PSA7_MOUSE
ID PSA7_MOUSE Reviewed; 248 AA.
AC Q9Z2U0;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Proteasome subunit alpha type-7;
DE AltName: Full=Proteasome subunit RC6-1;
GN Name=Psma7;
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].
RC STRAIN=B10.BR;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 96-109.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
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 [5]
RP INDUCTION.
RX PubMed=16317774; DOI=10.1002/pmic.200500218;
RA Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA Zhang X., Yang X.;
RT "The up-regulation of proteasome subunits and lysosomal proteases in
RT hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL Proteomics 6:498-504(2006).
RN [6]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
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 [7]
RP IDENTIFICATION BY 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 [8]
RP GLYCOSYLATION AT SER-130.
RC TISSUE=Brain, and Spleen;
RX PubMed=22556278; DOI=10.1074/mcp.m111.015966;
RA Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
RA Siele D., Kloetzel P.M., Janek K.;
RT "Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel
RT biotin-cystamine tag.";
RL Mol. Cell. Proteomics 11:467-477(2012).
RN [9]
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). {ECO:0000269|PubMed:16581775,
CC 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). PSMA7 interacts directly with the
CC PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By
CC similarity). Interacts with HIF1A (By similarity). Interacts with RAB7A
CC (By similarity). Interacts with PRKN (By similarity). Interacts with
CC ABL1 and ABL2 (By similarity). Interacts with EMAP2 (By similarity).
CC Interacts with MAVS (By similarity). {ECO:0000250|UniProtKB:O14818,
CC ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14818}. Nucleus
CC {ECO:0000250|UniProtKB:O14818}. 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:O14818}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- INDUCTION: Up-regulated in liver tumor tissues.
CC {ECO:0000269|PubMed:16317774}.
CC -!- PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of
CC proteasomal activity and cell cycle transition blocks.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; AF019662; AAC69150.1; -; mRNA.
DR EMBL; BC008222; AAH08222.1; -; mRNA.
DR CCDS; CCDS17166.1; -.
DR RefSeq; NP_036099.1; NM_011969.2.
DR PDB; 3UNB; X-ray; 2.90 A; C/Q/e/s=1-248.
DR PDB; 3UNE; X-ray; 3.20 A; C/Q/e/s=1-248.
DR PDB; 3UNF; X-ray; 2.90 A; C/Q=1-248.
DR PDB; 3UNH; X-ray; 3.20 A; C/Q=1-248.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; Q9Z2U0; -.
DR SMR; Q9Z2U0; -.
DR BioGRID; 204995; 56.
DR CORUM; Q9Z2U0; -.
DR IntAct; Q9Z2U0; 4.
DR STRING; 10090.ENSMUSP00000029082; -.
DR MEROPS; T01.974; -.
DR GlyGen; Q9Z2U0; 1 site.
DR iPTMnet; Q9Z2U0; -.
DR PhosphoSitePlus; Q9Z2U0; -.
DR SwissPalm; Q9Z2U0; -.
DR REPRODUCTION-2DPAGE; Q9Z2U0; -.
DR CPTAC; non-CPTAC-3734; -.
DR EPD; Q9Z2U0; -.
DR jPOST; Q9Z2U0; -.
DR MaxQB; Q9Z2U0; -.
DR PaxDb; Q9Z2U0; -.
DR PRIDE; Q9Z2U0; -.
DR ProteomicsDB; 291690; -.
DR Antibodypedia; 29428; 492 antibodies from 33 providers.
DR DNASU; 26444; -.
DR Ensembl; ENSMUST00000029082; ENSMUSP00000029082; ENSMUSG00000027566.
DR GeneID; 26444; -.
DR KEGG; mmu:26444; -.
DR UCSC; uc008oib.2; mouse.
DR CTD; 5688; -.
DR MGI; MGI:1347070; Psma7.
DR VEuPathDB; HostDB:ENSMUSG00000027566; -.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000159695; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; Q9Z2U0; -.
DR OMA; KICMLDH; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; Q9Z2U0; -.
DR TreeFam; TF106212; -.
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; 26444; 29 hits in 72 CRISPR screens.
DR ChiTaRS; Psma7; mouse.
DR PRO; PR:Q9Z2U0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z2U0; protein.
DR Bgee; ENSMUSG00000027566; Expressed in floor plate of midbrain and 262 other tissues.
DR ExpressionAtlas; Q9Z2U0; baseline and differential.
DR Genevisible; Q9Z2U0; 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:0098794; C:postsynapse; IDA:SynGO.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
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; IPR035190; Proteasome_alpha7.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF40; PTHR11599:SF40; 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;
KW Glycoprotein; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..248
FT /note="Proteasome subunit alpha type-7"
FT /id="PRO_0000124143"
FT MOD_RES 153
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT CARBOHYD 130
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:22556278"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3UNF"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 248 AA; 27855 MW; E2C8D607D8E2BC9C CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDDA
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQPLKIL NPEEIEKYVA EIEKEKEENE
KKKQKKAS
