PSA3_MOUSE
ID PSA3_MOUSE Reviewed; 255 AA.
AC O70435;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Proteasome subunit alpha type-3;
DE AltName: Full=Macropain subunit C8;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C8;
DE AltName: Full=Proteasome component C8;
DE AltName: Full=Proteasome subunit K;
GN Name=Psma3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gao Y., Simons M.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=10436176; DOI=10.1007/s002510050562;
RA Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT "The complete primary structure of mouse 20S proteasomes.";
RL Immunogenetics 49:835-842(1999).
RN [3]
RP PROTEIN SEQUENCE OF 73-86.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, AND ACETYLATION AT
RP SER-2.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [5]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby
CC mediates its degradation. Negatively regulates the membrane trafficking
CC of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.
CC {ECO:0000269|PubMed:16581775, ECO:0000269|PubMed:22341445}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7
CC (PubMed:16857966, PubMed:22341445). Interacts with AURKB. Interacts
CC with CDKN1A. Interacts with MDM2 and RB1. Interacts with the C-terminus
CC of TBXA2R isoform 2. Interacts with DNAJB2.
CC {ECO:0000250|UniProtKB:P25788, ECO:0000269|PubMed:16857966,
CC ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus
CC {ECO:0000250|UniProtKB:P25788}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:P25788}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; AF055983; AAC12943.1; -; mRNA.
DR EMBL; AF060089; AAD50534.1; -; mRNA.
DR CCDS; CCDS25961.1; -.
DR RefSeq; NP_035314.3; NM_011184.5.
DR RefSeq; XP_017170485.1; XM_017314996.1.
DR PDB; 3UNB; X-ray; 2.90 A; F/T/h/v=1-255.
DR PDB; 3UNE; X-ray; 3.20 A; F/T/h/v=1-255.
DR PDB; 3UNF; X-ray; 2.90 A; F/T=1-255.
DR PDB; 3UNH; X-ray; 3.20 A; F/T=1-255.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; O70435; -.
DR SMR; O70435; -.
DR BioGRID; 202417; 68.
DR CORUM; O70435; -.
DR IntAct; O70435; 10.
DR STRING; 10090.ENSMUSP00000125548; -.
DR iPTMnet; O70435; -.
DR PhosphoSitePlus; O70435; -.
DR SwissPalm; O70435; -.
DR EPD; O70435; -.
DR jPOST; O70435; -.
DR PaxDb; O70435; -.
DR PeptideAtlas; O70435; -.
DR PRIDE; O70435; -.
DR ProteomicsDB; 291911; -.
DR Antibodypedia; 80; 313 antibodies from 35 providers.
DR DNASU; 19167; -.
DR Ensembl; ENSMUST00000160027; ENSMUSP00000125548; ENSMUSG00000060073.
DR GeneID; 19167; -.
DR KEGG; mmu:19167; -.
DR UCSC; uc007ntz.2; mouse.
DR CTD; 5684; -.
DR MGI; MGI:104883; Psma3.
DR VEuPathDB; HostDB:ENSMUSG00000060073; -.
DR eggNOG; KOG0184; Eukaryota.
DR GeneTree; ENSGT00550000074912; -.
DR HOGENOM; CLU_035750_0_0_1; -.
DR InParanoid; O70435; -.
DR OMA; SMYMHAY; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; O70435; -.
DR TreeFam; TF106208; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19167; 31 hits in 73 CRISPR screens.
DR ChiTaRS; Psma3; mouse.
DR PRO; PR:O70435; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; O70435; protein.
DR Bgee; ENSMUSG00000060073; Expressed in right kidney and 201 other tissues.
DR ExpressionAtlas; O70435; baseline and differential.
DR Genevisible; O70435; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
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; IPR037555; Proteasome_alpha_3.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF10; PTHR11599:SF10; 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:16857966"
FT CHAIN 2..255
FT /note="Proteasome subunit alpha type-3"
FT /id="PRO_0000124092"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:16857966"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25788"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 219..223
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 255 AA; 28405 MW; CFB4405E143CEB23 CRC64;
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV
HAYTLYSAVR PFGCSFMLGS YSANDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL
QMKEMTCRDV VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DIREEAEKYA
KESLKEEDES DDDNM
