PRS6B_DICDI
ID PRS6B_DICDI Reviewed; 403 AA.
AC P34123; Q54I49;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=26S proteasome regulatory subunit 6B homolog;
DE AltName: Full=Tat-binding protein homolog 2;
GN Name=psmC4; Synonyms=tbp2, tbpB; ORFNames=DDB_G0289003;
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].
RC STRAIN=AX4;
RX PubMed=8323548; DOI=10.1006/bbrc.1993.1765;
RA Shaw D.R., Ennis H.L.;
RT "Molecular cloning and developmental regulation of Dictyostelium discoideum
RT homologues of the human and yeast HIV1 Tat-binding protein.";
RL Biochem. Biophys. Res. Commun. 193:1291-1296(1993).
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 1-10; 186-197; 215-223; 260-272; 328-336 AND 395-403,
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
CC -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highest expression in vegetatively growing cells.
CC The level of expression falls steadily throughout multicellular
CC development and are not found in dormant or germinating spores.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; L16578; AAA33253.1; -; mRNA.
DR EMBL; AAFI02000129; EAL62917.1; -; Genomic_DNA.
DR PIR; JN0611; JN0611.
DR RefSeq; XP_636422.1; XM_631330.1.
DR AlphaFoldDB; P34123; -.
DR SMR; P34123; -.
DR STRING; 44689.DDB0191435; -.
DR PaxDb; P34123; -.
DR EnsemblProtists; EAL62917; EAL62917; DDB_G0289003.
DR GeneID; 8626913; -.
DR KEGG; ddi:DDB_G0289003; -.
DR dictyBase; DDB_G0289003; psmC4.
DR eggNOG; KOG0727; Eukaryota.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P34123; -.
DR OMA; AYAAQVK; -.
DR PhylomeDB; P34123; -.
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:P34123; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005838; C:proteasome regulatory particle; ISS:dictyBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0006972; P:hyperosmotic response; IEP:dictyBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035256; PSMC4.
DR PANTHER; PTHR23073:SF120; PTHR23073:SF120; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Nucleotide-binding; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..403
FT /note="26S proteasome regulatory subunit 6B homolog"
FT /id="PRO_0000084691"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3"
SQ SEQUENCE 403 AA; 45542 MW; BC433B2D29587383 CRC64;
MEELGLATAK VTVTKEASHH READLYQKMK SLESKLDFFN IQEEYIKYEY KNLKRELLHA
QEEVKRIRSV PLLIGQLLEM VDSNTGIVQS TSGSTLCVRI LSTIDRELLK PSASVALQRH
SNALVDTLPP ESDSSIHLLG ADEKPSESYS DIGGGDIQKQ EMREAVELPL THHNLYKQIG
IDPPRGVLLY GPPGTGKTML AKAVAHHTSA AFIRVVGSEF VQKYLGEGPR LVRDVFRLAR
ENSPAIIFID EIDAIATKRF DAQTGADREV QRILMELLNQ MDGFDVSVNV KVIMATNRQD
TLDPALLRPG RLDRKIEFPL PDRRQKRLIF QVITSKMNLS DEVDLEDYVS RPDKLSGAEI
QSICQEAGMH AIRKNRYVIL PKDFEKGYKA SIKKNTHEFN FYN
