PSA2_RAT
ID PSA2_RAT Reviewed; 234 AA.
AC P17220;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Proteasome subunit alpha type-2;
DE AltName: Full=Macropain subunit C3;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE AltName: Full=Proteasome component C3;
GN Name=Psma2;
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], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2340272; DOI=10.1021/bi00467a026;
RA Tanaka K., Fujiwara T., 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 from rat liver: primary
RT structure of component C3 with a possible tyrosine phosphorylation site.";
RL Biochemistry 29:3777-3785(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION
RP AT ALA-2.
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 [3]
RP PROTEIN SEQUENCE OF 5-39 AND 71-84, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, AND PHOSPHORYLATION AT
RP TYR-121.
RX PubMed=8794741; DOI=10.1021/bi960889p;
RA Benedict C.M., Clawson G.A.;
RT "Nuclear multicatalytic proteinase subunit RRC3 is important for growth
RT regulation in hepatocytes.";
RL Biochemistry 35:11612-11621(1996).
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:P25787}.
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:P25787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8794741}. Nucleus
CC {ECO:0000269|PubMed:8794741}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9 (By similarity).
CC Colocalizes with TRIM5 in cytoplasmic bodies (By similarity).
CC {ECO:0000250|UniProtKB:P25787, ECO:0000250|UniProtKB:P49722}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2340272}.
CC -!- PTM: Phosphorylated on tyrosine residues; which may be important for
CC nuclear import. {ECO:0000269|PubMed:8794741}.
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; J02897; AAA40838.1; -; mRNA.
DR PIR; A34535; SNRTC3.
DR RefSeq; NP_058975.1; NM_017279.1.
DR PDB; 6EPC; EM; 12.30 A; B=1-234.
DR PDB; 6EPD; EM; 15.40 A; B=1-234.
DR PDB; 6EPE; EM; 12.80 A; B=1-234.
DR PDB; 6EPF; EM; 11.80 A; B=1-234.
DR PDB; 6TU3; EM; 2.70 A; B/P=1-234.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P17220; -.
DR SMR; P17220; -.
DR BioGRID; 248290; 6.
DR IntAct; P17220; 2.
DR STRING; 10116.ENSRNOP00000066950; -.
DR MEROPS; T01.972; -.
DR iPTMnet; P17220; -.
DR PhosphoSitePlus; P17220; -.
DR World-2DPAGE; 0004:P17220; -.
DR jPOST; P17220; -.
DR PaxDb; P17220; -.
DR PRIDE; P17220; -.
DR Ensembl; ENSRNOT00000073834; ENSRNOP00000066950; ENSRNOG00000049920.
DR GeneID; 29669; -.
DR KEGG; rno:29669; -.
DR UCSC; RGD:61842; rat.
DR CTD; 5683; -.
DR RGD; 61842; Psma2.
DR eggNOG; KOG0181; Eukaryota.
DR GeneTree; ENSGT00550000074870; -.
DR HOGENOM; CLU_035750_4_1_1; -.
DR InParanoid; P17220; -.
DR OMA; YQEQIPT; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; P17220; -.
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-6798695; Neutrophil degranulation.
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:P17220; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000049920; Expressed in thymus and 20 other tissues.
DR Genevisible; P17220; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0009615; P:response to virus; ISO:RGD.
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; IPR001353; Proteasome_sua/b.
DR InterPro; IPR034644; Proteasome_subunit_alpha2.
DR PANTHER; PTHR11599:SF16; PTHR11599:SF16; 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:0000269|PubMed:2335242"
FT CHAIN 2..234
FT /note="Proteasome subunit alpha type-2"
FT /id="PRO_0000124079"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2335242"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P49722"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 121
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:8794741"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MUTAGEN 121
FT /note="Y->F: Abolishes nuclear localization and
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:8794741"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 64..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 133..139
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 234 AA; 25927 MW; 4ECB56A233583821 CRC64;
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA
