PSA4_PETHY
ID PSA4_PETHY Reviewed; 249 AA.
AC O82530;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Proteasome subunit alpha type-4;
DE AltName: Full=20S proteasome alpha subunit C;
DE AltName: Full=20S proteasome subunit alpha-3;
GN Name=PAC1; Synonyms=PRS1;
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Petal;
RA Lee H.S., Moon J.H., Kim S.G.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; AF088914; AAC35982.1; -; mRNA.
DR AlphaFoldDB; O82530; -.
DR SMR; O82530; -.
DR MEROPS; T01.973; -.
DR PRIDE; O82530; -.
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; ISS:UniProtKB.
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:SF157; PTHR11599:SF157; 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 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Proteasome.
FT CHAIN 1..249
FT /note="Proteasome subunit alpha type-4"
FT /id="PRO_0000124113"
SQ SEQUENCE 249 AA; 27232 MW; 662E72C4945F11A5 CRC64;
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGN AGSAIGISSK DGVVLVGEKK VTSKLLQTST
SSEKMYKIDD HVACAVAGIM SDANILINTA RVQAQRYTFS YQEPMPVEQL VQSLCDTKQG
YTQYGGLPPF GVSFLFAGWD KNFGFQLFMS DPSGNYAGWK AAAIGANNQA AQSMLKQDYK
DDITREEAVQ LALKVLSKTM DSTSLTSEKL ELAEVFLSNG KVKYQACSPE KLNSMLVKSG
LTQPSAEES