ID PSA3_CAEEL Reviewed; 250 AA. AC Q09583; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 175. DE RecName: Full=Proteasome subunit alpha type-3; DE AltName: Full=Proteasome subunit alpha 7; GN Name=pas-7; ORFNames=ZK945.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(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 (By CC similarity). {ECO:0000250}. 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 -!- INTERACTION: CC Q09583; O17586: pas-1; NbExp=6; IntAct=EBI-315406, EBI-315388; CC Q09583; O44156: pas-6; NbExp=5; IntAct=EBI-315406, EBI-318264; CC Q09583; Q09583: pas-7; NbExp=5; IntAct=EBI-315406, EBI-315406; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. 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; Z48544; CAA88436.2; -; Genomic_DNA. DR PIR; T28119; T28119. DR RefSeq; NP_496177.2; NM_063776.3. DR AlphaFoldDB; Q09583; -. DR SMR; Q09583; -. DR BioGRID; 39890; 59. DR IntAct; Q09583; 13. DR STRING; 6239.ZK945.2.1; -. DR EPD; Q09583; -. DR PaxDb; 6239-ZK945-2-1; -. DR PeptideAtlas; Q09583; -. DR EnsemblMetazoa; ZK945.2.1; ZK945.2.1; WBGene00003928. DR GeneID; 174571; -. DR KEGG; cel:CELE_ZK945.2; -. DR UCSC; ZK945.2.1; c. elegans. DR AGR; WB:WBGene00003928; -. DR WormBase; ZK945.2; CE36420; WBGene00003928; pas-7. DR eggNOG; KOG0184; Eukaryota. DR GeneTree; ENSGT00550000074912; -. DR HOGENOM; CLU_035750_0_0_1; -. DR InParanoid; Q09583; -. DR OMA; RVSMYMH; -. DR OrthoDB; 166567at2759; -. DR PhylomeDB; Q09583; -. DR PRO; PR:Q09583; -. DR Proteomes; UP000001940; Chromosome II. DR Bgee; WBGene00003928; Expressed in adult organism and 4 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB. DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd03751; proteasome_alpha_type_3; 1. 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:SF10; PROTEASOME SUBUNIT ALPHA TYPE-3; 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. PE 1: Evidence at protein level; KW Cytoplasm; Nucleus; Proteasome; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..250 FT /note="Proteasome subunit alpha type-3" FT /id="PRO_0000124095" SQ SEQUENCE 250 AA; 27752 MW; FC97B4486B924855 CRC64; MSSIGTGYDL AASTFSPDGR IFQVEYAQKA VDNAGTMIAI RGKNGVVVVA DKLISSKLYT DNANPRMFNV NDNVGVAVAG NYPDGFALKN YAYGEAMKWL KDYREPMPIQ NIANSVAEYI HIHTLGISRP FGAGAFFMSW NKQTGGRLFL VEPSGLNYEY KAWAVGKHRQ AAKAEIEKLK IEELDVNQLV KEAARIIMVV RDENKDKNVQ IEMGWVGEQT NGKYEEVPSE VVTAAEEWAI AKLDEDDMDD //