ID   PSA1A_ARATH             Reviewed;         278 AA.
AC   P34066; O81150; Q8LF69;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Proteasome subunit alpha type-1-A;
DE   AltName: Full=20S proteasome alpha subunit F-1;
DE   AltName: Full=Proteasome 30 kDa subunit;
DE   AltName: Full=Proteasome component 2A;
DE            Short=AtPSM30;
DE   AltName: Full=Proteasome subunit alpha type-6;
DE   AltName: Full=Protein ARSENIC TOLERANCE 5;
GN   Name=PAF1; Synonyms=ARS5, PRC2A, PRS1, PSM30;
GN   OrderedLocusNames=At5g42790; ORFNames=MJB21.17;
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 [GENOMIC DNA], INDUCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=8264533; DOI=10.1007/bf00279901;
RA   Shirley B.W., Goodman H.M.;
RT   "An Arabidopsis gene homologous to mammalian and insect genes encoding the
RT   largest proteasome subunit.";
RL   Mol. Gen. Genet. 241:586-594(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
RN   [4]
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   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=9373170; DOI=10.1016/s0014-5793(97)01228-3;
RA   Parmentier Y., Bouchez D., Fleck J., Genschik P.;
RT   "The 20S proteasome gene family in Arabidopsis thaliana.";
RL   FEBS Lett. 416:281-285(1997).
RN   [8]
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   [9]
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   [10]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19453443; DOI=10.1111/j.1365-313x.2009.03914.x;
RA   Sung D.-Y., Kim T.-H., Komives E.A., Mendoza-Cozatl D.G., Schroeder J.I.;
RT   "ARS5 is a component of the 26S proteasome complex, and negatively
RT   regulates thiol biosynthesis and arsenic tolerance in Arabidopsis.";
RL   Plant J. 59:802-812(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP   COMPLEX, SUBUNIT, ACETYLATION AT MET-1, AND UBIQUITINATION AT LYS-51.
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       Negatively regulates thiol biosynthesis and arsenic tolerance.
CC       {ECO:0000269|PubMed:19453443}.
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   -!- DEVELOPMENTAL STAGE: Levels decrease as seedling grow (9-day-old) but
CC       is high in 3-week-old plants. {ECO:0000269|PubMed:8264533}.
CC   -!- INDUCTION: Slightly induced by heat-shock and high intensity light.
CC       {ECO:0000269|PubMed:8264533}.
CC   -!- DISRUPTION PHENOTYPE: Enhanced thiol accumulation and arsenic
CC       tolerance. Mutation can be complemented by overexpression of PAF2.
CC       {ECO:0000269|PubMed:19453443}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; M98495; AAA16326.1; -; Unassigned_DNA.
DR   EMBL; AF043526; AAC32062.1; -; mRNA.
DR   EMBL; AB007647; BAB10635.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94864.1; -; Genomic_DNA.
DR   EMBL; AF375447; AAK53031.1; -; mRNA.
DR   EMBL; AY058128; AAL25544.1; -; mRNA.
DR   EMBL; AY113047; AAM47355.1; -; mRNA.
DR   EMBL; AY085017; AAM61575.1; -; mRNA.
DR   PIR; S39900; S39900.
DR   PIR; T51974; T51974.
DR   RefSeq; NP_199093.1; NM_123644.5.
DR   AlphaFoldDB; P34066; -.
DR   SMR; P34066; -.
DR   BioGRID; 19540; 68.
DR   IntAct; P34066; 1.
DR   STRING; 3702.P34066; -.
DR   MEROPS; T01.976; -.
DR   iPTMnet; P34066; -.
DR   PaxDb; 3702-AT5G42790-1; -.
DR   ProteomicsDB; 226302; -.
DR   EnsemblPlants; AT5G42790.1; AT5G42790.1; AT5G42790.
DR   GeneID; 834290; -.
DR   Gramene; AT5G42790.1; AT5G42790.1; AT5G42790.
DR   KEGG; ath:AT5G42790; -.
DR   Araport; AT5G42790; -.
DR   TAIR; AT5G42790; PAF1.
DR   eggNOG; KOG0863; Eukaryota.
DR   HOGENOM; CLU_035750_8_0_1; -.
DR   InParanoid; P34066; -.
DR   OMA; NTQVYGK; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; P34066; -.
DR   PRO; PR:P34066; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P34066; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
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:0030163; P:protein catabolic process; ISS:TAIR.
DR   GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
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; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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   PANTHER; PTHR11599:SF12; PROTEASOME SUBUNIT ALPHA TYPE-1; 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.
DR   Genevisible; P34066; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   CHAIN           1..278
FT                   /note="Proteasome subunit alpha type-1-A"
FT                   /id="PRO_0000124072"
FT   REGION          238..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:20516081"
FT   CROSSLNK        51
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:20516081"
FT   CONFLICT        244
FT                   /note="G -> A (in Ref. 6; AAM61575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="E -> G (in Ref. 2; AAC32062 and 6; AAM61575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="R -> Q (in Ref. 2; AAC32062 and 6; AAM61575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        267
FT                   /note="V -> G (in Ref. 2; AAC32062 and 6; AAM61575)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  30476 MW;  93E1BC4D0EA99F70 CRC64;
     MFRNQYDTDV TTWSPTGRLF QVEYAMEAVK QGSAAIGLRS RSHVVLACVN KAQSELSSHQ
     RKIFKVDDHI GVAIAGLTAD GRVLSRYMRS ESINHSFTYE SPLPVGRLVV HLADKAQVCT
     QRSWKRPYGV GLLVGGLDES GAHLYYNCPS GNYFEYQAFA IGSRSQAAKT YLERRFESFG
     DSSREDLIKD AILAVRETLQ GETLKSSLCT VAILGVDEPF HFLDQEAIQK VIDTFEKVPE
     EEEGEGEAGE GEAEAAEAAP AERGGGVAGD QDVAPMEM
//