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 11-JUN-2014, entry version 120. 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. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. 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. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body. CC Note=Colocalizes with TRIM5 in the cytoplasmic bodies. CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). CC -!- SIMILARITY: Belongs to the peptidase T1A family. 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 RefSeq; NP_036096.1; NM_011966.3. DR RefSeq; XP_006511261.1; XM_006511198.1. 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; 2. DR IntAct; Q9R1P0; 6. DR MINT; MINT-1850528; -. 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; KQEYKDD; -. DR OrthoDB; EOG7F512J; -. DR PhylomeDB; Q9R1P0; -. DR TreeFam; TF106209; -. DR ChiTaRS; PSMA4; mouse. DR NextBio; 304521; -. DR PRO; PR:Q9R1P0; -. DR ArrayExpress; Q9R1P0; -. DR Bgee; Q9R1P0; -. DR Genevestigator; Q9R1P0; -. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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: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; 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 (By similarity). FT MOD_RES 75 75 Phosphoserine (By similarity). FT MOD_RES 127 127 N6-acetyllysine (By similarity). FT MOD_RES 176 176 N6-acetyllysine (By similarity). FT TURN 3 5 FT HELIX 19 28 FT STRAND 34 38 FT STRAND 40 48 FT STRAND 63 67 FT STRAND 69 78 FT HELIX 80 101 FT HELIX 107 123 FT STRAND 124 126 FT STRAND 132 140 FT TURN 141 143 FT STRAND 144 150 FT STRAND 156 165 FT HELIX 168 178 FT TURN 181 183 FT HELIX 186 200 FT STRAND 202 205 FT HELIX 208 210 FT STRAND 211 219 FT STRAND 222 227 FT HELIX 230 244 FT STRAND 245 247 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 //