ID PSA2B_ARATH Reviewed; 235 AA. AC Q8L4A7; O64532; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 12-JUN-2007, entry version 29. DE Proteasome subunit alpha type 2-B (EC 3.4.25.1) (20S proteasome alpha DE subunit B-2). GN Name=PAB2; OrderedLocusNames=At1g79210; ORFNames=YUP8H12R.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [3] RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14623884; DOI=10.1074/jbc.M311977200; RA Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., RA Vierstra R.D.; RT "Purification of the Arabidopsis 26 S proteasome: biochemical and RT molecular analyses revealed the presence of multiple isoforms."; RL J. Biol. Chem. 279:6401-6413(2004). 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 proteasome is composed of at least 15 non identical CC subunits which form a highly ordered ring-shaped structure. The CC 26S proteasome consisting of a 20S core protease (CP) complex CC capped at one or both ends by a 19S regulatory particle (RP). The CC CP has a cylindrical shape composed by 4 heptameric rings made of CC alpha and beta subunits. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- SIMILARITY: Belongs to the peptidase T1A family. CC -!- SEQUENCE CAUTION: CC Sequence=AAC17043.1; Type=Erroneous gene model prediction; 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; AC002986; AAC17043.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY094433; AAM19806.1; -; mRNA. DR EMBL; AY122893; AAM67426.1; -; mRNA. DR PIR; T01036; T01036. DR UniGene; At.10591; -. DR HSSP; P23639; 1RYP. DR MEROPS; T01.972; -. DR GenomeReviews; CT485782_GR; AT1G79210. DR KEGG; ath:At1g79210; -. DR TAIR; At1g79210; -. DR GermOnline; AT1G79210; Arabidopsis thaliana. DR InterPro; IPR001353; Proteasome_A_B. DR InterPro; IPR000426; Proteasome_alpha. DR Pfam; PF00227; Proteasome; 1. DR PROSITE; PS00388; PROTEASOME_A; 1. KW Hydrolase; Nuclear protein; Protease; Proteasome; Threonine protease. FT CHAIN 1 235 Proteasome subunit alpha type 2-B. FT /FTId=PRO_0000124086. 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 //