ID   PSA6A_ARATH             Reviewed;         246 AA.
AC   O81146; O23713; Q0WR56; Q8RWN8;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 160.
DE   RecName: Full=Proteasome subunit alpha type-6-A;
DE   AltName: Full=20S proteasome subunit alpha A-1;
DE   AltName: Full=Proteasome component 1;
DE   AltName: Full=Proteasome subunit alpha type-1;
GN   Name=PAA1; Synonyms=PRC1; OrderedLocusNames=At5g35590; ORFNames=K2K18.4;
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], 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-246.
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   [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, 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   -!- 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}.
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; AF043518; AAC32054.1; -; mRNA.
DR   EMBL; AB023031; BAB09993.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED93984.1; -; Genomic_DNA.
DR   EMBL; AY092969; AAM12968.1; -; mRNA.
DR   EMBL; AY114564; AAM47883.1; -; mRNA.
DR   EMBL; AK228466; BAF00393.1; -; mRNA.
DR   EMBL; Y13691; CAA74025.1; -; mRNA.
DR   RefSeq; NP_198409.1; NM_122950.4.
DR   AlphaFoldDB; O81146; -.
DR   SMR; O81146; -.
DR   BioGRID; 18777; 77.
DR   IntAct; O81146; 2.
DR   STRING; 3702.AT5G35590.1; -.
DR   MEROPS; T01.971; -.
DR   iPTMnet; O81146; -.
DR   PaxDb; O81146; -.
DR   PRIDE; O81146; -.
DR   ProteomicsDB; 226305; -.
DR   EnsemblPlants; AT5G35590.1; AT5G35590.1; AT5G35590.
DR   GeneID; 833524; -.
DR   Gramene; AT5G35590.1; AT5G35590.1; AT5G35590.
DR   KEGG; ath:AT5G35590; -.
DR   Araport; AT5G35590; -.
DR   TAIR; locus:2157106; AT5G35590.
DR   eggNOG; KOG0182; Eukaryota.
DR   HOGENOM; CLU_035750_4_1_1; -.
DR   OMA; IDAHLMA; -.
DR   OrthoDB; 1222564at2759; -.
DR   PhylomeDB; O81146; -.
DR   PRO; PR:O81146; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; O81146; baseline and differential.
DR   Genevisible; O81146; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
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; IPR034642; Proteasome_subunit_alpha6.
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; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..246
FT                   /note="Proteasome subunit alpha type-6-A"
FT                   /id="PRO_0000124135"
FT   CONFLICT        55
FT                   /note="K -> E (in Ref. 4; AAM12968/AAM47883)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181..182
FT                   /note="KK -> EE (in Ref. 1; AAC32054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="E -> G (in Ref. 1; AAC32054)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   246 AA;  27294 MW;  8F90960EC9EA9CCD CRC64;
     MSRGSGAGYD RHITIFSPEG RLFQVEYAFK AVKTAGITSI GVRGKDSVCV VTQKKVPDKL
     LDQSSVTHLF PITKYIGLVA TGITADARSL VQQARNQAAE FRFTYGYEMP VDILAKWIAD
     KSQVYTQHAY MRPLGVVAMV MGVDEENGPL LYKCDPAGHF YGHKATSAGM KEQEAVNFLE
     KKMKENPSFT FDETVQTAIS ALQSVLQEDF KATEIEVGVV RAENPEFRAL TTEEIEEHLT
     AISERD