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 23-MAY-2018, entry version 157. DE RecName: Full=Proteasome subunit alpha type-4; DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P25789}; 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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., RA 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 RT 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 RT complex with HIV-1 virions."; RL Retrovirology 8:93-93(2011). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, RP SUBUNIT, 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., RA Groettrup M., Groll M.; RT "Immuno- and constitutive proteasome crystal structures reveal RT differences in substrate and inhibitor specificity."; RL Cell 148:727-738(2012). CC -!- FUNCTION: Component of the 20S core proteasome complex involved in CC the proteolytic degradation of most intracellular proteins. This CC complex plays numerous essential roles within the cell by CC associating with different regulatory particles. Associated with CC two 19S regulatory particles, forms the 26S proteasome and thus CC participates in the ATP-dependent degradation of ubiquitinated CC proteins. The 26S proteasome plays a key role in the maintenance CC of protein homeostasis by removing misfolded or damaged proteins CC that could impair cellular functions, and by removing proteins CC whose functions are no longer required. Associated with the PA200 CC or PA28, the 20S proteasome mediates ubiquitin-independent protein CC degradation. This type of proteolysis is required in several CC 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 -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000255|PROSITE-ProRule:PRU00808}. CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and CC two 19S regulatory subunits. The 20S proteasome core is a barrel- CC shaped complex made of 28 subunits that are arranged in four CC stacked rings. The two outer rings are each formed by seven alpha CC subunits, and the two inner rings are formed by seven beta CC subunits. The proteolytic activity is exerted by three beta- CC subunits PSMB5, PSMB6 and PSMB7 (PubMed:16857966, CC PubMed:22341445). {ECO:0000269|PubMed:16857966, CC ECO:0000269|PubMed:22341445}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. CC Nucleus {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 CC in the cytoplasmic bodies. {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. CC {ECO:0000255|PROSITE-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 UniGene; Mm.30270; -. DR UniGene; Mm.440582; -. 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 ProteinModelPortal; Q9R1P0; -. DR SMR; Q9R1P0; -. DR BioGrid; 204992; 4. DR CORUM; Q9R1P0; -. DR IntAct; Q9R1P0; 6. DR MINT; Q9R1P0; -. DR STRING; 10090.ENSMUSP00000034848; -. DR MEROPS; T01.973; -. DR iPTMnet; Q9R1P0; -. DR PhosphoSitePlus; Q9R1P0; -. DR SwissPalm; Q9R1P0; -. DR EPD; Q9R1P0; -. DR MaxQB; Q9R1P0; -. DR PaxDb; Q9R1P0; -. DR PeptideAtlas; Q9R1P0; -. DR PRIDE; Q9R1P0; -. DR Ensembl; ENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301. DR GeneID; 26441; -. DR KEGG; mmu:26441; -. DR UCSC; uc009pru.1; mouse. DR CTD; 5685; -. DR MGI; MGI:1347060; Psma4. DR eggNOG; KOG0178; Eukaryota. DR eggNOG; COG0638; LUCA. DR GeneTree; ENSGT00550000074827; -. DR HOGENOM; HOG000091085; -. DR HOVERGEN; HBG003005; -. DR InParanoid; Q9R1P0; -. DR KO; K02728; -. DR OMA; MSKTMDS; -. DR OrthoDB; EOG091G0F2L; -. 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-174113; SCF-beta-TrCP mediated degradation of Emi1. 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-68827; CDT1 association with the CDC6:ORC:origin 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-69229; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; R-MMU-69481; G2/M Checkpoints. DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. 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-9020702; Interleukin-1 signaling. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR ChiTaRS; Psma4; mouse. DR PRO; PR:Q9R1P0; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; ENSMUSG00000032301; -. DR ExpressionAtlas; Q9R1P0; baseline and differential. DR Genevisible; Q9R1P0; MM. 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; TAS:Reactome. 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:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 3.60.20.10; -; 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 InterPro; IPR034647; Proteasome_subunit_alpha4. DR PANTHER; PTHR11599:SF13; PTHR11599:SF13; 1. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; SSF56235; 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; Complete proteome; Cytoplasm; KW Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; KW Protease; Proteasome; Reference proteome; Threonine protease. FT CHAIN 1 261 Proteasome subunit alpha type-4. FT /FTId=PRO_0000124105. FT MOD_RES 13 13 Phosphoserine. FT {ECO:0000250|UniProtKB:P25789}. FT MOD_RES 75 75 Phosphoserine. FT {ECO:0000250|UniProtKB:P25789}. FT MOD_RES 127 127 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P25789}. FT MOD_RES 173 173 Phosphoserine. FT {ECO:0000250|UniProtKB:P25789}. FT MOD_RES 176 176 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P25789}. FT TURN 3 5 {ECO:0000244|PDB:3UNF}. FT HELIX 19 28 {ECO:0000244|PDB:3UNB}. FT STRAND 34 38 {ECO:0000244|PDB:3UNB}. FT STRAND 40 48 {ECO:0000244|PDB:3UNB}. FT STRAND 63 67 {ECO:0000244|PDB:3UNB}. FT STRAND 69 78 {ECO:0000244|PDB:3UNB}. FT HELIX 80 101 {ECO:0000244|PDB:3UNB}. FT HELIX 107 123 {ECO:0000244|PDB:3UNB}. FT STRAND 124 126 {ECO:0000244|PDB:3UNB}. FT STRAND 132 140 {ECO:0000244|PDB:3UNB}. FT TURN 141 143 {ECO:0000244|PDB:3UNB}. FT STRAND 144 150 {ECO:0000244|PDB:3UNB}. FT STRAND 156 165 {ECO:0000244|PDB:3UNB}. FT HELIX 168 178 {ECO:0000244|PDB:3UNB}. FT TURN 181 183 {ECO:0000244|PDB:3UNB}. FT HELIX 186 200 {ECO:0000244|PDB:3UNB}. FT STRAND 202 205 {ECO:0000244|PDB:3UNF}. FT HELIX 208 210 {ECO:0000244|PDB:3UNB}. FT STRAND 211 219 {ECO:0000244|PDB:3UNB}. FT STRAND 222 227 {ECO:0000244|PDB:3UNB}. FT HELIX 230 244 {ECO:0000244|PDB:3UNB}. FT STRAND 245 247 {ECO:0000244|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 //