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 22-JUL-2015, entry version 132. DE RecName: Full=Proteasome subunit alpha type-4; DE EC=3.4.25.1; 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; Sciurognathi; 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/2; 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 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 [7] 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: The proteasome is a multicatalytic proteinase complex CC which is characterized by its ability to cleave peptides with Arg, CC Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or CC slightly basic pH. The proteasome has an ATP-dependent proteolytic CC activity. {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 composed CC of 28 subunits that are arranged in four stacked rings, resulting CC in a barrel-shaped structure. The two end rings are each formed by CC seven alpha subunits, and the two central rings are each formed by CC seven beta subunits. The catalytic chamber with the active sites CC is on the inside of the barrel. {ECO:0000269|PubMed:16857966, CC ECO:0000269|PubMed:22341445}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. CC Nucleus {ECO:0000269|PubMed:22078707}. Cytoplasm, P-body CC {ECO:0000269|PubMed:22078707}. Note=Colocalizes with TRIM5 in the CC cytoplasmic bodies. 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_006511198.2. DR UniGene; Mm.30270; -. 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; 2-237. DR BioGrid; 204992; 3. DR IntAct; Q9R1P0; 6. DR MINT; MINT-1850528; -. DR STRING; 10090.ENSMUSP00000034848; -. DR MEROPS; T01.973; -. DR PhosphoSite; Q9R1P0; -. DR MaxQB; Q9R1P0; -. DR PaxDb; 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; COG0638; -. DR GeneTree; ENSGT00550000074827; -. DR HOGENOM; HOG000091085; -. DR HOVERGEN; HBG003005; -. DR InParanoid; Q9R1P0; -. DR KO; K02728; -. DR OMA; LVSHLCD; -. DR OrthoDB; EOG7F512J; -. DR PhylomeDB; Q9R1P0; -. DR TreeFam; TF106209; -. DR Reactome; REACT_274287; Degradation of beta-catenin by the destruction complex. DR Reactome; REACT_275686; Activation of NF-kappaB in B cells. DR Reactome; REACT_275732; degradation of AXIN. DR Reactome; REACT_278878; AUF1 (hnRNP D0) destabilizes mRNA. DR Reactome; REACT_289441; Regulation of activated PAK-2p34 by proteasome mediated degradation. DR Reactome; REACT_294625; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; REACT_297888; degradation of DVL. DR Reactome; REACT_299120; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; REACT_301078; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1. DR Reactome; REACT_308964; ER-Phagosome pathway. DR Reactome; REACT_310780; Degradation of GLI2 by the proteasome. DR Reactome; REACT_315933; Orc1 removal from chromatin. DR Reactome; REACT_321346; Separation of Sister Chromatids. DR Reactome; REACT_326233; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A. DR Reactome; REACT_329431; APC/C:Cdc20 mediated degradation of Securin. DR Reactome; REACT_334737; Regulation of ornithine decarboxylase (ODC). DR Reactome; REACT_336463; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; REACT_336745; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; REACT_337766; Autodegradation of Cdh1 by Cdh1:APC/C. DR Reactome; REACT_341044; SCF-beta-TrCP mediated degradation of Emi1. DR Reactome; REACT_341075; ER-Phagosome pathway. DR Reactome; REACT_342086; SCF(Skp2)-mediated degradation of p27/p21. DR Reactome; REACT_342636; Asymmetric localization of PCP proteins. DR Reactome; REACT_343561; CDT1 association with the CDC6:ORC:origin complex. DR Reactome; REACT_343568; Antigen processing: Ubiquitination & Proteasome degradation. DR Reactome; REACT_345193; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; REACT_347264; Hedgehog ligand biogenesis. DR Reactome; REACT_351311; Hedgehog 'on' state. DR Reactome; REACT_353777; GLI3 is processed to GLI3R by the proteasome. DR Reactome; REACT_359269; Dectin-1 mediated noncanonical NF-kB signaling. DR Reactome; REACT_359387; Degradation of GLI1 by the proteasome. DR Reactome; REACT_360804; CLEC7A (Dectin-1) signaling. DR ChiTaRS; Psma4; mouse. DR NextBio; 304521; -. DR PRO; PR:Q9R1P0; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; Q9R1P0; -. DR ExpressionAtlas; Q9R1P0; baseline and differential. DR Genevisible; Q9R1P0; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. 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; IEA:InterPro. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR023332; Proteasome_suA-type. DR InterPro; IPR001353; Proteasome_sua/b. 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 //