PSB6_DICDI
ID PSB6_DICDI Reviewed; 214 AA.
AC Q55GJ6; O60953;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Proteasome subunit beta type-6;
DE EC=3.4.25.1;
DE AltName: Full=Differentiation-associated proteasome subunit 1;
DE Short=DAPS-1;
DE Flags: Precursor;
GN Name=psmB6; Synonyms=dapA; ORFNames=DDB_G0267390;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=9535814; DOI=10.1006/bbrc.1998.8306;
RA Chae S.-C., Maeda Y.;
RT "Preferential expression of the cDNA encoding the proteasome subunit during
RT the growth/differentiation transition of Dictyostelium cells.";
RL Biochem. Biophys. Res. Commun. 245:231-234(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP PROTEIN SEQUENCE OF 15-32, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=8130037; DOI=10.1006/jsbi.1993.1044;
RA Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A.,
RA Gerisch G., Baumeister W.;
RT "Proteasomes from Dictyostelium discoideum: characterization of structure
RT and function.";
RL J. Struct. Biol. 111:135-147(1993).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity.
CC {ECO:0000269|PubMed:8130037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809,
CC ECO:0000269|PubMed:8130037}. Nucleus {ECO:0000269|PubMed:8130037}.
CC -!- DEVELOPMENTAL STAGE: Maximally expressed 4-6 hours after starvation
CC (around the aggregation-stream stage), followed by a drastic decrease
CC from the mound to tipped aggregate stage. {ECO:0000269|PubMed:9535814}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AB007024; BAA25923.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73147.1; -; Genomic_DNA.
DR PIR; JE0101; JE0101.
DR RefSeq; XP_647188.1; XM_642096.1.
DR AlphaFoldDB; Q55GJ6; -.
DR SMR; Q55GJ6; -.
DR STRING; 44689.DDB0191199; -.
DR MEROPS; T01.010; -.
DR PaxDb; Q55GJ6; -.
DR EnsemblProtists; EAL73147; EAL73147; DDB_G0267390.
DR GeneID; 8615992; -.
DR KEGG; ddi:DDB_G0267390; -.
DR dictyBase; DDB_G0267390; psmB6.
DR eggNOG; KOG0174; Eukaryota.
DR HOGENOM; CLU_035750_5_2_1; -.
DR InParanoid; Q55GJ6; -.
DR OMA; HKQAYAI; -.
DR PhylomeDB; Q55GJ6; -.
DR Reactome; R-DDI-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q55GJ6; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IPI:dictyBase.
DR GO; GO:0005634; C:nucleus; IPI:dictyBase.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:dictyBase.
DR GO; GO:0004175; F:endopeptidase activity; IDA:dictyBase.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:dictyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR037559; Proteasome_beta_Pre3.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF4; PTHR11599:SF4; 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 Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Protease;
KW Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..14
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:8130037"
FT /id="PRO_0000327384"
FT CHAIN 15..214
FT /note="Proteasome subunit beta type-6"
FT /id="PRO_0000327385"
FT ACT_SITE 15
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 25
FT /note="G -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="M -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="S -> C (in Ref. 1; BAA25923)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="Missing (in Ref. 1; BAA25923)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="E -> R (in Ref. 1; BAA25923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23446 MW; 1EA0E6921D37AAE2 CRC64;
MEAPEWLDNA VDLGTSIMAV EYDGGVIMGA DSRTTTGAYI ANRVTNKITP IHERIYCCRS
GSAADTQAIS DYVRYYLEMH TSELCDEPDV KTAASLFQLL CYSNKNNLMA GIIVAGWDKH
QGGSVYNISL GGSMVKQPFA IGGSGSTYIY GYCDSKFKPK MTKDECIEFV QNSLALAMFR
DGSSGGVIRL CIIDKNGVER KMIPGNNLPR FWEG
