PSB6_RAT
ID PSB6_RAT Reviewed; 238 AA.
AC P28073; Q6IE68; Q6PDW5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1 {ECO:0000250|UniProtKB:P28072};
DE AltName: Full=Macropain delta chain;
DE AltName: Full=Multicatalytic endopeptidase complex delta chain;
DE AltName: Full=Proteasome chain 5;
DE AltName: Full=Proteasome delta chain;
DE AltName: Full=Proteasome subunit Y;
DE Flags: Precursor;
GN Name=Psmb6; Synonyms=Psmb6l;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-238.
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 [4]
RP PROTEIN SEQUENCE OF 34-51.
RX PubMed=2335214; DOI=10.1016/0014-5793(90)80220-d;
RA Lilley K.S., Davison M.D., Rivett A.J.;
RT "N-terminal sequence similarities between components of the multicatalytic
RT proteinase complex.";
RL FEBS Lett. 262:327-329(1990).
RN [5]
RP PROTEIN SEQUENCE OF 67-78 AND 209-229, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION.
RX PubMed=15060002; DOI=10.1101/gr.1946304;
RA Puente X.S., Lopez-Otin C.;
RT "A genomic analysis of rat proteases and protease inhibitors.";
RL Genome Res. 14:609-622(2004).
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). Within the 20S core complex, PSMB6 displays a
CC peptidylglutamyl-hydrolyzing activity also termed postacidic or
CC caspase-like activity, meaning that the peptides bond hydrolysis occurs
CC directly after acidic residues. {ECO:0000250|UniProtKB:P28072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:P28072};
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:P28072}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28072}. Nucleus
CC {ECO:0000250|UniProtKB:P28072}. 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:P28072}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA01586.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC058451; AAH58451.1; -; mRNA.
DR EMBL; AABR03076595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D10754; BAA01586.1; ALT_INIT; mRNA.
DR EMBL; BN000325; CAE48380.1; -; mRNA.
DR PIR; JX0228; JX0228.
DR PIR; S09086; S09086.
DR RefSeq; NP_001316812.1; NM_001329883.1.
DR RefSeq; NP_476440.2; NM_057099.3.
DR PDB; 6EPC; EM; 12.30 A; 1=1-238.
DR PDB; 6EPD; EM; 15.40 A; 1=1-238.
DR PDB; 6EPE; EM; 12.80 A; 1=1-238.
DR PDB; 6EPF; EM; 11.80 A; 1=1-238.
DR PDB; 6TU3; EM; 2.70 A; H/V=1-238.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P28073; -.
DR SMR; P28073; -.
DR BioGRID; 248287; 3.
DR IntAct; P28073; 1.
DR STRING; 10116.ENSRNOP00000026507; -.
DR MEROPS; T01.010; -.
DR PhosphoSitePlus; P28073; -.
DR World-2DPAGE; 0004:P28073; -.
DR jPOST; P28073; -.
DR PaxDb; P28073; -.
DR PRIDE; P28073; -.
DR Ensembl; ENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
DR GeneID; 100360846; -.
DR GeneID; 29666; -.
DR KEGG; rno:100360846; -.
DR KEGG; rno:29666; -.
DR UCSC; RGD:61881; rat.
DR CTD; 5694; -.
DR RGD; 61881; Psmb6.
DR eggNOG; KOG0174; Eukaryota.
DR GeneTree; ENSGT00940000155114; -.
DR HOGENOM; CLU_035750_5_1_1; -.
DR InParanoid; P28073; -.
DR OMA; WTTDGSG; -.
DR OrthoDB; 1172133at2759; -.
DR PhylomeDB; P28073; -.
DR TreeFam; TF106221; -.
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:P28073; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019551; Expressed in quadriceps femoris and 16 other tissues.
DR Genevisible; P28073; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035140; Proteasome_beta6.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF46; PTHR11599:SF46; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT PROPEP 2..33
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2335214"
FT /id="PRO_0000026617"
FT CHAIN 34..238
FT /note="Proteasome subunit beta type-6"
FT /id="PRO_0000026618"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28072"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 82..103
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 154..164
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 238 AA; 25290 MW; 4B051AF11D78E49B CRC64;
MAAALAVRGA VSAPAFGPEA LTPDWENREV STGTTIMAVQ FDGGVVLGAD SRTTTGSYIA
NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS IELNEPPLVH TAASLFKEMC
YRYREDLMAG IIIAGWDPQE GGQVYSVPMG GMMVRQSFAI GGSGSSYIYG YVDATYREGM
TKDECLQFTA NALALAMERD GSSGGVIRLA AIQQSGVERQ VLLGDQIPKV TISTLPPP
