PSA7_RAT
ID PSA7_RAT Reviewed; 254 AA.
AC P48004;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Proteasome subunit alpha type-7;
DE AltName: Full=Proteasome subunit RC6-1;
GN Name=Psma7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS RC6-IL AND RC6-IS), AND PARTIAL
RP PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=7578256; DOI=10.1016/0167-4781(95)00113-u;
RA Ni R., Tomita Y., Tokunaga F., Liang T.J., Noda C., Ichihara A., Tanaka K.;
RT "Molecular cloning of two types of cDNA encoding subunit RC6-I of rat
RT proteasomes.";
RL Biochim. Biophys. Acta 1264:45-52(1995).
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). Inhibits the transactivation function of HIF-1A
CC under both normoxic and hypoxia-mimicking conditions. The interaction
CC with EMAP2 increases the proteasome-mediated HIF-1A degradation under
CC the hypoxic conditions. Plays a role in hepatitis C virus internal
CC ribosome entry site-mediated translation. Mediates nuclear
CC translocation of the androgen receptor (AR) and thereby enhances
CC androgen-mediated transactivation. Promotes MAVS degradation and
CC thereby negatively regulates MAVS-mediated innate immune response.
CC {ECO:0000250|UniProtKB:O14818}.
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 PSMA7 interacts directly with the PSMG1-PSMG2 heterodimer which
CC promotes 20S proteasome assembly. Interacts with HIF1A. Interacts with
CC RAB7A. Interacts with PRKN. Interacts with ABL1 and ABL2. Interacts
CC with EMAP2. Interacts with MAVS. {ECO:0000250|UniProtKB:O14818}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=RC6-IL;
CC IsoId=P48004-1; Sequence=Displayed;
CC Name=RC6-IS;
CC IsoId=P48004-2; Sequence=VSP_005284;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D30804; BAA06463.1; -; mRNA.
DR PIR; S60038; S60038.
DR PDB; 6EPC; EM; 12.30 A; D=1-254.
DR PDB; 6EPD; EM; 15.40 A; D=1-254.
DR PDB; 6EPE; EM; 12.80 A; D=1-254.
DR PDB; 6EPF; EM; 11.80 A; D=1-254.
DR PDB; 6TU3; EM; 2.70 A; D/R=1-254.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P48004; -.
DR SMR; P48004; -.
DR IntAct; P48004; 2.
DR STRING; 10116.ENSRNOP00000011724; -.
DR GlyGen; P48004; 1 site.
DR PhosphoSitePlus; P48004; -.
DR jPOST; P48004; -.
DR PaxDb; P48004; -.
DR PeptideAtlas; P48004; -.
DR PRIDE; P48004; -.
DR RGD; 61851; Psma7.
DR eggNOG; KOG0183; Eukaryota.
DR InParanoid; P48004; -.
DR PhylomeDB; P48004; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641257; Degradation of AXIN.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P48004; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..254
FT /note="Proteasome subunit alpha type-7"
FT /id="PRO_0000124144"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT MOD_RES 233
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O14818"
FT CARBOHYD 136
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 75..80
FT /note="Missing (in isoform RC6-IS)"
FT /evidence="ECO:0000303|PubMed:7578256"
FT /id="VSP_005284"
FT CONFLICT 70
FT /note="C -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="T -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 17..26
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 61..74
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 83..104
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 159..168
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 254 AA; 28326 MW; C454A63F59B5FA8D CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAVVASVS GLTADARIVI NRARVECQSH RLTVGDPVTV EYITRYIASL
KQRYTQSNGR RPFGISALIV GFDFDGTPRL YQTDPSGTYH AWKANAIGRG AKSVREFLEK
NYTDDAIETD DLTIKLVIKA LLEVVQSGGK NIELAVMRRD QPLKILSPEE IEKYVAEIEK
EKEENEKKKQ KKAS
