PSA71_DROME
ID PSA71_DROME Reviewed; 249 AA.
AC P22769; Q9VXI9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Proteasome subunit alpha type-7-1;
DE AltName: Full=PROS-Dm28.1;
DE AltName: Full=Proteasome 28 kDa subunit 1;
GN Name=Prosalpha4; Synonyms=PROS-28.1, Pros28.1; ORFNames=CG3422;
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].
RX PubMed=2169443; DOI=10.1016/0378-1119(90)90185-t;
RA Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.;
RT "The Drosophila PROS-28.1 gene is a member of the proteasome gene family.";
RL Gene 90:235-241(1990).
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 [GENOMIC DNA].
RC STRAIN=b pr tk, 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 [4]
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 [5]
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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
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; this interaction is
CC reduced by PI31 ADP-ribosylation. {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; M57712; AAA62768.1; -; mRNA.
DR EMBL; X62286; CAA44174.1; -; Genomic_DNA.
DR EMBL; AY542383; AAS86210.1; -; Genomic_DNA.
DR EMBL; AY542384; AAS86211.1; -; Genomic_DNA.
DR EMBL; AY542385; AAS86212.1; -; Genomic_DNA.
DR EMBL; AY542386; AAS86213.1; -; Genomic_DNA.
DR EMBL; AY542387; AAS86214.1; -; Genomic_DNA.
DR EMBL; AY542388; AAS86215.1; -; Genomic_DNA.
DR EMBL; AY542389; AAS86216.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48573.1; -; Genomic_DNA.
DR EMBL; AY071241; AAL48863.1; -; mRNA.
DR PIR; JQ0681; JQ0681.
DR PIR; S23451; S23451.
DR RefSeq; NP_525092.1; NM_080353.5.
DR AlphaFoldDB; P22769; -.
DR SMR; P22769; -.
DR BioGRID; 58925; 52.
DR DIP; DIP-17376N; -.
DR IntAct; P22769; 14.
DR STRING; 7227.FBpp0073989; -.
DR iPTMnet; P22769; -.
DR PaxDb; P22769; -.
DR PRIDE; P22769; -.
DR DNASU; 32584; -.
DR EnsemblMetazoa; FBtr0074210; FBpp0073989; FBgn0004066.
DR GeneID; 32584; -.
DR KEGG; dme:Dmel_CG3422; -.
DR CTD; 32584; -.
DR FlyBase; FBgn0004066; Prosalpha4.
DR VEuPathDB; VectorBase:FBgn0004066; -.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000167759; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; P22769; -.
DR OMA; KICMLDH; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; P22769; -.
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-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; 32584; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 32584; -.
DR PRO; PR:P22769; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004066; Expressed in ovary and 43 other tissues.
DR Genevisible; P22769; DM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IDA:FlyBase.
DR GO; GO:0005839; C:proteasome core complex; IDA:FlyBase.
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; IC:FlyBase.
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 Pfam; PF10584; Proteasome_A_N; 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 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..249
FT /note="Proteasome subunit alpha type-7-1"
FT /id="PRO_0000124153"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 224
FT /note="T -> N (in Ref. 1; AAA62768)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 27973 MW; 56987932DADD02B3 CRC64;
MSSRYDRAVT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKK SVAQLQEDRK
VRKICMLDNH VVMAFAGLTA DARIMINRAQ VECQSHRLNV EDPVTLEYIT RFIAQLKQKY
TQSNGRRPFG ISCLIGGFDA DGSAHLFQTE PSGIFYEYKA NATGRSAKVV REFFEKSYRE
EEVANEHGAV KLAIRALLEV AQSGQNNLEV AIMENGKPLK MLDTDVITDY VKIIEKEKEE
ELEKKKQKK
