PSA1_ORYSJ
ID PSA1_ORYSJ Reviewed; 270 AA.
AC P52428; Q0E466; Q6Z6I2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Proteasome subunit alpha type-1;
DE AltName: Full=20S proteasome alpha subunit F;
DE AltName: Full=20S proteasome subunit alpha-6;
DE AltName: Full=Proteasome component C2;
GN Name=PAF1; OrderedLocusNames=Os02g0133800, LOC_Os02g04100;
GN ORFNames=OsJ_05275 {ECO:0000312|EMBL:EEE56253.1}, P0030G11.18, P0585B01.3;
OS Oryza sativa subsp. japonica (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=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9230895; DOI=10.1007/s004380050470;
RA Umeda M., Fujii N., Manabe Y., Uchimiya H.;
RT "Molecular and biochemical characterization of a proteasome subunit from
RT rice and carrot cells.";
RL Mol. Gen. Genet. 255:19-27(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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=BAD08003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD10085.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D37886; BAA07128.1; -; mRNA.
DR EMBL; AP004799; BAD10085.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP004997; BAD08003.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008208; BAF07722.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS76843.1; -; Genomic_DNA.
DR EMBL; CM000139; EEE56253.1; -; Genomic_DNA.
DR EMBL; AK103646; BAG96186.1; -; mRNA.
DR EMBL; AK109376; BAG98703.1; -; mRNA.
DR PIR; T03925; T03925.
DR RefSeq; XP_015626959.1; XM_015771473.1.
DR AlphaFoldDB; P52428; -.
DR SMR; P52428; -.
DR STRING; 4530.OS02T0133800-01; -.
DR PaxDb; P52428; -.
DR PRIDE; P52428; -.
DR EnsemblPlants; Os02t0133800-01; Os02t0133800-01; Os02g0133800.
DR GeneID; 4328215; -.
DR Gramene; Os02t0133800-01; Os02t0133800-01; Os02g0133800.
DR KEGG; osa:4328215; -.
DR eggNOG; KOG0863; Eukaryota.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; P52428; -.
DR OMA; NTQVYGK; -.
DR OrthoDB; 1222564at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR Genevisible; P52428; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..270
FT /note="Proteasome subunit alpha type-1"
FT /id="PRO_0000124074"
FT REGION 239..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 270 AA; 29630 MW; 37954184C6588900 CRC64;
MFRNQYDTDV TTWSPAGRLF QVEYAMEAVK QGSACVGLRS RTHAVLAAAN KAASELSSHQ
RKVFRVADHA GVALAGLTAD GRVLSRFLRS ECINHAFVYD APLPVSRLAL RLADKAQVCT
QRSWKRPYGV GLLVAGLDES GAHLYYNCPS GNYFEYQAFA IGSRSQAAKT FLERRFEGYN
DYTPEQLIKD ALSAIKETLQ GEKLTSSNCT VAIVGRKDDG TVEPFEMIDV KRIQEIIDSM
EAAEEAPAAE AESSSMQEED KGTDAAPMDI
