ID   PSA6_RAT                Reviewed;         246 AA.
AC   P60901; P34062;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Proteasome subunit alpha type-6;
DE   AltName: Full=Macropain iota chain;
DE   AltName: Full=Multicatalytic endopeptidase complex iota chain;
DE   AltName: Full=Proteasome iota chain;
GN   Name=Psma6;
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].
RX   PubMed=1491007; DOI=10.1093/oxfordjournals.jbchem.a123933;
RA   Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K.,
RA   Ichihara A.;
RT   "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures
RT   of four other subunits.";
RL   J. Biochem. 112:530-534(1992).
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 12-21; 60-71; 154-164 AND 229-246, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) 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:P60900}.
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 ALKBH4. {ECO:0000250|UniProtKB:P60900}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P60900,
CC       ECO:0000250|UniProtKB:Q9QUM9}. Nucleus {ECO:0000250|UniProtKB:P60900}.
CC       Note=Translocated from the cytoplasm into the nucleus following
CC       interaction with AKIRIN2, which bridges the proteasome with the nuclear
CC       import receptor IPO9 (By similarity). Colocalizes with TRIM5 in
CC       cytoplasmic bodies (By similarity). {ECO:0000250|UniProtKB:P60900,
CC       ECO:0000250|UniProtKB:Q9QUM9}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; D10755; BAA01587.1; -; mRNA.
DR   EMBL; BC062232; AAH62232.1; -; mRNA.
DR   PIR; JX0230; JX0230.
DR   RefSeq; NP_058979.1; NM_017283.3.
DR   PDB; 6EPC; EM; 12.30 A; A=1-246.
DR   PDB; 6EPD; EM; 15.40 A; A=1-246.
DR   PDB; 6EPE; EM; 12.80 A; A=1-246.
DR   PDB; 6EPF; EM; 11.80 A; A=1-246.
DR   PDB; 6TU3; EM; 2.70 A; A/O=1-246.
DR   PDBsum; 6EPC; -.
DR   PDBsum; 6EPD; -.
DR   PDBsum; 6EPE; -.
DR   PDBsum; 6EPF; -.
DR   PDBsum; 6TU3; -.
DR   AlphaFoldDB; P60901; -.
DR   EMDB; EMD-10586; -.
DR   EMDB; EMD-3913; -.
DR   EMDB; EMD-3914; -.
DR   EMDB; EMD-3915; -.
DR   EMDB; EMD-3916; -.
DR   SMR; P60901; -.
DR   BioGRID; 248294; 5.
DR   IntAct; P60901; 1.
DR   STRING; 10116.ENSRNOP00000009666; -.
DR   MEROPS; T01.971; -.
DR   GlyCosmos; P60901; 1 site, No reported glycans.
DR   GlyGen; P60901; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P60901; -.
DR   PhosphoSitePlus; P60901; -.
DR   jPOST; P60901; -.
DR   PaxDb; 10116-ENSRNOP00000009666; -.
DR   Ensembl; ENSRNOT00000009666.7; ENSRNOP00000009666.3; ENSRNOG00000007114.7.
DR   Ensembl; ENSRNOT00055023043; ENSRNOP00055018686; ENSRNOG00055013444.
DR   Ensembl; ENSRNOT00060035234; ENSRNOP00060028969; ENSRNOG00060020304.
DR   Ensembl; ENSRNOT00065007447; ENSRNOP00065005177; ENSRNOG00065005071.
DR   GeneID; 29673; -.
DR   KEGG; rno:29673; -.
DR   UCSC; RGD:61849; rat.
DR   AGR; RGD:61849; -.
DR   CTD; 5687; -.
DR   RGD; 61849; Psma6.
DR   eggNOG; KOG0182; Eukaryota.
DR   GeneTree; ENSGT00550000074807; -.
DR   HOGENOM; CLU_035750_4_1_1; -.
DR   InParanoid; P60901; -.
DR   OMA; YGYDMPV; -.
DR   OrthoDB; 166567at2759; -.
DR   PhylomeDB; P60901; -.
DR   TreeFam; TF106210; -.
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-174113; SCF-beta-TrCP mediated degradation of Emi1.
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:P60901; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000007114; Expressed in testis and 20 other cell types or tissues.
DR   ExpressionAtlas; P60901; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0030016; C:myofibril; IDA:BHF-UCL.
DR   GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0005844; C:polysome; 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:0005840; C:ribosome; ISS:BHF-UCL.
DR   GO; GO:0030017; C:sarcomere; IDA:BHF-UCL.
DR   GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR   GO; GO:0003723; F:RNA binding; ISS:BHF-UCL.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISS:BHF-UCL.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd03754; proteasome_alpha_type_6; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 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; IPR034642; Proteasome_subunit_alpha6.
DR   PANTHER; PTHR11599:SF11; PROTEASOME SUBUNIT ALPHA TYPE-6; 1.
DR   PANTHER; PTHR11599; PROTEASOME SUBUNIT ALPHA/BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
DR   World-2DPAGE; 0004:P60901; -.
DR   Genevisible; P60901; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Glycoprotein; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT   CHAIN           1..246
FT                   /note="Proteasome subunit alpha type-6"
FT                   /id="PRO_0000124132"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60900"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60900"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P60900"
FT   MOD_RES         102
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60900"
FT   MOD_RES         104
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P60900"
FT   MOD_RES         159
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QUM9"
FT   CARBOHYD        5
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
FT   TURN            10..12
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           23..32
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          45..53
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           63..65
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           84..105
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           111..125
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          136..144
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          162..169
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           172..180
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           194..204
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   STRAND          214..224
FT                   /evidence="ECO:0007829|PDB:6TU3"
FT   HELIX           232..241
FT                   /evidence="ECO:0007829|PDB:6TU3"
SQ   SEQUENCE   246 AA;  27399 MW;  94D1FD3C0A7CC72A CRC64;
     MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
     LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
     ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
     KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
     ALAERD
//