PRO; PR:P12881; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0250843; Expressed in egg cell and 41 other cell types or tissues.
DR   ExpressionAtlas; P12881; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR   GO; GO:0000502; C:proteasome complex; IDA:FlyBase.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:FlyBase.
DR   GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
DR   CDD; cd03749; proteasome_alpha_type_1; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR   Genevisible; P12881; DM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..279
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124068"
FT   REGION          235..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..261
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         103
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        189
FT                   /note="R -> H (in Ref. 5; AAL48800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   279 AA;  31059 MW;  1478BDC2C61EF3F1 CRC64;
     MFRNQYDSDV TVWSPQGRLH QVEYAMEAVK LGTATVGLKN KDYAVLVALC KPTSELSDTQ
     RKIIPIDDHL GISIAGLTAD ARVLSRYLRS ECLNYKHSYD TTYPVSRLIT NLGNKMQTTT
     QRYDRRPYGV GLLVAGYDER GPHIYQVTPS ATFFNCKANS IGSRSQSART YLEKNLNKFL
     DSSKDEIIRH GIRAILGTLP TDEQGKDAGQ YDITVAIVGK DQPFTILSNK DSAKHVAIAK
     ENDNDTPRND DDDDRPSPPE EPAAGPRDPE VLVATEQRP
//