PSME1_PIG
ID PSME1_PIG Reviewed; 249 AA.
AC Q64L94; Q863Z1;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Proteasome activator complex subunit 1;
DE AltName: Full=Proteasome activator 28 subunit alpha;
DE Short=PA28a;
DE Short=PA28alpha;
GN Name=PSME1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ILE-146; LEU-220 AND
RP GLY-228.
RX PubMed=15373739; DOI=10.1111/j.1365-2052.2004.01176.x;
RA Wang Y.F., Yu M., te Pas M.F.W., Yerle M., Liu B., Fan B., Xiong T.A.,
RA Li K.;
RT "Sequence characterization, polymorphism and chromosomal localizations of
RT the porcine PSME1 and PSME2 genes.";
RL Anim. Genet. 35:361-366(2004).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC PSME1 can form homoheptamers (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000305}.
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DR EMBL; AY317124; AAQ83574.1; -; Genomic_DNA.
DR EMBL; AF527990; AAP30878.1; -; mRNA.
DR RefSeq; NP_999469.1; NM_214304.1.
DR AlphaFoldDB; Q64L94; -.
DR SMR; Q64L94; -.
DR STRING; 9823.ENSSSCP00000002192; -.
DR PaxDb; Q64L94; -.
DR PeptideAtlas; Q64L94; -.
DR PRIDE; Q64L94; -.
DR Ensembl; ENSSSCT00015041951; ENSSSCP00015016569; ENSSSCG00015030054.
DR Ensembl; ENSSSCT00030087806; ENSSSCP00030040576; ENSSSCG00030062637.
DR Ensembl; ENSSSCT00050108041; ENSSSCP00050047858; ENSSSCG00050078329.
DR Ensembl; ENSSSCT00060013032; ENSSSCP00060004944; ENSSSCG00060010044.
DR GeneID; 397572; -.
DR KEGG; ssc:397572; -.
DR CTD; 5720; -.
DR eggNOG; KOG4470; Eukaryota.
DR InParanoid; Q64L94; -.
DR OrthoDB; 1251022at2759; -.
DR Reactome; R-SSC-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SSC-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-SSC-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SSC-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-SSC-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-SSC-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-SSC-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-SSC-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SSC-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-SSC-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SSC-382556; ABC-family proteins mediated transport.
DR Reactome; R-SSC-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-SSC-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-SSC-4641257; Degradation of AXIN.
DR Reactome; R-SSC-4641258; Degradation of DVL.
DR Reactome; R-SSC-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SSC-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SSC-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SSC-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-SSC-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-SSC-5632684; Hedgehog 'on' state.
DR Reactome; R-SSC-5658442; Regulation of RAS by GAPs.
DR Reactome; R-SSC-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SSC-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-SSC-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SSC-5689603; UCH proteinases.
DR Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR Reactome; R-SSC-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SSC-68949; Orc1 removal from chromatin.
DR Reactome; R-SSC-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SSC-69481; G2/M Checkpoints.
DR Reactome; R-SSC-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SSC-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SSC-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-SSC-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SSC-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-SSC-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-SSC-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-SSC-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SSC-8951664; Neddylation.
DR Reactome; R-SSC-9020702; Interleukin-1 signaling.
DR Reactome; R-SSC-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SSC-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
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 2: Evidence at transcript level;
KW Proteasome; Reference proteome.
FT CHAIN 1..249
FT /note="Proteasome activator complex subunit 1"
FT /id="PRO_0000161782"
FT REGION 60..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 VARIANT 146
FT /note="N -> I"
FT /evidence="ECO:0000269|PubMed:15373739"
FT VARIANT 220
FT /note="R -> L"
FT /evidence="ECO:0000269|PubMed:15373739"
FT VARIANT 228
FT /note="D -> G"
FT /evidence="ECO:0000269|PubMed:15373739"
SQ SEQUENCE 249 AA; 28617 MW; 90444860393908C4 CRC64;
MAALRVQPEA QAKVDVFRED LCTKTENLLG SYFPKKISEL DAFLKEPALN EANLSNLKAP
LDIPVPDPVK EKEKEERKKQ QEKEDKDEKK KGEDEDKGPP CGPVNCNEKI VVLLQRLKPE
IKDVIEQLNL VTTWLQLQIP RIEDGNNFGV AVQEKVFELM TALHTKLEGF HTQISKYFSE
RGDAVAKAAK QPHVGDYRQL VHELDEAEYR DIRLMVMEIR NAYAVLYDII LKNFEKLKKP
RGETKGMIY
