ID   PSA73_DROME             Reviewed;         252 AA.
AC   Q27575; Q6QH11; Q8T3X2; Q9W162;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Proteasome subunit alpha type-7-1B;
DE   AltName: Full=Testis-specific alpha4-t2 proteasome subunit;
DE   AltName: Full=Testis-specific proteasome 28 kDa subunit 1B;
GN   Name=Prosalpha4T2; Synonyms=Pros28.1B; ORFNames=CG4569;
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].
RC   TISSUE=Testis;
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, S-23, 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;
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).
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; U46009; AAC47281.1; -; Genomic_DNA.
DR   EMBL; AY542417; AAS86225.1; -; Genomic_DNA.
DR   EMBL; AY542418; AAS86226.1; -; Genomic_DNA.
DR   EMBL; AY542421; AAS86229.1; -; Genomic_DNA.
DR   EMBL; AY542422; AAS86230.1; -; Genomic_DNA.
DR   EMBL; AY542423; AAS86231.1; -; Genomic_DNA.
DR   EMBL; AY542424; AAS86232.1; -; Genomic_DNA.
DR   EMBL; AY542425; AAS86233.1; -; Genomic_DNA.
DR   EMBL; AY542426; AAS86234.1; -; Genomic_DNA.
DR   EMBL; AY542427; AAS86235.1; -; Genomic_DNA.
DR   EMBL; AE013599; AAF47215.1; -; Genomic_DNA.
DR   EMBL; AY089456; AAL90194.1; -; mRNA.
DR   PIR; S72226; S72226.
DR   RefSeq; NP_001286844.1; NM_001299915.1.
DR   RefSeq; NP_611920.1; NM_138076.4.
DR   AlphaFoldDB; Q27575; -.
DR   SMR; Q27575; -.
DR   STRING; 7227.FBpp0310089; -.
DR   PaxDb; 7227-FBpp0072257; -.
DR   DNASU; 37910; -.
DR   EnsemblMetazoa; FBtr0072350; FBpp0072257; FBgn0017556.
DR   EnsemblMetazoa; FBtr0343481; FBpp0310089; FBgn0017556.
DR   GeneID; 37910; -.
DR   KEGG; dme:Dmel_CG4569; -.
DR   AGR; FB:FBgn0017556; -.
DR   CTD; 37910; -.
DR   FlyBase; FBgn0017556; Prosalpha4T2.
DR   VEuPathDB; VectorBase:FBgn0017556; -.
DR   eggNOG; KOG0183; Eukaryota.
DR   GeneTree; ENSGT00940000167759; -.
DR   HOGENOM; CLU_035750_4_0_1; -.
DR   InParanoid; Q27575; -.
DR   OMA; KYKQPLR; -.
DR   OrthoDB; 3534174at2759; -.
DR   PhylomeDB; Q27575; -.
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   BioGRID-ORCS; 37910; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 37910; -.
DR   PRO; PR:Q27575; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0017556; Expressed in testis and 9 other cell types or tissues.
DR   ExpressionAtlas; Q27575; 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   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; Q27575; DM.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..252
FT                   /note="Proteasome subunit alpha type-7-1B"
FT                   /id="PRO_0000124155"
FT   VARIANT         45
FT                   /note="I -> L (in strain: S-23)"
FT   VARIANT         191
FT                   /note="I -> V (in strain: S-23)"
FT   VARIANT         213
FT                   /note="V -> E (in strain: S-23)"
FT   VARIANT         241
FT                   /note="D -> A (in strain: S-23)"
FT   CONFLICT        3..4
FT                   /note="QR -> HG (in Ref. 1; AAC47281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        188..190
FT                   /note="AAA -> RG (in Ref. 1; AAC47281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="K -> N (in Ref. 5; AAL90194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243..249
FT                   /note="AEASRRP -> PSESA (in Ref. 1; AAC47281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="A -> V (in Ref. 5; AAL90194)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   252 AA;  28720 MW;  00116788A4813146 CRC64;
     MAQRYDRAVT IYSPDGHLLQ VEYAQEAVRR GSTVMGLRTN NAIVIGVEKR SVGDLQEERM
     VRKICMLDDH VVMTFSGLTA DARILVSRAQ MEAQSHRLNF EKPTTVEYIT RYIAQLKQNY
     TQSNGRRPFG LSCLVGGFDE DGTPHLFQTD PSGIFYEWRA NTTGRSSQPV RDYMEKHADE
     ILTIADEAAA IKHIVRTLVS VSSLNHTQME VAVLKYRQPL RMIDHQVLAD LERTVRREIE
     DEAEASRRPR AP
//