ID PSA4A_ORYSI Reviewed; 250 AA. AC A2Y9X7; DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 22-FEB-2023, entry version 84. DE RecName: Full=Proteasome subunit alpha type-4-1; DE AltName: Full=20S proteasome alpha subunit C; DE AltName: Full=20S proteasome subunit alpha-3; GN ORFNames=OsI_021120; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39946; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=cv. CO43; TISSUE=Leaf; RA Saveetha K., Samiyappan R., Raveendran M., Balasubramanian P.; RT "Interactive genomics and proteomics of plant growth promoting RT rhizobacteria (PGPR) for the management of major pests and diseases in RT rice."; RL Submitted (NOV-2008) to UniProtKB. 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: The 26S proteasome consists of a 20S proteasome core and two CC 19S regulatory subunits. The 20S proteasome core is composed of 28 CC subunits that are arranged in four stacked rings, resulting in a CC barrel-shaped structure. The two end rings are each formed by seven CC alpha subunits, and the two central rings are each formed by seven beta CC subunits. The catalytic chamber with the active sites is on the inside CC of the barrel (By similarity). {ECO:0000250}. 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=EAY99887.1; Type=Erroneous initiation; 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; CM000131; EAY99887.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; A2Y9X7; -. DR SMR; A2Y9X7; -. DR STRING; 39946.A2Y9X7; -. DR MEROPS; T01.973; -. DR Proteomes; UP000007015; Chromosome 6. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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; cd03752; proteasome_alpha_type_4; 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:SF13; PROTEASOME SUBUNIT ALPHA TYPE-4; 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; Nucleus; Proteasome; Reference proteome. FT CHAIN 1..250 FT /note="Proteasome subunit alpha type-4-1" FT /id="PRO_0000361768" SQ SEQUENCE 250 AA; 27044 MW; 00FDAD801A97ABD4 CRC64; MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGN AGSALGVLAA DGVVLVGEKK VTSKLLQTSR SAEKMYKIDS HLACAVAGIM SDANILLNTA RLHAQRYALS YQEPIPVEQL VQSLCDTKQG YTQFGGLRPF GVSFLFAGWD KHHGFQLYMS DPSGNYSGWK AAAVGANSQA AQSMLKQDYR DGMTREEAVA LALKVLSKTM DSTSLTAEKL ELAEVFLQPG TGEVQYQVCS PEAMGKLLAK AGLSQPAPEA //