PSA4_RAT
ID PSA4_RAT Reviewed; 261 AA.
AC P21670;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Proteasome subunit alpha type-4;
DE AltName: Full=Macropain subunit C9;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C9;
DE AltName: Full=Proteasome component C9;
DE AltName: Full=Proteasome subunit L;
GN Name=Psma4;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2358075; DOI=10.1016/0014-5793(90)80267-m;
RA Kumatori A., Tanaka K., Tamura T., Fujiwara T., Ichihara A., Tokunaga F.,
RA Onikura A., Iwanaga S.;
RT "cDNA cloning and sequencing of component C9 of proteasomes from rat
RT hepatoma cells.";
RL FEBS Lett. 264:279-282(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2249692; DOI=10.1111/j.1432-1033.1990.tb19399.x;
RA Sorimachi H., Tsukahara T., Kawasaki H., Ishiura S., Emori Y., Sugita H.,
RA Suzuki K.;
RT "Molecular cloning of cDNAs for two subunits of rat multicatalytic
RT proteinase. Existence of N-terminal conserved and C-terminal diverged
RT sequences among subunits.";
RL Eur. J. Biochem. 193:775-781(1990).
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:0000250|UniProtKB:P25789}.
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 {ECO:0000250|UniProtKB:P25789}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25789}. Nucleus
CC {ECO:0000250|UniProtKB:P25789}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9 (By similarity).
CC Colocalizes with TRIM5 in the cytoplasmic bodies (By similarity).
CC {ECO:0000250|UniProtKB:P25789, ECO:0000250|UniProtKB:Q9R1P0}.
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; X53304; CAA37390.1; -; mRNA.
DR EMBL; X55986; CAA39458.1; -; mRNA.
DR PIR; S10566; SNRTC9.
DR RefSeq; NP_058977.1; NM_017281.1.
DR PDB; 6EPC; EM; 12.30 A; C=1-261.
DR PDB; 6EPD; EM; 15.40 A; C=1-261.
DR PDB; 6EPE; EM; 12.80 A; C=1-261.
DR PDB; 6EPF; EM; 11.80 A; C=1-261.
DR PDB; 6TU3; EM; 2.70 A; C/Q=1-261.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P21670; -.
DR SMR; P21670; -.
DR BioGRID; 248292; 2.
DR IntAct; P21670; 2.
DR STRING; 10116.ENSRNOP00000018173; -.
DR MEROPS; T01.973; -.
DR iPTMnet; P21670; -.
DR PhosphoSitePlus; P21670; -.
DR World-2DPAGE; 0004:P21670; -.
DR jPOST; P21670; -.
DR PaxDb; P21670; -.
DR PRIDE; P21670; -.
DR Ensembl; ENSRNOT00000018173; ENSRNOP00000018173; ENSRNOG00000013493.
DR GeneID; 29671; -.
DR KEGG; rno:29671; -.
DR UCSC; RGD:61846; rat.
DR CTD; 5685; -.
DR RGD; 61846; Psma4.
DR eggNOG; KOG0178; Eukaryota.
DR GeneTree; ENSGT00550000074827; -.
DR HOGENOM; CLU_035750_4_3_1; -.
DR InParanoid; P21670; -.
DR OMA; YVLNDNM; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; P21670; -.
DR TreeFam; TF106209; -.
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:P21670; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000013493; Expressed in ovary and 20 other tissues.
DR Genevisible; P21670; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
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: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; IPR000426; Proteasome_asu_N.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR034647; Proteasome_subunit_alpha4.
DR PANTHER; PTHR11599:SF13; PTHR11599:SF13; 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 CHAIN 1..261
FT /note="Proteasome subunit alpha type-4"
FT /id="PRO_0000124106"
FT REGION 240..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25789"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25789"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25789"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25789"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25789"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 80..101
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 230..247
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 261 AA; 29498 MW; BB6742398E91E13B CRC64;
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK
EGEMTLKSAL ALAVKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
EEEEAKAERE KKEKEQREKD K
