ID   PSA73_DROVI             Reviewed;         245 AA.
AC   O16812;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Proteasome subunit alpha type-7-1B;
DE   AltName: Full=Testis-specific proteasome 28 kDa subunit 1B;
GN   Name=Pros28.1B;
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   PubMed=9666090; DOI=10.1016/s0378-1119(98)00256-x;
RA   Belote J.M., Miller M., Smyth K.A.;
RT   "Evolutionary conservation of a testes-specific proteasome subunit gene in
RT   Drosophila.";
RL   Gene 215:93-100(1998).
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}.
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; AF017650; AAC34197.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16812; -.
DR   SMR; O16812; -.
DR   STRING; 7244.FBpp0233774; -.
DR   eggNOG; KOG0183; Eukaryota.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.20.10; -; 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   Pfam; PF00227; Proteasome; 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   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Proteasome.
FT   CHAIN           1..245
FT                   /note="Proteasome subunit alpha type-7-1B"
FT                   /id="PRO_0000124157"
SQ   SEQUENCE   245 AA;  27475 MW;  C44DF83375853971 CRC64;
     MSRFDESVNI YSDGHLLQVE YAQEAVRKGS TVGLRTKECV VLGVEKRAID SLQIERTSRK
     IKKIDQHMAM TFAGLTADAR VLVSRAQVEA QSHRLNFDRP ASVEYITRYL ARLKQTYTQS
     VARRPFGVSC LIGGFDEDGR PRLFQTDPSG IYYEWSANTT GRLGQTVNEY LEKNTAAISR
     TPDAASAMKH VVRALFTATS LDPASIELAV LRYWQPIEMV KPETLEYLLG VIKQEAVEEA
     LTKAP