ID   PSA4_SPIOL              Reviewed;         250 AA.
AC   P52427;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Proteasome subunit alpha type-4;
DE   AltName: Full=20S proteasome alpha subunit C;
DE   AltName: Full=20S proteasome subunit alpha-3;
DE   AltName: Full=Proteasome 27 kDa subunit;
GN   Name=PAC1;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Baur B., Fischer K.;
RL   Submitted (APR-1996) 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}.
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DR   EMBL; X96974; CAA65660.1; -; mRNA.
DR   PIR; T09160; T09160.
DR   PDB; 7QVE; EM; 3.30 A; D/j=1-250.
DR   PDBsum; 7QVE; -.
DR   AlphaFoldDB; P52427; -.
DR   SMR; P52427; -.
DR   MEROPS; T01.973; -.
DR   Proteomes; UP001155700; Unplaced.
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   CDD; cd03752; proteasome_alpha_type_4; 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; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF234; PROTEASOME SUBUNIT ALPHA TYPE; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..250
FT                   /note="Proteasome subunit alpha type-4"
FT                   /id="PRO_0000124114"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           19..29
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          34..38
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          40..47
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          69..78
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           80..101
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           107..123
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          156..165
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           168..178
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           185..199
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          200..204
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           207..209
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:7QVE"
FT   HELIX           230..248
FT                   /evidence="ECO:0007829|PDB:7QVE"
SQ   SEQUENCE   250 AA;  27448 MW;  264B118E84B159D9 CRC64;
     MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGN AGSAIGILAK DGVVLIGEKK VTSKLLQTST
     STEKMYKIDD HVACAVAGIM SDANILINTA RVQAQRYTFS YQEPMPVEQL VQSLCDTKQG
     YTQFGGLRPF GVSFLFAGWD KNYGFQLYMS DPSGNYGGWK ATAIGANNQA AQSMLKQDYK
     DDVTREDAVK LALKALSKTM DSTSLTSEKL ELAEVYLLPS GKVKYQVHSP ESLNRLLTES
     GLTQPAAETS
//