PSME1_MOUSE
ID PSME1_MOUSE Reviewed; 249 AA.
AC P97371; O35561; Q9D841;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Proteasome activator complex subunit 1;
DE AltName: Full=11S regulator complex subunit alpha;
DE Short=REG-alpha;
DE AltName: Full=Activator of multicatalytic protease subunit 1;
DE AltName: Full=Proteasome activator 28 subunit alpha;
DE Short=PA28a;
DE Short=PA28alpha;
GN Name=Psme1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=9218537; DOI=10.1007/s002510050281;
RA Kandil E., Kohda K., Ishibashi T., Tanaka K., Kasahara M.;
RT "PA28 subunits of the mouse proteasome: primary structures and chromosomal
RT localization of the genes.";
RL Immunogenetics 46:337-344(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=B10.BR;
RX PubMed=9162094; DOI=10.1007/s002510050246;
RA Jiang H., Monaco J.J.;
RT "Sequence and expression of mouse proteasome activator PA28 and the related
RT autoantigen Ki.";
RL Immunogenetics 46:93-98(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9590240;
RA Kohda K., Ishibashi T., Shimbara N., Tanaka K., Matsuda Y., Kasahara M.;
RT "Characterization of the mouse PA28 activator complex gene family: complete
RT organizations of the three member genes and a physical map of the
RT approximately 150-kb region containing the alpha- and beta-subunit genes.";
RL J. Immunol. 160:4923-4935(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvJ;
RX PubMed=11345588; DOI=10.1007/s002510100308;
RA Yawata M., Murata S., Tanaka K., Ishigatsubo Y., Kasahara M.;
RT "Nucleotide sequence analysis of the ~35-kb segment containing interferon-
RT gamma-inducible mouse proteasome activator genes.";
RL Immunogenetics 53:119-129(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC efficient antigen processing. The PA28 activator complex enhances the
CC generation of class I binding peptides by altering the cleavage pattern
CC of the proteasome.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC PSME1 can form homoheptamers (By similarity). {ECO:0000250}.
CC -!- INDUCTION: By interferon gamma.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; D87909; BAA22039.1; -; mRNA.
DR EMBL; U60328; AAC53295.1; -; mRNA.
DR EMBL; AB007136; BAA28835.1; -; Genomic_DNA.
DR EMBL; AB053120; BAB47403.1; -; Genomic_DNA.
DR EMBL; AK019390; BAB31696.1; -; mRNA.
DR EMBL; AK008514; BAB25712.1; -; mRNA.
DR CCDS; CCDS36931.1; -.
DR RefSeq; NP_035319.1; NM_011189.1.
DR PDB; 5MSJ; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-249.
DR PDB; 5MX5; X-ray; 2.90 A; A/C/E/G/H/J/L/N=1-249.
DR PDBsum; 5MSJ; -.
DR PDBsum; 5MX5; -.
DR AlphaFoldDB; P97371; -.
DR SMR; P97371; -.
DR BioGRID; 202432; 52.
DR IntAct; P97371; 1.
DR STRING; 10090.ENSMUSP00000134735; -.
DR iPTMnet; P97371; -.
DR PhosphoSitePlus; P97371; -.
DR SwissPalm; P97371; -.
DR EPD; P97371; -.
DR jPOST; P97371; -.
DR PaxDb; P97371; -.
DR PRIDE; P97371; -.
DR ProteomicsDB; 291577; -.
DR Antibodypedia; 1712; 322 antibodies from 38 providers.
DR DNASU; 19186; -.
DR Ensembl; ENSMUST00000174259; ENSMUSP00000134735; ENSMUSG00000022216.
DR GeneID; 19186; -.
DR KEGG; mmu:19186; -.
DR UCSC; uc007tzd.1; mouse.
DR CTD; 5720; -.
DR MGI; MGI:1096367; Psme1.
DR VEuPathDB; HostDB:ENSMUSG00000022216; -.
DR eggNOG; KOG4470; Eukaryota.
DR GeneTree; ENSGT00950000183098; -.
DR InParanoid; P97371; -.
DR OMA; GPIYSNE; -.
DR OrthoDB; 1251022at2759; -.
DR PhylomeDB; P97371; -.
DR TreeFam; TF106236; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19186; 8 hits in 77 CRISPR screens.
DR ChiTaRS; Psme1; mouse.
DR PRO; PR:P97371; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97371; protein.
DR Bgee; ENSMUSG00000022216; Expressed in peripheral lymph node and 259 other tissues.
DR ExpressionAtlas; P97371; baseline and differential.
DR Genevisible; P97371; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR GO; GO:0061133; F:endopeptidase activator activity; IDA:MGI.
DR GO; GO:0019884; P:antigen processing and presentation of exogenous antigen; IMP:MGI.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.120.180; -; 1.
DR Gene3D; 1.20.5.120; -; 1.
DR InterPro; IPR003186; PA28_C.
DR InterPro; IPR036997; PA28_C_sf.
DR InterPro; IPR036996; PA28_N_sf.
DR InterPro; IPR009077; Proteasome_activ_PA28.
DR InterPro; IPR003185; Proteasome_activ_PA28_N.
DR InterPro; IPR036252; Proteasome_activ_sf.
DR PANTHER; PTHR10660; PTHR10660; 1.
DR Pfam; PF02251; PA28_alpha; 1.
DR Pfam; PF02252; PA28_beta; 1.
DR SUPFAM; SSF47216; SSF47216; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Proteasome; Reference proteome.
FT CHAIN 1..249
FT /note="Proteasome activator complex subunit 1"
FT /id="PRO_0000161781"
FT REGION 59..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 17
FT /note="F -> L (in Ref. 5; BAB25712)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="K -> E (in Ref. 5; BAB25712)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> S (in Ref. 2; AAC53295)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="V -> L (in Ref. 2; AAC53295)"
FT /evidence="ECO:0000305"
FT HELIX 8..30
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 108..137
FT /evidence="ECO:0007829|PDB:5MX5"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5MSJ"
FT HELIX 148..190
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 196..232
FT /evidence="ECO:0007829|PDB:5MX5"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:5MX5"
SQ SEQUENCE 249 AA; 28673 MW; 1E2CE09DA44A5346 CRC64;
MATLRVHPEA QAKVDVFRED LCSKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP
LDIPVPDPVK EKEKEERKKQ QEKEEKEEKK KGDEDDKGPP CGPVNCNEKI VVLLQRLKPE
IKDVTEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TNLHTKLEGF HTQISKYFSE
RGDAVAKAAK QPHVGDYRQL VHELDEAEYQ EIRLMVMEIR NAYAVLYDII LKNFEKLKKP
RGETKGMIY
