PSME3_PONAB
ID PSME3_PONAB Reviewed; 254 AA.
AC Q5RFD3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Proteasome activator complex subunit 3;
DE AltName: Full=Activator of multicatalytic protease subunit 3;
DE AltName: Full=Proteasome activator 28 subunit gamma;
DE Short=PA28g;
DE Short=PA28gamma;
GN Name=PSME3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the 11S REG-gamma (also called PA28-gamma)
CC proteasome regulator, a doughnut-shaped homoheptamer which associates
CC with the proteasome. 11S REG-gamma activates the trypsin-like catalytic
CC subunit of the proteasome but inhibits the chymotrypsin-like and
CC postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53
CC interaction which promotes ubiquitination- and MDM2-dependent
CC proteasomal degradation of p53/TP53, limiting its accumulation and
CC resulting in inhibited apoptosis after DNA damage. May also be involved
CC in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1
CC inhibition (By similarity). {ECO:0000250|UniProtKB:P61289}.
CC -!- SUBUNIT: Homoheptamer; the stability of the heptamer is essential for
CC the specific activation of the trypsine-like subunit and inhibition of
CC the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits of
CC the proteasome. Interacts with p53/TP53, MDM2 and MAP3K3. Associates
CC with the proteasome. Interacts with CCAR2. Interacts with PSME3IP1 (via
CC C-terminus); the interaction is direct and promotes the association of
CC PSME3 with the 20S proteasome. Interacts with COIL; the interaction is
CC inhibited by PSME3IP1. {ECO:0000250|UniProtKB:P61289,
CC ECO:0000250|UniProtKB:P61290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Localizes to the cytoplasm during mitosis following nuclear
CC envelope breakdown at this distinct stage of the cell cycle which
CC allows its interaction with MAP3K3 kinase. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal sequences affect heptamer stability and
CC proteasome affinity. {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAP3K3. Phosphorylation at Ser-247 promotes its
CC association with CCAR2. {ECO:0000250|UniProtKB:P61289,
CC ECO:0000250|UniProtKB:P61290}.
CC -!- PTM: Acetylation at the major site Lys-195 is important for
CC oligomerization and ability to degrade its target substrates.
CC Deacetylated by SIRT1 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; CR857225; CAH89524.1; -; mRNA.
DR RefSeq; NP_001124661.1; NM_001131189.2.
DR AlphaFoldDB; Q5RFD3; -.
DR SMR; Q5RFD3; -.
DR STRING; 9601.ENSPPYP00000009413; -.
DR Ensembl; ENSPPYT00000009791; ENSPPYP00000009413; ENSPPYG00000008372.
DR GeneID; 100171504; -.
DR KEGG; pon:100171504; -.
DR CTD; 10197; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_1_0_1; -.
DR InParanoid; Q5RFD3; -.
DR OMA; PCNKPLC; -.
DR OrthoDB; 1251022at2759; -.
DR TreeFam; TF106236; -.
DR Proteomes; UP000001595; Chromosome 17.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT CHAIN 2..254
FT /note="Proteasome activator complex subunit 3"
FT /id="PRO_0000223498"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 195
FT /note="N6-acetyllysine; by P300/CBP"
FT /evidence="ECO:0000250|UniProtKB:P61289"
FT MOD_RES 247
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:P61289"
SQ SEQUENCE 254 AA; 29492 MW; E46EFA02395428DA CRC64;
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD DCEEAFQGTK VFVMPNGMLK SNQQLVDIIE
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE
KIKRPRSSNA ETLY
