ID   PSA1_CAEEL              Reviewed;         260 AA.
AC   O44156;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=Proteasome subunit alpha 6;
GN   Name=pas-6; ORFNames=CD4.6;
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       O44156; Q27488: pas-2; NbExp=3; IntAct=EBI-318264, EBI-318271;
CC       O44156; Q09583: pas-7; NbExp=5; IntAct=EBI-318264, 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}.
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DR   EMBL; FO080609; CCD65121.1; -; Genomic_DNA.
DR   PIR; T32525; T32525.
DR   RefSeq; NP_504472.1; NM_072071.5.
DR   AlphaFoldDB; O44156; -.
DR   SMR; O44156; -.
DR   BioGRID; 43992; 44.
DR   IntAct; O44156; 10.
DR   STRING; 6239.CD4.6.1; -.
DR   MEROPS; T01.976; -.
DR   EPD; O44156; -.
DR   PaxDb; 6239-CD4-6; -.
DR   PeptideAtlas; O44156; -.
DR   EnsemblMetazoa; CD4.6.1; CD4.6.1; WBGene00003927.
DR   GeneID; 178943; -.
DR   KEGG; cel:CELE_CD4.6; -.
DR   UCSC; CD4.6.1; c. elegans.
DR   AGR; WB:WBGene00003927; -.
DR   WormBase; CD4.6; CE16954; WBGene00003927; pas-6.
DR   eggNOG; KOG0863; Eukaryota.
DR   GeneTree; ENSGT00550000074855; -.
DR   HOGENOM; CLU_035750_8_0_1; -.
DR   InParanoid; O44156; -.
DR   OMA; NTQVYGK; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; O44156; -.
DR   Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR   Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-CEL-4641258; Degradation of DVL.
DR   Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR   Reactome; R-CEL-5689603; UCH proteinases.
DR   Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR   Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR   Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-CEL-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-CEL-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O44156; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00003927; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03749; proteasome_alpha_type_1; 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; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 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   World-2DPAGE; 0020:O44156; -.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..260
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124066"
FT   REGION          240..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  28311 MW;  D8EEEF5E480F8F70 CRC64;
     MFRNQYDGDV TVWSPQGRLH QVEYAVEAMK QGSATVGIKS ETHAVIVALK RAQNDLSSHQ
     KKVYEIDTHA GVSIAGLLSD GRILARYLQT ECSSWRWDYK QAVPIKKLAE SMQLKLQANT
     QYYGRRPFGV GILIAGYDKD GAHIIQTDPS AEVVSMHGTS IGARSQSART YLERNVDNFE
     KSTPEQLIVH ALLALRDTLP AEENLNAQNT SIGIVGKDSP FSLLEDAQVA VHLNQVSTHP
     RTTGGAAAAA APGGAEPMQM
//