ID   PSA72_DROME             Reviewed;         249 AA.
AC   Q24178; Q6QH19; Q8T8U0; Q9VDJ1;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Proteasome subunit alpha type-7-1A;
DE   AltName: Full=Testis-specific alpha4-t1 proteasome subunit;
DE   AltName: Full=Testis-specific proteasome 28 kDa subunit 1A;
GN   Name=Prosalpha4T1; Synonyms=Pros28.1A; ORFNames=CG17268;
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 [GENOMIC DNA].
RX   PubMed=8878681; DOI=10.1093/genetics/144.1.147;
RA   Yuan X., Miller M., Belote J.M.;
RT   "Duplicated proteasome subunit genes in Drosophila melanogaster encoding
RT   testes-specific isoforms.";
RL   Genetics 144:147-157(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CPA-129, CPA-46, Z(H)12, Z(H)16, and Z(H)34;
RX   PubMed=15579695; DOI=10.1534/genetics.104.027631;
RA   Torgerson D.G., Singh R.S.;
RT   "Rapid evolution through gene duplication and subfunctionalization of the
RT   testes-specific alpha4 proteasome subunits in Drosophila.";
RL   Genetics 168:1421-1432(2004).
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=Testis;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Testis specific.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; U46008; AAC47280.1; -; Genomic_DNA.
DR   EMBL; AY542403; AAS86247.1; -; Genomic_DNA.
DR   EMBL; AY542404; AAS86248.1; -; Genomic_DNA.
DR   EMBL; AY542405; AAS86249.1; -; Genomic_DNA.
DR   EMBL; AY542406; AAS86250.1; -; Genomic_DNA.
DR   EMBL; AY542407; AAS86251.1; -; Genomic_DNA.
DR   EMBL; AY542408; AAS86252.1; -; Genomic_DNA.
DR   EMBL; AY542409; AAS86253.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55802.1; -; Genomic_DNA.
DR   EMBL; AY075276; AAL68143.1; -; mRNA.
DR   PIR; S72225; S72225.
DR   RefSeq; NP_650910.1; NM_142653.3.
DR   AlphaFoldDB; Q24178; -.
DR   SMR; Q24178; -.
DR   BioGRID; 67432; 1.
DR   DIP; DIP-19969N; -.
DR   IntAct; Q24178; 2.
DR   STRING; 7227.FBpp0083336; -.
DR   PaxDb; 7227-FBpp0083336; -.
DR   EnsemblMetazoa; FBtr0083928; FBpp0083336; FBgn0265606.
DR   GeneID; 42457; -.
DR   KEGG; dme:Dmel_CG17268; -.
DR   AGR; FB:FBgn0265606; -.
DR   CTD; 42457; -.
DR   FlyBase; FBgn0265606; Prosalpha4T1.
DR   VEuPathDB; VectorBase:FBgn0265606; -.
DR   eggNOG; KOG0183; Eukaryota.
DR   HOGENOM; CLU_035750_4_0_1; -.
DR   InParanoid; Q24178; -.
DR   OMA; DHHVGMA; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; Q24178; -.
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-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-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-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   SignaLink; Q24178; -.
DR   BioGRID-ORCS; 42457; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 42457; -.
DR   PRO; PR:Q24178; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0265606; Expressed in testis and 6 other cell types or tissues.
DR   ExpressionAtlas; Q24178; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:FlyBase.
DR   CDD; cd03755; proteasome_alpha_type_7; 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; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF15; PROTEASOME SUBUNIT ALPHA TYPE-7-1-RELATED; 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; Q24178; DM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..249
FT                   /note="Proteasome subunit alpha type-7-1A"
FT                   /id="PRO_0000124154"
FT   VARIANT         29
FT                   /note="R -> P (in strain: CPA-46)"
FT   VARIANT         236
FT                   /note="N -> K (in strain: CPA-46)"
FT   CONFLICT        24
FT                   /note="A -> G (in Ref. 1; AAC47280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="C -> V (in Ref. 1; AAC47280)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127..128
FT                   /note="RP -> PS (in Ref. 1; AAC47280)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27940 MW;  18B642DE3F1AE453 CRC64;
     MSSRYGRALT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKS SVSEMQEDRT
     VRKISMLDRH VALAFAGLTA DARILINRGQ VECQSHRLNF ENQVTLEYIT RYLAQLKQKY
     TQCNGRRPFG ISCLIGGIDA DGSARLFHTE PSGIFHEYKA TATGRWANTV REFFEKAYSD
     HEVTTKCDAI KLAMRALLEV TQMSQMRLEV AVLENGKPMK MLDSVVISEI VKIVQNEKEL
     QAKAHKMKR
//