ID PSA1_RAT Reviewed; 263 AA. AC P18420; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 02-SEP-2026, entry version 195. DE RecName: Full=Proteasome subunit alpha type-1; DE AltName: Full=Macropain subunit C2; DE AltName: Full=Multicatalytic endopeptidase complex subunit C2; DE AltName: Full=Proteasome component C2; DE AltName: Full=Proteasome nu chain; GN Name=Psma1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=2819072; DOI=10.1021/bi00444a028; RA Fujiwara T., Tanaka K., Kumatori A., Shin S., Yoshimura T., Ichihara A., RA Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.; RT "Molecular cloning of cDNA for proteasomes (multicatalytic proteinase RT complexes) from rat liver: primary structure of the largest component RT (C2)."; RL Biochemistry 28:7332-7340(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 1-30, AND ACETYLATION AT MET-1. RC TISSUE=Liver; RX PubMed=2335242; DOI=10.1016/0014-5793(90)81417-m; RA Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., RA Shimonishi Y.; RT "The NH2-terminal residues of rat liver proteasome (multicatalytic RT proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."; RL FEBS Lett. 263:373-375(1990). RN [4] RP PROTEIN SEQUENCE OF 63-82 AND 97-107, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus; RA Lubec G., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the CC proteolytic degradation of most intracellular proteins. This complex CC plays numerous essential roles within the cell by associating with CC different regulatory particles. Associated with two 19S regulatory CC particles, forms the 26S proteasome and thus participates in the ATP- CC dependent degradation of ubiquitinated proteins. The 26S proteasome CC plays a key role in the maintenance of protein homeostasis by removing CC misfolded or damaged proteins that could impair cellular functions, and CC by removing proteins whose functions are no longer required. Associated CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin- CC independent protein degradation. This type of proteolysis is required CC in several pathways including spermatogenesis (20S-PA200 complex) or CC generation of a subset of MHC class I-presented antigenic peptides CC (20S-PA28 complex). {ECO:0000250|UniProtKB:P25786}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped CC complex made of 28 subunits that are arranged in four stacked rings. CC The two outer rings are each formed by seven alpha subunits, and the CC two inner rings are formed by seven beta subunits. The proteolytic CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. CC Interacts with NOTCH3. Interacts with ZFAND1 (By similarity). CC {ECO:0000250|UniProtKB:P25786}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus CC {ECO:0000250|UniProtKB:P25786}. Note=Translocated from the cytoplasm CC into the nucleus following interaction with AKIRIN2, which bridges the CC proteasome with the nuclear import receptor IPO9. CC {ECO:0000250|UniProtKB:P25786}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Proteolytically cleaved from a C-terminal extension in the course CC of the conversion of the proteasome from its latent form into its CC active form. 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; M29859; AAA41943.1; -; mRNA. DR EMBL; D90265; BAA14312.1; -; mRNA. DR EMBL; BC062233; AAH62233.1; -; mRNA. DR PIR; A32968; SNRTC2. DR RefSeq; NP_058974.1; NM_017278.1. DR PDB; 6EPC; EM; 12.30 A; F=1-263. DR PDB; 6EPD; EM; 15.40 A; F=1-263. DR PDB; 6EPE; EM; 12.80 A; F=1-263. DR PDB; 6EPF; EM; 11.80 A; F=1-263. DR PDB; 6TU3; EM; 2.70 A; F/T=1-263. DR AlphaFoldDB; P18420; -. DR EMDB; EMD-10586; -. DR EMDB; EMD-3913; -. DR EMDB; EMD-3914; -. DR EMDB; EMD-3915; -. DR EMDB; EMD-3916; -. DR SMR; P18420; -. DR BioGRID; 248289; 2. DR ComplexPortal; CPX-8965; 30S proteasome complex. DR FunCoup; P18420; 3131. DR IntAct; P18420; 1. DR STRING; 10116.ENSRNOP00000015946; -. DR GlyCosmos; P18420; 1 site, No reported glycans. DR GlyGen; P18420; 1 site. DR iPTMnet; P18420; -. DR PhosphoSitePlus; P18420; -. DR SwissPalm; P18420; -. DR jPOST; P18420; -. DR PaxDb; 10116-ENSRNOP00000015946; -. DR GeneID; 29668; -. DR KEGG; rno:29668; -. DR UCSC; RGD:61841; rat. DR AGR; RGD:61841; -. DR CTD; 5682; -. DR RGD; 61841; Psma1. DR eggNOG; KOG0863; Eukaryota. DR HOGENOM; CLU_035750_8_0_1; -. DR InParanoid; P18420; -. DR OMA; NTQVYGK; -. DR OrthoDB; 431557at2759; -. DR PhylomeDB; P18420; -. DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-RNO-1236974; ER-Phagosome pathway. DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-RNO-174113; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-2467813; Separation of Sister Chromatids. DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation. DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-RNO-382556; ABC-family protein mediated transport. DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-RNO-4641257; Degradation of AXIN. DR Reactome; R-RNO-4641258; Degradation of DVL. DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis. DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-RNO-5632684; Hedgehog 'on' state. DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs. DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-RNO-5689603; UCH proteinases. DR Reactome; R-RNO-5689880; Ub-specific processing proteases. DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex. DR Reactome; R-RNO-68949; Orc1 removal from chromatin. DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-RNO-69481; G2/M Checkpoints. DR Reactome; R-RNO-69601; Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity. DR Reactome; R-RNO-8951664; Neddylation. DR Reactome; R-RNO-9020702; Interleukin-1 signaling. DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-RNO-9766229; Degradation of CDH1. DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR Reactome; R-RNO-9907900; Proteasome assembly. DR Reactome; R-RNO-9912633; Antigen processing: Ub, ATP-independent proteasomal degradation. DR Reactome; R-RNO-9929356; GSK3B-mediated proteasomal degradation of PD-L1(CD274). DR Reactome; R-RNO-9929491; SPOP-mediated proteasomal degradation of PD-L1(CD274). DR Reactome; R-RNO-9931269; AMPK-induced ERAD and lysosome mediated degradation of PD-L1(CD274). DR Reactome; R-RNO-9932298; Degradation of CRY and PER proteins. DR Reactome; R-RNO-9954709; Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide. DR PRO; PR:P18420; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000011745; Expressed in ovary and 20 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA. DR GO; GO:0016604; C:nuclear body; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000502; C:proteasome complex; ISO:RGD. DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB. DR GO; GO:0008021; C:synaptic vesicle; NAS:ComplexPortal. DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:RGD. DR GO; GO:0140756; F:structural constituent of proteasome; ISO:RGD. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD. DR GO; GO:0010498; P:proteasomal protein catabolic process; ISO:RGD. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD. DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; ISO:RGD. DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD. DR CDD; cd03749; proteasome_alpha_type_1; 1. DR FunFam; 3.60.20.10:FF:000025; Proteasome subunit alpha type; 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; 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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Glycoprotein; Immunity; Isopeptide bond; Nucleus; Phosphoprotein; KW Proteasome; Reference proteome; Ubl conjugation. FT CHAIN 1..263 FT /note="Proteasome subunit alpha type-1" FT /id="PRO_0000124064" FT REGION 232..263 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 253..263 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|PubMed:2335242" FT MOD_RES 110 FT /note="Phosphoserine; alternate" FT /evidence="ECO:0000250|UniProtKB:P25786" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25786" FT CARBOHYD 110 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P25786" FT CROSSLNK 208 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P25786" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 20..29 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 78..99 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 105..117 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 118..121 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 130..136 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 156..159 FT /evidence="ECO:0007829|PDB:6TU3" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 166..175 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:6TU3" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 184..197 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 207..216 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:6TU3" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:6TU3" FT HELIX 230..232 FT /evidence="ECO:0007829|PDB:6TU3" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:6TU3" SQ SEQUENCE 263 AA; 29518 MW; 68660696B43A4051 CRC64; MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHVFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM QCNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP QRKAQPSQAA DEPAEKADEP MEH //