ID   PSA4A_ARATH             Reviewed;         250 AA.
AC   O81148; O23711;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 164.
DE   RecName: Full=Proteasome subunit alpha type-4-A;
DE   AltName: Full=20S proteasome alpha subunit C-1;
DE   AltName: Full=Proteasome 27 kDa subunit;
DE   AltName: Full=Proteasome component 9;
DE   AltName: Full=Proteasome subunit alpha type-3;
GN   Name=PAC1; Synonyms=PRC9, PRS1; OrderedLocusNames=At3g22110;
GN   ORFNames=MKA23.2;
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 [MRNA].
RC   STRAIN=cv. Columbia;
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, GENE FAMILY, AND
RP   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=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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   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   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME
RP   COMPLEX, SUBUNIT, AND UBIQUITINATION AT LYS-40.
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   -!- TISSUE SPECIFICITY: Ubiquitous low levels, higher expression in
CC       siliques and flowers. {ECO:0000269|PubMed:9611183}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; Y13181; CAA73624.1; -; mRNA.
DR   EMBL; AF043521; AAC32057.1; -; mRNA.
DR   EMBL; AP001306; BAB03060.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76591.1; -; Genomic_DNA.
DR   EMBL; AF386953; AAK62398.1; -; mRNA.
DR   EMBL; BT000001; AAN15320.1; -; mRNA.
DR   EMBL; AY085914; AAM63126.1; -; mRNA.
DR   PIR; T51969; T51969.
DR   RefSeq; NP_188850.1; NM_113108.5.
DR   AlphaFoldDB; O81148; -.
DR   SMR; O81148; -.
DR   BioGRID; 7106; 63.
DR   IntAct; O81148; 2.
DR   STRING; 3702.AT3G22110.1; -.
DR   iPTMnet; O81148; -.
DR   MetOSite; O81148; -.
DR   PaxDb; O81148; -.
DR   PRIDE; O81148; -.
DR   ProteomicsDB; 226386; -.
DR   EnsemblPlants; AT3G22110.1; AT3G22110.1; AT3G22110.
DR   GeneID; 821774; -.
DR   Gramene; AT3G22110.1; AT3G22110.1; AT3G22110.
DR   KEGG; ath:AT3G22110; -.
DR   Araport; AT3G22110; -.
DR   TAIR; locus:2090399; AT3G22110.
DR   eggNOG; KOG0178; Eukaryota.
DR   HOGENOM; CLU_035750_4_3_1; -.
DR   InParanoid; O81148; -.
DR   OMA; YVLNDNM; -.
DR   OrthoDB; 1222564at2759; -.
DR   PhylomeDB; O81148; -.
DR   PRO; PR:O81148; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; O81148; baseline and differential.
DR   Genevisible; O81148; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA: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:0005773; C:vacuole; HDA:TAIR.
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   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; IPR034647; Proteasome_subunit_alpha4.
DR   PANTHER; PTHR11599:SF146; PTHR11599:SF146; 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   Cytoplasm; Isopeptide bond; Nucleus; Proteasome; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..250
FT                   /note="Proteasome subunit alpha type-4-A"
FT                   /id="PRO_0000124111"
FT   CROSSLNK        40
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:20516081"
FT   CROSSLNK        64
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:O81149"
FT   CONFLICT        24
FT                   /note="A -> V (in Ref. 1; CAA73624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   250 AA;  27475 MW;  5B8F105F2C336E5B CRC64;
     MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGN AGSAIGILSK DGVVLIGEKK VTSKLLQTST
     SAEKMYKIDD HVACAVAGIM SDANILINTA RVQAQRYTFM YQEPMPVEQL VQSLCDTKQG
     YTQFGGLRPF GVSFLFAGWD KHHGFQLYMS DPSGNYGGWK AAAVGANNQA AQSILKQDYK
     DDATREEAVE LALKVLTKTM DSTSLTSEKL ELAEVYLTPS KTVKYHVHSP ESLTKLLVKH
     GVTQPAAETS