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 10-AUG-2010, entry version 85. DE RecName: Full=Proteasome subunit alpha type-4; DE EC=3.4.25.1; DE AltName: Full=Proteasome component C9; DE AltName: Full=Macropain subunit C9; DE AltName: Full=Multicatalytic endopeptidase complex subunit 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. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=B10.BR; RX MEDLINE=99367391; 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. 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. 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 IPI; IPI00277001; -. DR RefSeq; NP_036096.1; -. DR UniGene; Mm.30270; -. DR ProteinModelPortal; Q9R1P0; -. DR SMR; Q9R1P0; 2-237. DR STRING; Q9R1P0; -. DR MEROPS; T01.973; -. DR PhosphoSite; Q9R1P0; -. DR PRIDE; Q9R1P0; -. DR Ensembl; ENSMUST00000034848; ENSMUSP00000034848; ENSMUSG00000032301; Mus musculus. DR GeneID; 26441; -. DR KEGG; mmu:26441; -. DR NMPDR; fig|10090.3.peg.20227; -. DR UCSC; uc009pru.1; mouse. DR CTD; 26441; -. DR MGI; MGI:1347060; Psma4. DR eggNOG; roNOG06617; -. DR HOGENOM; HBG499923; -. DR HOVERGEN; HBG003005; -. DR InParanoid; Q9R1P0; -. DR OMA; MARRYDS; -. DR OrthoDB; EOG9J402D; -. DR PhylomeDB; Q9R1P0; -. DR BRENDA; 3.4.25.1; 244. DR NextBio; 304521; -. DR ArrayExpress; Q9R1P0; -. DR Bgee; Q9R1P0; -. DR Genevestigator; Q9R1P0; -. DR GermOnline; ENSMUSG00000032301; Mus musculus. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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 InterPro; IPR000426; Proteasome_asu_CS. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR PROSITE; PS00388; PROTEASOME_A_1; 1. DR PROSITE; PS51475; PROTEASOME_A_2; 1. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; KW Phosphoprotein; Protease; Proteasome; 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 MOD_RES 238 238 N6-acetyllysine (By similarity). 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 //