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 03-MAY-2023, entry version 140. DE RecName: Full=Proteasome subunit alpha type-2-B; 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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; 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., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., 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., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis 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 reference RT 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., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA 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; DOI=10.1093/genetics/149.2.677; RA Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.; RT "Molecular organization of the 20S proteasome gene family from Arabidopsis RT 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., Vierstra R.D.; RT "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular RT 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 PROTEASOME RP 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., Vierstra R.D.; RT "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse RT array of plant proteolytic complexes."; RL J. Biol. Chem. 285:25554-25569(2010). CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr, CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic CC pH. The proteasome has an ATP-dependent proteolytic activity. CC -!- SUBUNIT: Component of the 20S core complex of the 26S proteasome. The CC 26S proteasome is composed of a core protease (CP), known as the 20S CC proteasome, capped at one or both ends by the 19S regulatory particle CC (RP/PA700). The 20S proteasome core is composed of 28 subunits that are CC arranged in four stacked rings, resulting in a barrel-shaped structure. CC The two end rings are each formed by seven alpha subunits, and the two CC central rings are each formed by seven beta subunits. The catalytic CC chamber with the 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 {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE- CC 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 AlphaFoldDB; Q8L4A7; -. DR SMR; Q8L4A7; -. DR BioGRID; 29481; 72. DR STRING; 3702.AT1G79210.2; -. DR MEROPS; T01.972; -. DR iPTMnet; Q8L4A7; -. DR PaxDb; Q8L4A7; -. DR ProteomicsDB; 226485; -. 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 HOGENOM; CLU_035750_4_1_1; -. DR OMA; WKACANG; -. DR OrthoDB; 166567at2759; -. DR PhylomeDB; Q8L4A7; -. DR PRO; PR:Q8L4A7; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q8L4A7; baseline and differential. DR Genevisible; Q8L4A7; AT. DR GO; GO:0005829; C:cytosol; HDA:TAIR. DR GO; GO:0005739; C:mitochondrion; HDA:TAIR. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000502; C:proteasome complex; IDA:TAIR. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR CDD; cd03750; proteasome_alpha_type_2; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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 PANTHER; PTHR11599:SF16; PROTEASOME SUBUNIT ALPHA TYPE-2; 1. DR PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. PE 1: Evidence at protein level; KW Cytoplasm; Isopeptide bond; Nucleus; Proteasome; Reference proteome; KW Ubl conjugation. FT CHAIN 1..235 FT /note="Proteasome subunit alpha type-2-B" FT /id="PRO_0000124086" FT CROSSLNK 64 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="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 //