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PSA5_SOYBN
ID   PSA5_SOYBN              Reviewed;         237 AA.
AC   Q9M4T8;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Proteasome subunit alpha type-5;
DE   AltName: Full=20S proteasome alpha subunit E;
DE   AltName: Full=20S proteasome subunit alpha-5;
GN   Name=PAE1;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Choi J., Bhoo S.H., Park P.B.;
RT   "Isolation of a cDNA encoding 20S proteasome subunit from soybean.";
RL   Submitted (APR-2000) 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; AF255338; AAF70292.1; -; mRNA.
DR   RefSeq; NP_001235159.1; NM_001248230.1.
DR   AlphaFoldDB; Q9M4T8; -.
DR   SMR; Q9M4T8; -.
DR   STRING; 3847.GLYMA10G42650.1; -.
DR   PRIDE; Q9M4T8; -.
DR   ProMEX; Q9M4T8; -.
DR   GeneID; 547598; -.
DR   KEGG; gmx:547598; -.
DR   eggNOG; KOG0176; Eukaryota.
DR   InParanoid; Q9M4T8; -.
DR   OrthoDB; 1222564at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03753; proteasome_alpha_type_5; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR033812; Proteasome_alpha_type_5.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
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; Reference proteome.
FT   CHAIN           1..237
FT                   /note="Proteasome subunit alpha type-5"
FT                   /id="PRO_0000124127"
SQ   SEQUENCE   237 AA;  25980 MW;  ADEB685608400F67 CRC64;
     MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGL KTKEGVVLAV EKRITSPLLE
     PSSVEKIMEI DEHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA
     LRFGEGDEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNGKAIGS GSEGADSSLQ
     EQFNKDLTLQ EAETIALSIL KQVMEEKVTP NNVDIAKVAP TYHLYTPSEV EAVISRL
 
 
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