PSME3_PIG
ID PSME3_PIG Reviewed; 254 AA.
AC P61291;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu M., Wang Y.F., te Pas M.F.W., Yerle M., Liu B., Fan B., Xiong T.A.,
RA Li K.;
RT "Investigation of the porcine PA28 activator gamma-subunit (PSME3) gene:
RT isolation, polymorphism and its chromosomal localization.";
RL J. Anim. Breed. Genet. 121:142-148(2004).
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; AY134854; AAN85724.1; -; mRNA.
DR RefSeq; NP_999513.1; NM_214348.1.
DR AlphaFoldDB; P61291; -.
DR SMR; P61291; -.
DR STRING; 9823.ENSSSCP00000018419; -.
DR PaxDb; P61291; -.
DR PeptideAtlas; P61291; -.
DR PRIDE; P61291; -.
DR Ensembl; ENSSSCT00000041498; ENSSSCP00000047936; ENSSSCG00000017385.
DR Ensembl; ENSSSCT00005015359; ENSSSCP00005009161; ENSSSCG00005010026.
DR Ensembl; ENSSSCT00015101976; ENSSSCP00015042260; ENSSSCG00015075406.
DR Ensembl; ENSSSCT00025073910; ENSSSCP00025031977; ENSSSCG00025054060.
DR Ensembl; ENSSSCT00030101041; ENSSSCP00030046615; ENSSSCG00030072129.
DR Ensembl; ENSSSCT00035016657; ENSSSCP00035005766; ENSSSCG00035013193.
DR Ensembl; ENSSSCT00040034358; ENSSSCP00040014175; ENSSSCG00040025703.
DR Ensembl; ENSSSCT00045012433; ENSSSCP00045008513; ENSSSCG00045007466.
DR Ensembl; ENSSSCT00050082721; ENSSSCP00050035493; ENSSSCG00050060716.
DR Ensembl; ENSSSCT00055049510; ENSSSCP00055039570; ENSSSCG00055025037.
DR Ensembl; ENSSSCT00060057729; ENSSSCP00060024698; ENSSSCG00060042579.
DR Ensembl; ENSSSCT00065004165; ENSSSCP00065001682; ENSSSCG00065003129.
DR Ensembl; ENSSSCT00070024466; ENSSSCP00070020248; ENSSSCG00070012475.
DR GeneID; 397625; -.
DR KEGG; ssc:397625; -.
DR CTD; 10197; -.
DR VGNC; VGNC:91926; PSME3.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR HOGENOM; CLU_062515_1_0_1; -.
DR InParanoid; P61291; -.
DR OMA; PCNKPLC; -.
DR OrthoDB; 1251022at2759; -.
DR TreeFam; TF106236; -.
DR Reactome; R-SSC-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SSC-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-SSC-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SSC-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-SSC-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-SSC-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-SSC-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-SSC-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SSC-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-SSC-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SSC-382556; ABC-family proteins mediated transport.
DR Reactome; R-SSC-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-SSC-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-SSC-4641257; Degradation of AXIN.
DR Reactome; R-SSC-4641258; Degradation of DVL.
DR Reactome; R-SSC-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SSC-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SSC-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SSC-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-SSC-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-SSC-5632684; Hedgehog 'on' state.
DR Reactome; R-SSC-5658442; Regulation of RAS by GAPs.
DR Reactome; R-SSC-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SSC-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-SSC-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SSC-5689603; UCH proteinases.
DR Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR Reactome; R-SSC-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SSC-68949; Orc1 removal from chromatin.
DR Reactome; R-SSC-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SSC-69481; G2/M Checkpoints.
DR Reactome; R-SSC-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SSC-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SSC-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-SSC-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SSC-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-SSC-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-SSC-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-SSC-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SSC-8951664; Neddylation.
DR Reactome; R-SSC-9020702; Interleukin-1 signaling.
DR Reactome; R-SSC-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SSC-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000008227; Chromosome 12.
DR Proteomes; UP000314985; Chromosome 12.
DR Bgee; ENSSSCG00000017385; Expressed in hindlimb bud and 44 other tissues.
DR ExpressionAtlas; P61291; baseline and differential.
DR Genevisible; P61291; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
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 GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
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_0000161791"
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; 29506 MW; 116FAB47D60A26C0 CRC64;
MASLLKVDQE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDSFLKEPIL NIHDLTQIHS
DMNLPVPDPI LLTNSHDGLD GPTYKKRRLD ECEEAFQGTK VFVMPNGMLK SNQQLVDIIE
KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS
RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE
KIKRPRSSNA ETLY
