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 16-JAN-2019, entry version 120. 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; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX 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 GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana RT reference genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX 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 [4] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=9611183; RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.; RT "Molecular organization of the 20S proteasome gene family from RT Arabidopsis thaliana."; RL Genetics 149:677-692(1998). RN [5] RP SUBUNIT. RX PubMed=10363660; DOI=10.1023/A:1006926322501; RA Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., RA Finley D., Vierstra R.D.; RT "Structure and functional analyses of the 26S proteasome subunits from RT plants."; RL Mol. Biol. Rep. 26:137-146(1999). RN [6] 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). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S RP PROTEASOME COMPLEX, AND SUBUNIT. RX PubMed=20516081; DOI=10.1074/jbc.M110.136622; RA Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., RA Vierstra R.D.; RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a RT diverse array of plant proteolytic complexes."; RL J. Biol. Chem. 285:25554-25569(2010). 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: CC Reaction=Cleavage of peptide bonds with very broad specificity.; CC EC=3.4.25.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00808}; CC -!- SUBUNIT: Component of the 20S core complex of the 26S proteasome. CC The 26S proteasome is composed of a core protease (CP), known as CC the 20S proteasome, capped at one or both ends by the 19S CC regulatory particle (RP/PA700). The 20S proteasome core is CC composed of 28 subunits that are arranged in four stacked rings, CC resulting in a barrel-shaped structure. The two end rings are each CC formed by seven alpha subunits, and the two central rings are each CC formed by seven beta subunits. The catalytic chamber with the CC active sites is on the inside of the barrel. CC {ECO:0000269|PubMed:10363660, ECO:0000269|PubMed:14623884, CC ECO:0000269|PubMed:20516081}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1A family. CC {ECO:0000255|PROSITE-ProRule:PRU00808}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC17043.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; CP002684; AEE36215.1; -; Genomic_DNA. DR EMBL; CP002684; AEE36216.1; -; Genomic_DNA. DR EMBL; CP002684; AEE36217.1; -; Genomic_DNA. DR EMBL; AY094433; AAM19806.1; -; mRNA. DR EMBL; AY122893; AAM67426.1; -; mRNA. DR PIR; T01036; T01036. DR RefSeq; NP_001077845.1; NM_001084376.1. DR RefSeq; NP_001077846.1; NM_001084377.1. DR RefSeq; NP_178042.1; NM_106572.6. DR UniGene; At.10591; -. DR ProteinModelPortal; Q8L4A7; -. DR SMR; Q8L4A7; -. DR BioGrid; 29481; 2. DR STRING; 3702.AT1G79210.1; -. DR MEROPS; T01.972; -. DR iPTMnet; Q8L4A7; -. DR PaxDb; Q8L4A7; -. DR PRIDE; Q8L4A7; -. DR EnsemblPlants; AT1G79210.1; AT1G79210.1; AT1G79210. DR EnsemblPlants; AT1G79210.2; AT1G79210.2; AT1G79210. DR EnsemblPlants; AT1G79210.3; AT1G79210.3; AT1G79210. DR GeneID; 844262; -. DR Gramene; AT1G79210.1; AT1G79210.1; AT1G79210. DR Gramene; AT1G79210.2; AT1G79210.2; AT1G79210. DR Gramene; AT1G79210.3; AT1G79210.3; AT1G79210. DR KEGG; ath:AT1G79210; -. DR Araport; AT1G79210; -. DR TAIR; locus:2207340; AT1G79210. DR eggNOG; KOG0181; Eukaryota. DR eggNOG; ENOG410XPQ8; LUCA. DR HOGENOM; HOG000091085; -. DR KO; K02726; -. DR OMA; DEINTYA; -. DR OrthoDB; 1222564at2759; -. DR PhylomeDB; Q8L4A7; -. DR Reactome; R-ATH-1236978; Cross-presentation of soluble exogenous antigens (endosomes). DR Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; R-ATH-349425; Autodegradation of the E3 ubiquitin ligase COP1. DR Reactome; R-ATH-5632684; Hedgehog 'on' state. DR Reactome; R-ATH-5687128; MAPK6/MAPK4 signaling. DR Reactome; R-ATH-5689603; UCH proteinases. DR Reactome; R-ATH-5689880; Ub-specific processing proteases. DR Reactome; R-ATH-6798695; Neutrophil degranulation. DR Reactome; R-ATH-68949; Orc1 removal from chromatin. DR Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6. DR Reactome; R-ATH-69229; Ubiquitin-dependent degradation of Cyclin D1. DR Reactome; R-ATH-8951664; Neddylation. DR Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR PRO; PR:Q8L4A7; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q8L4A7; baseline and differential. DR Genevisible; Q8L4A7; AT. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000502; C:proteasome complex; IDA:TAIR. DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central. DR GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR023332; Proteasome_alpha-type. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR034644; Proteasome_subunit_alpha2. DR PANTHER; PTHR11599:SF16; PTHR11599:SF16; 1. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Hydrolase; Isopeptide bond; Nucleus; KW Protease; Proteasome; Reference proteome; Threonine protease; KW Ubl conjugation. FT CHAIN 1 235 Proteasome subunit alpha type-2-B. FT /FTId=PRO_0000124086. FT CROSSLNK 64 64 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:O81149}. 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 //