ID PSA2_BOVIN Reviewed; 234 AA. AC Q3T0Y5; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 141. DE RecName: Full=Proteasome subunit alpha type-2; GN Name=PSMA2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME. RX PubMed=12015144; DOI=10.1016/s0969-2126(02)00748-7; RA Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., RA Tsukihara T.; RT "The structure of the mammalian 20S proteasome at 2.75 A resolution."; RL Structure 10:609-618(2002). 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:P25787}. 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 {ECO:0000269|PubMed:12015144}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25787}. Nucleus CC {ECO:0000250|UniProtKB:P25787}. Note=Translocated from the cytoplasm CC into the nucleus following interaction with AKIRIN2, which bridges the CC proteasome with the nuclear import receptor IPO9 (By similarity). CC Colocalizes with TRIM5 in cytoplasmic bodies (By similarity). CC {ECO:0000250|UniProtKB:P25787, ECO:0000250|UniProtKB:P49722}. CC -!- PTM: Phosphorylated on tyrosine residues; which may be important for CC nuclear import. {ECO:0000250|UniProtKB:P17220}. 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; BC102206; AAI02207.1; -; mRNA. DR RefSeq; NP_001029834.1; NM_001034662.2. DR PDB; 1IRU; X-ray; 2.75 A; B/P=2-234. DR PDB; 7DR6; EM; 4.10 A; M/f=1-234. DR PDB; 7DR7; EM; 3.30 A; F/M=1-234. DR PDB; 7DRW; EM; 4.20 A; B/h=1-234. DR PDB; 8FZ5; EM; 2.23 A; B/P=1-234. DR PDB; 8FZ6; EM; 2.54 A; B/P=1-234. DR PDBsum; 1IRU; -. DR PDBsum; 7DR6; -. DR PDBsum; 7DR7; -. DR PDBsum; 7DRW; -. DR PDBsum; 8FZ5; -. DR PDBsum; 8FZ6; -. DR AlphaFoldDB; Q3T0Y5; -. DR EMDB; EMD-29603; -. DR EMDB; EMD-29604; -. DR EMDB; EMD-30824; -. DR EMDB; EMD-30825; -. DR EMDB; EMD-30828; -. DR SMR; Q3T0Y5; -. DR BioGRID; 195708; 3. DR STRING; 9913.ENSBTAP00000001309; -. DR MEROPS; T01.972; -. DR PaxDb; 9913-ENSBTAP00000001309; -. DR PeptideAtlas; Q3T0Y5; -. DR Ensembl; ENSBTAT00000001309.6; ENSBTAP00000001309.5; ENSBTAG00000000990.6. DR GeneID; 539141; -. DR KEGG; bta:539141; -. DR CTD; 5683; -. DR VEuPathDB; HostDB:ENSBTAG00000000990; -. DR VGNC; VGNC:55751; PSMA2. DR eggNOG; KOG0181; Eukaryota. DR GeneTree; ENSGT00550000074870; -. DR HOGENOM; CLU_035750_4_1_1; -. DR InParanoid; Q3T0Y5; -. DR OMA; YQEQIPT; -. DR OrthoDB; 166567at2759; -. DR TreeFam; TF106207; -. DR Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-BTA-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-BTA-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-BTA-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-2467813; Separation of Sister Chromatids. DR Reactome; R-BTA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-BTA-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-BTA-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-BTA-382556; ABC-family proteins mediated transport. DR Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-BTA-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-BTA-4641257; Degradation of AXIN. DR Reactome; R-BTA-4641258; Degradation of DVL. DR Reactome; R-BTA-5358346; Hedgehog ligand biogenesis. DR Reactome; R-BTA-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-BTA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-BTA-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-BTA-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-BTA-5632684; Hedgehog 'on' state. DR Reactome; R-BTA-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-BTA-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-BTA-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-BTA-5689603; UCH proteinases. DR Reactome; R-BTA-5689880; Ub-specific processing proteases. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-68867; Assembly of the pre-replicative complex. DR Reactome; R-BTA-68949; Orc1 removal from chromatin. DR Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-BTA-69481; G2/M Checkpoints. DR Reactome; R-BTA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-BTA-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-BTA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-BTA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-BTA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-BTA-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-BTA-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-BTA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-BTA-8951664; Neddylation. DR Reactome; R-BTA-9020702; Interleukin-1 signaling. DR Reactome; R-BTA-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-BTA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR EvolutionaryTrace; Q3T0Y5; -. DR Proteomes; UP000009136; Chromosome 4. DR Bgee; ENSBTAG00000000990; Expressed in tongue muscle and 104 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:P-body; ISS:UniProtKB. 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd03750; proteasome_alpha_type_2; 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:SF16; PROTEASOME SUBUNIT ALPHA TYPE-2; 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 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Proteasome; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P25787" FT CHAIN 2..234 FT /note="Proteasome subunit alpha type-2" FT /id="PRO_0000239865" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 6 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P49722" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 24 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 70 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 76 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT MOD_RES 121 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P17220" FT MOD_RES 171 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25787" FT STRAND 8..10 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 20..30 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 44..49 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 55..57 FT /evidence="ECO:0007829|PDB:1IRU" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:7DR7" FT STRAND 64..78 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 80..101 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 107..120 FT /evidence="ECO:0007829|PDB:1IRU" FT TURN 121..123 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 131..139 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 141..149 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 155..164 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 167..177 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 184..196 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 205..214 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 217..220 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 223..230 FT /evidence="ECO:0007829|PDB:1IRU" SQ SEQUENCE 234 AA; 25899 MW; 63CB56A233583836 CRC64; MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVKDYL AAIA //