ID   PSA4L_DROME             Reviewed;         251 AA.
AC   Q9VA12; B3DN24; Q8IS89;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Proteasome subunit alpha type-4-like;
GN   Name=Prosalpha3T; ORFNames=CG1736;
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], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12421421; DOI=10.1046/j.1365-2583.2002.00374.x;
RA   Ma J., Katz E., Belote J.M.;
RT   "Expression of proteasome subunit isoforms during spermatogenesis in
RT   Drosophila melanogaster.";
RL   Insect Mol. Biol. 11:627-639(2002).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (MAY-2008) 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: Nucleus {ECO:0000269|PubMed:12421421}.
CC   -!- TISSUE SPECIFICITY: Testis, prominent after meiosis II. After meiosis,
CC       predominantly localized to the haploid spermatid nuclei of the 64-cell
CC       cysts, remaining during the elongation and condensation of the
CC       spermatid nuclei. In mature, motile sperm, expression is seen
CC       exclusively in the sperm head. {ECO:0000269|PubMed:12421421}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACD81826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014297; AAF57116.1; -; Genomic_DNA.
DR   EMBL; AY147240; AAN63094.1; -; Genomic_DNA.
DR   EMBL; BT032812; ACD81826.1; ALT_INIT; mRNA.
DR   RefSeq; NP_651843.1; NM_143586.3.
DR   AlphaFoldDB; Q9VA12; -.
DR   SMR; Q9VA12; -.
DR   BioGRID; 68527; 1.
DR   STRING; 7227.FBpp0085100; -.
DR   PaxDb; 7227-FBpp0085100; -.
DR   DNASU; 43679; -.
DR   EnsemblMetazoa; FBtr0085738; FBpp0085100; FBgn0261395.
DR   GeneID; 43679; -.
DR   KEGG; dme:Dmel_CG1736; -.
DR   UCSC; CG1736-RA; d. melanogaster.
DR   AGR; FB:FBgn0261395; -.
DR   CTD; 43679; -.
DR   FlyBase; FBgn0261395; Prosalpha3T.
DR   VEuPathDB; VectorBase:FBgn0261395; -.
DR   eggNOG; KOG0178; Eukaryota.
DR   GeneTree; ENSGT00550000074827; -.
DR   HOGENOM; CLU_035750_4_3_1; -.
DR   InParanoid; Q9VA12; -.
DR   OMA; FLYMGWD; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; Q9VA12; -.
DR   BioGRID-ORCS; 43679; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 43679; -.
DR   PRO; PR:Q9VA12; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0261395; Expressed in testis and 8 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:FlyBase.
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:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 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; Q9VA12; DM.
PE   2: Evidence at transcript level;
KW   Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..251
FT                   /note="Proteasome subunit alpha type-4-like"
FT                   /id="PRO_0000124110"
FT   CONFLICT        74..75
FT                   /note="CA -> WP (in Ref. 1; AAN63094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="F -> L (in Ref. 1; AAN63094)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141..142
FT                   /note="RF -> AS (in Ref. 1; AAN63094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   251 AA;  28169 MW;  B1AFF83978DB14D3 CRC64;
     MARFFDSRTT IFSPEGRLYQ VEYAMEAASQ SGTCVGLLAK NGVLLATERS VDKLMDTSIP
     VPRISWLNEN IACCATGNTA DGNVLVNQLR MIAQQYQFNF GEMIPCEQLV TNLCDIKQAY
     TQYGGKRPFG VSFLYMGWDC RFGFQLYQSD PSGNYSGWKA TCIGRKSGAA MEMLQKELFS
     KGYVSPSVEE AKDVAIKVMG MTLGRDSLTP EKLEIAFVQR YGNTTVFHIL EKNEIHRLIE
     RNNNLKRRVG S
//