ID   PSA7_DICDI              Reviewed;         250 AA.
AC   P34120; Q558X6;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Proteasome subunit alpha type-7;
DE   AltName: Full=Proteasome component DD5;
GN   Name=psmA7; Synonyms=prdE; ORFNames=DDB_G0272831;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX2;
RX   PubMed=8130037; DOI=10.1006/jsbi.1993.1044;
RA   Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A.,
RA   Gerisch G., Baumeister W.;
RT   "Proteasomes from Dictyostelium discoideum: characterization of structure
RT   and function.";
RL   J. Struct. Biol. 111:135-147(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; L22213; AAA33234.1; -; Genomic_DNA.
DR   EMBL; AAFI02000008; EAL71053.1; -; Genomic_DNA.
DR   RefSeq; XP_644940.1; XM_639848.1.
DR   AlphaFoldDB; P34120; -.
DR   SMR; P34120; -.
DR   STRING; 44689.DDB0185059; -.
DR   PaxDb; P34120; -.
DR   EnsemblProtists; EAL71053; EAL71053; DDB_G0272831.
DR   GeneID; 8618619; -.
DR   KEGG; ddi:DDB_G0272831; -.
DR   dictyBase; DDB_G0272831; psmA7.
DR   eggNOG; KOG0183; Eukaryota.
DR   HOGENOM; CLU_035750_4_0_1; -.
DR   InParanoid; P34120; -.
DR   OMA; KICMLDH; -.
DR   PhylomeDB; P34120; -.
DR   Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DDI-4641258; Degradation of DVL.
DR   Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR   Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DDI-5689603; UCH proteinases.
DR   Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR   Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR   Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DDI-8951664; Neddylation.
DR   Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P34120; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR   GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR   GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:dictyBase.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProt.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IDA:dictyBase.
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   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   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..250
FT                   /note="Proteasome subunit alpha type-7"
FT                   /id="PRO_0000124152"
SQ   SEQUENCE   250 AA;  27637 MW;  49D83DBB57A91D4D CRC64;
     MSSARYDRAI TVFSPDGHLF QVEYAMEAVR KGTVAVGVRG KDVIVLGVEK KATAKLQDAR
     SIRKIVKLDD HICLTFAGLT ADSRVLISKA LMECQSYRLT VEDSPSVEYI SKFIAGIQQR
     YTQSGGVRPF GISTLIVGFD TDGTPNLYQT DPSGSYSSWK AAAIGRSSKS VGEFLEKNYT
     DVSEEESIKL AVRALLEIVE SGNKNIEIAV IRNKQPIVLL DEQEIDKLVA VVEAEKEIQK
     EQEKSEKQQK