ID   PSA1_DICDI              Reviewed;         248 AA.
AC   Q27562; Q54SK2;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=Proteasome subunit C2;
GN   Name=psmA1; Synonyms=prtC; ORFNames=DDB_G0282363;
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=AX4;
RX   PubMed=8986798; DOI=10.1073/pnas.93.26.15260;
RA   Shaulsky G., Escalante R., Loomis W.F.;
RT   "Developmental signal transduction pathways uncovered by genetic
RT   suppressors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:15260-15265(1996).
RN   [2]
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; U60168; AAB03506.1; -; Genomic_DNA.
DR   EMBL; AAFI02000047; EAL66041.1; -; Genomic_DNA.
DR   RefSeq; XP_640037.1; XM_634945.1.
DR   AlphaFoldDB; Q27562; -.
DR   SMR; Q27562; -.
DR   BioGRID; 1248566; 1.
DR   STRING; 44689.DDB0214956; -.
DR   MEROPS; T01.976; -.
DR   PaxDb; Q27562; -.
DR   EnsemblProtists; EAL66041; EAL66041; DDB_G0282363.
DR   GeneID; 8623563; -.
DR   KEGG; ddi:DDB_G0282363; -.
DR   dictyBase; DDB_G0282363; psmA1.
DR   eggNOG; KOG0863; Eukaryota.
DR   HOGENOM; CLU_035750_8_0_1; -.
DR   InParanoid; Q27562; -.
DR   OMA; NTQVYGK; -.
DR   PhylomeDB; Q27562; -.
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:Q27562; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IPI:dictyBase.
DR   GO; GO:0005634; C:nucleus; IPI:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA: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; ISS:dictyBase.
DR   CDD; cd03749; proteasome_alpha_type_1; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PTHR11599:SF12; 1.
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..248
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124067"
SQ   SEQUENCE   248 AA;  27988 MW;  42C717B37BDA0F3B CRC64;
     MYRNQYDSDI TTFSPSGRIH QIEYAMEAVK QGGAAVALKS KQFAVLVSLK RSSSELGSYQ
     KKIFVVDDHV GIAISGLTAD ARMLCNYMRN ECSNYNYVYE SQMRVERLVT KVADKHQVHT
     QRYGRRPYGV GLLVAGYDQL GAHIYQTCPS GNFYDYKSIS IGSRSQSAKT YLEKHFESFE
     ECTLEQLITH GLRALRETIP NTDDTLNSKN VSIGIVGEGQ PFKIIEEADA QPYLNLLENE
     EPVEMQTN