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 28-JUL-2009, entry version 48. DE RecName: Full=Proteasome subunit alpha type-2-B; DE EC=3.4.25.1; DE AltName: Full=20S proteasome alpha 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 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 (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 IPI; IPI00516979; -. DR PIR; T01036; T01036. DR RefSeq; NP_001077845.1; -. DR RefSeq; NP_001077846.1; -. DR RefSeq; NP_178042.1; -. DR UniGene; At.10591; -. DR HSSP; P23639; 1RYP. DR MEROPS; T01.972; -. DR PRIDE; Q8L4A7; -. DR GeneID; 844262; -. DR GenomeReviews; CT485782_GR; AT1G79210. DR KEGG; ath:AT1G79210; -. DR NMPDR; fig|3702.1.peg.7485; -. DR TAIR; At1g79210; -. DR OMA; Q8L4A7; HIALLTL. DR BRENDA; 3.4.25.1; 302. DR GermOnline; AT1G79210; Arabidopsis thaliana. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005839; C:proteasome core complex; IEA:InterPro. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEP:TAIR. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR InterPro; IPR000426; Proteasome_asu_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. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Hydrolase; Nucleus; Protease; KW 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 //