ID PSA4_MOUSE STANDARD; PRT; 261 AA. AC Q9R1P0; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Proteasome subunit alpha type 4 (EC 3.4.25.1) (Proteasome component DE C9) (Macropain subunit C9) (Multicatalytic endopeptidase complex DE subunit C9) (Proteasome subunit L). GN Name=Psma4; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Heart; RX MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266; RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T., RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., RA Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., RA Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., RA Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., RA Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., RA Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., RA Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., RA Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., RA Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., RA Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., RA Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., RA Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., RA Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., RA Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., RA Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., RA Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., RA Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., RA Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., RA Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., RA Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., RA Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., RA Birney E., Hayashizaki Y.; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). 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 -!- PATHWAY: Involved in an ATP/ubiquitin-dependent non-lysosomal CC proteolytic pathway. CC -!- SUBUNIT: The proteasome is composed of at least 15 non identical CC subunits which form a highly ordered ring-shaped structure. CC -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear. CC -!- SIMILARITY: Belongs to peptidase family T1A. 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; -. DR EMBL; AK085937; BAC39573.1; -. DR EMBL; BC001982; AAH01982.1; -. DR HSSP; P23638; 1RYP. DR MEROPS; T01.973; -. DR MGD; MGI:1347060; Psma4. DR InterPro; IPR000426; Proteasome_alpha. DR InterPro; IPR001353; Proteasome_A_B. DR Pfam; PF00227; Proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Hydrolase; Protease; Proteasome; Threonine protease. 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 //