ID Q8L4A7 PRELIMINARY; PRT; 235 AA. AC Q8L4A7; DT 01-OCT-2002 (TrEMBLrel. 22, Created) DT 01-OCT-2002 (TrEMBLrel. 22, Last sequence update) DT 25-JAN-2005 (TrEMBLrel. 29, Last annotation update) DE At1g79210/YUP8H12R_1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RA Shinn P., Chen H., Cheuk R., Kim C.J., Meyers M.C., Banh J., RA Bowser L., Carninci P., Chang E., Dale J.M., Goldsmith A.D., RA Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., RA Kawai J., Lam B., Lee J.M., Lin J., Miranda M., Narusaka M., RA Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., RA Seki M., Southwick A., Tang C.C., Toriumi M., Wu H.C., Yamada K., RA Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RA Shinn P., Chen H., Cheuk R., Kim C.J., Banh J., Bowser L., RA Carninci P., Chang E., Dale J.M., Goldsmith A.D., Hayashizaki Y., RA Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B., RA Lee J.M., Lin J., Miranda M., Narusaka M., Nguyen M., Onodera C.S., RA Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., RA Tang C.C., Toriumi M., Wu H.C., Yamada K., Yamamura Y., Yu G., Yu S., RA Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). 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 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic and nuclear (By similarity). 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; AY094433; AAM19806.1; -. DR EMBL; AY122893; AAM67426.1; -. DR HSSP; P23639; 1G0U. DR GO; GO:0005829; C:cytosol; IEA. DR GO; GO:0005839; C:proteasome core complex (sensu Eukaryota); IEA. DR GO; GO:0004175; F:endopeptidase activity; IEA. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolism; IEA. DR InterPro; IPR000169; Pept_cys_acsite. DR InterPro; IPR000426; Proteasome_alpha. DR InterPro; IPR001353; Proteasome_A_B. DR Pfam; PF00227; Proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. DR PROSITE; PS00639; THIOL_PROTEASE_HIS; UNKNOWN_1. KW Hydrolase; Protease; Proteasome; Threonine protease. SQ SEQUENCE 235 AA; 25733 MW; 9B2DA84B57FC8B95 CRC64; MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA SNGVVIATEK KLPSILVDEA SVQKIQHLTP NIGTVYSGMG PDFRVLVRKS RKQAEQYLRL YKEPIPVTQL VRETATVMQE FTQSGGVRPF GVSLLVAGYD DKGPQLYQVD PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE DMELDDAIHT AILTLKEGFE GEISSKNIEI GKIGTDKVFR VLTPAEIDDY LAEVE //