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Database: UniProt
Entry: A0A453L8I7_AEGTS
LinkDB: A0A453L8I7_AEGTS
Original site: A0A453L8I7_AEGTS 
ID   A0A453L8I7_AEGTS        Unreviewed;       141 AA.
AC   A0A453L8I7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 18.
DE   RecName: Full=Proteasome subunit alpha type {ECO:0000256|RuleBase:RU000551};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET5Gv20670500.10, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET5Gv20670500.10}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) 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       {ECO:0000256|ARBA:ARBA00002000}.
CC   -!- SUBUNIT: 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.
CC       {ECO:0000256|RuleBase:RU000551}.
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. {ECO:0000256|ARBA:ARBA00026071}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000551}.
CC       Nucleus {ECO:0000256|RuleBase:RU000551}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00808, ECO:0000256|RuleBase:RU000551}.
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DR   AlphaFoldDB; A0A453L8I7; -.
DR   EnsemblPlants; AET5Gv20670500.10; AET5Gv20670500.10; AET5Gv20670500.
DR   Gramene; AET5Gv20670500.10; AET5Gv20670500.10; AET5Gv20670500.
DR   Proteomes; UP000015105; Chromosome 5D.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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:SF10; PROTEASOME SUBUNIT ALPHA TYPE-3; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU000551};
KW   Nucleus {ECO:0000256|RuleBase:RU000551};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW   ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000015105}.
FT   DOMAIN          8..30
FT                   /note="Proteasome alpha-type subunits"
FT                   /evidence="ECO:0000259|PROSITE:PS00388"
SQ   SEQUENCE   141 AA;  15587 MW;  5797CF83434048F5 CRC64;
     MSSIGTGYDL SVTTFSPDGR VFQVEYAGKA VDNSGTIVGI KCKDGIVLGV EKLITSKMIL
     AGSNRRLHSV HRNSGLAVAG LAADGRQIVS RAKSEAANYE KVYGEPMPVK ELADRVASYV
     HLCTLYWWLR AFWLWSYSWR L
//
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