PSA1_RAT
ID PSA1_RAT Reviewed; 263 AA.
AC P18420;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Proteasome subunit alpha type-1;
DE AltName: Full=Macropain subunit C2;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE AltName: Full=Proteasome component C2;
DE AltName: Full=Proteasome nu chain;
GN Name=Psma1;
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=2819072; DOI=10.1021/bi00444a028;
RA Fujiwara T., Tanaka K., Kumatori A., Shin S., Yoshimura T., Ichihara A.,
RA Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.;
RT "Molecular cloning of cDNA for proteasomes (multicatalytic proteinase
RT complexes) from rat liver: primary structure of the largest component
RT (C2).";
RL Biochemistry 28:7332-7340(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 1-30, AND ACETYLATION AT MET-1.
RC TISSUE=Liver;
RX PubMed=2335242; DOI=10.1016/0014-5793(90)81417-m;
RA Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T.,
RA Shimonishi Y.;
RT "The NH2-terminal residues of rat liver proteasome (multicatalytic
RT proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated.";
RL FEBS Lett. 263:373-375(1990).
RN [4]
RP PROTEIN SEQUENCE OF 63-82 AND 97-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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:P25786}.
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 Interacts with NOTCH3. Interacts with ZFAND1 (By similarity).
CC {ECO:0000250|UniProtKB:P25786}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus
CC {ECO:0000250|UniProtKB:P25786}. 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:P25786}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Proteolytically cleaved from a C-terminal extension in the course
CC of the conversion of the proteasome from its latent form into its
CC active form.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; M29859; AAA41943.1; -; mRNA.
DR EMBL; D90265; BAA14312.1; -; mRNA.
DR EMBL; BC062233; AAH62233.1; -; mRNA.
DR PIR; A32968; SNRTC2.
DR RefSeq; NP_058974.1; NM_017278.1.
DR PDB; 6EPC; EM; 12.30 A; F=1-263.
DR PDB; 6EPD; EM; 15.40 A; F=1-263.
DR PDB; 6EPE; EM; 12.80 A; F=1-263.
DR PDB; 6EPF; EM; 11.80 A; F=1-263.
DR PDB; 6TU3; EM; 2.70 A; F/T=1-263.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P18420; -.
DR SMR; P18420; -.
DR BioGRID; 248289; 2.
DR IntAct; P18420; 1.
DR STRING; 10116.ENSRNOP00000015946; -.
DR GlyGen; P18420; 1 site.
DR iPTMnet; P18420; -.
DR SwissPalm; P18420; -.
DR World-2DPAGE; 0004:P18420; -.
DR jPOST; P18420; -.
DR PaxDb; P18420; -.
DR PRIDE; P18420; -.
DR Ensembl; ENSRNOT00000015946; ENSRNOP00000015946; ENSRNOG00000011745.
DR GeneID; 29668; -.
DR KEGG; rno:29668; -.
DR UCSC; RGD:61841; rat.
DR CTD; 5682; -.
DR RGD; 61841; Psma1.
DR eggNOG; KOG0863; Eukaryota.
DR GeneTree; ENSGT00550000074855; -.
DR HOGENOM; CLU_035750_8_0_1; -.
DR InParanoid; P18420; -.
DR OMA; NTQVYGK; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; P18420; -.
DR TreeFam; TF106206; -.
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:P18420; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000011745; Expressed in ovary and 20 other tissues.
DR Genevisible; P18420; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; 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:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; 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 CDD; cd03749; proteasome_alpha_type_1; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035144; Proteasome_alpha1.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF12; PTHR11599:SF12; 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; Immunity; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome; Ubl conjugation.
FT CHAIN 1..263
FT /note="Proteasome subunit alpha type-1"
FT /id="PRO_0000124064"
FT REGION 232..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:2335242"
FT MOD_RES 110
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT CARBOHYD 110
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P25786"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 78..99
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 263 AA; 29518 MW; 68660696B43A4051 CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHVFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
QCNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP
QRKAQPSQAA DEPAEKADEP MEH
