ID PSA4_MOUSE Reviewed; 261 AA. AC Q9R1P0; Q3THT1; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 189. DE RecName: Full=Proteasome subunit alpha type-4; DE AltName: Full=Macropain subunit C9; DE AltName: Full=Multicatalytic endopeptidase complex subunit C9; DE AltName: Full=Proteasome component C9; DE AltName: Full=Proteasome subunit L; GN Name=Psma4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=B10.BR; RX PubMed=10436176; DOI=10.1007/s002510050562; RA Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., RA Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.; RT "The complete primary structure of mouse 20S proteasomes."; RL Immunogenetics 49:835-842(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Heart; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [4] RP PROTEIN SEQUENCE OF 55-64. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX. RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7; RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.; RT "Mapping the murine cardiac 26S proteasome complexes."; RL Circ. Res. 99:362-371(2006). RN [6] RP FUNCTION. RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006; RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R., RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A., RA Sleckman B.P.; RT "Proteasome activator PA200 is required for normal spermatogenesis."; RL Mol. Cell. Biol. 26:2999-3007(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=22078707; DOI=10.1186/1742-4690-8-93; RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., RA Luban J., Campbell E.M.; RT "TRIM5alpha associates with proteasomal subunits in cells while in complex RT with HIV-1 virions."; RL Retrovirology 8:93-93(2011). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030; RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., RA Groll M.; RT "Immuno- and constitutive proteasome crystal structures reveal differences RT in substrate and inhibitor specificity."; RL Cell 148:727-738(2012). 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:0000269|PubMed:16581775, CC ECO:0000269|PubMed:22341445}. 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 (PubMed:16857966, PubMed:22341445). {ECO:0000269|PubMed:16857966, CC ECO:0000269|PubMed:22341445}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus CC {ECO:0000269|PubMed:22078707}. 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 the cytoplasmic bodies (PubMed:22078707). CC {ECO:0000250|UniProtKB:P25789, ECO:0000269|PubMed:22078707}. CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). CC {ECO:0000269|PubMed:22341445}. 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; AF060093; AAD50538.1; -; mRNA. DR EMBL; AK085937; BAC39573.1; -; mRNA. DR EMBL; AK168150; BAE40115.1; -; mRNA. DR EMBL; BC001982; AAH01982.1; -; mRNA. DR CCDS; CCDS40643.1; -. DR RefSeq; NP_036096.1; NM_011966.3. DR RefSeq; XP_006511261.1; XM_006511198.3. DR PDB; 3UNB; X-ray; 2.90 A; B/P/d/r=1-261. DR PDB; 3UNE; X-ray; 3.20 A; B/P/d/r=1-261. DR PDB; 3UNF; X-ray; 2.90 A; B/P=1-261. DR PDB; 3UNH; X-ray; 3.20 A; B/P=1-261. DR PDBsum; 3UNB; -. DR PDBsum; 3UNE; -. DR PDBsum; 3UNF; -. DR PDBsum; 3UNH; -. DR AlphaFoldDB; Q9R1P0; -. DR SMR; Q9R1P0; -. DR BioGRID; 204992; 62. DR CORUM; Q9R1P0; -. DR IntAct; Q9R1P0; 8. DR MINT; Q9R1P0; -. DR STRING; 10090.ENSMUSP00000034848; -. DR MEROPS; T01.973; -. DR iPTMnet; Q9R1P0; -. DR PhosphoSitePlus; Q9R1P0; -. DR SwissPalm; Q9R1P0; -. DR CPTAC; non-CPTAC-3424; -. DR EPD; Q9R1P0; -. DR jPOST; Q9R1P0; -. DR MaxQB; Q9R1P0; -. DR PaxDb; 10090-ENSMUSP00000034848; -. DR PeptideAtlas; Q9R1P0; -. DR ProteomicsDB; 291606; -. DR Pumba; Q9R1P0; -. DR Antibodypedia; 27657; 385 antibodies from 36 providers. DR DNASU; 26441; -. DR Ensembl; ENSMUST00000034848.14; ENSMUSP00000034848.8; ENSMUSG00000032301.14. DR GeneID; 26441; -. DR KEGG; mmu:26441; -. DR UCSC; uc009pru.1; mouse. DR AGR; MGI:1347060; -. DR CTD; 5685; -. DR MGI; MGI:1347060; Psma4. DR VEuPathDB; HostDB:ENSMUSG00000032301; -. DR eggNOG; KOG0178; Eukaryota. DR GeneTree; ENSGT00550000074827; -. DR InParanoid; Q9R1P0; -. DR OMA; YVLNDNM; -. DR OrthoDB; 166567at2759; -. DR PhylomeDB; Q9R1P0; -. DR TreeFam; TF106209; -. DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells. DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-2467813; Separation of Sister Chromatids. DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation. DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC). DR Reactome; R-MMU-382556; ABC-family proteins mediated transport. DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA. DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins. DR Reactome; R-MMU-4641257; Degradation of AXIN. DR Reactome; R-MMU-4641258; Degradation of DVL. DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis. DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome. DR Reactome; R-MMU-5632684; Hedgehog 'on' state. DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs. DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway. DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling. DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-MMU-5689603; UCH proteinases. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex. DR Reactome; R-MMU-68949; Orc1 removal from chromatin. DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-MMU-69481; G2/M Checkpoints. DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D. DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint. DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis. DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs. DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity. DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity. DR Reactome; R-MMU-8951664; Neddylation. DR Reactome; R-MMU-9020702; Interleukin-1 signaling. DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway. DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR BioGRID-ORCS; 26441; 28 hits in 72 CRISPR screens. DR ChiTaRS; Psma4; mouse. DR PRO; PR:Q9R1P0; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q9R1P0; Protein. DR Bgee; ENSMUSG00000032301; Expressed in maxillary prominence and 248 other cell types or tissues. DR ExpressionAtlas; Q9R1P0; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0000932; C:P-body; IDA:UniProtKB. DR GO; GO:0000502; C:proteasome complex; ISO:MGI. DR GO; GO:0005839; C:proteasome core complex; IDA: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; cd03752; proteasome_alpha_type_4; 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; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR PANTHER; PTHR11599:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 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 Genevisible; Q9R1P0; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus; KW Phosphoprotein; Proteasome; Reference proteome. FT CHAIN 1..261 FT /note="Proteasome subunit alpha type-4" FT /id="PRO_0000124105" FT REGION 240..261 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25789" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25789" FT MOD_RES 127 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25789" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P25789" FT MOD_RES 176 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P25789" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:3UNF" FT HELIX 19..28 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 34..38 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 40..48 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 63..67 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 69..78 FT /evidence="ECO:0007829|PDB:3UNB" FT HELIX 80..101 FT /evidence="ECO:0007829|PDB:3UNB" FT HELIX 107..123 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 132..140 FT /evidence="ECO:0007829|PDB:3UNB" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 144..150 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 156..165 FT /evidence="ECO:0007829|PDB:3UNB" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:3UNB" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:3UNB" FT HELIX 186..200 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:3UNF" FT HELIX 208..210 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 211..219 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:3UNB" FT HELIX 230..244 FT /evidence="ECO:0007829|PDB:3UNB" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:3UNH" SQ SEQUENCE 261 AA; 29471 MW; BB7CC8113791E13B CRC64; MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAVKVLNKT MDVSKLSAEK VEIATLTRES GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE KKEKEQREKD K //