ID   PRS6A_DICDI             Reviewed;         421 AA.
AC   Q54PN7;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=26S proteasome regulatory subunit 6A homolog;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT5;
DE   AltName: Full=Proteasome 26S subunit ATPase 3;
GN   Name=psmC3; ORFNames=DDB_0232967;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
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   [2]
RP   PROTEIN SEQUENCE OF 233-248; 317-326 AND 369-379, AND IDENTIFICATION BY
RP   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   -!- SUBUNIT: May form a heterodimer with a related family member.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AAFI02000064; EAL65256.1; -; Genomic_DNA.
DR   RefSeq; XP_638617.1; XM_633525.1.
DR   AlphaFoldDB; Q54PN7; -.
DR   SMR; Q54PN7; -.
DR   STRING; 44689.DDB0232967; -.
DR   PaxDb; Q54PN7; -.
DR   EnsemblProtists; EAL65256; EAL65256; DDB_G0284415.
DR   GeneID; 8624588; -.
DR   KEGG; ddi:DDB_G0284415; -.
DR   dictyBase; DDB_G0284415; psmC3.
DR   eggNOG; KOG0652; Eukaryota.
DR   HOGENOM; CLU_000688_2_4_1; -.
DR   InParanoid; Q54PN7; -.
DR   OMA; HEKAAMG; -.
DR   PhylomeDB; Q54PN7; -.
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-6798695; Neutrophil degranulation.
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:Q54PN7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA: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: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   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   ATP-binding; Cytoplasm; Direct protein sequencing; Nucleotide-binding;
KW   Nucleus; Proteasome; Reference proteome.
FT   CHAIN           1..421
FT                   /note="26S proteasome regulatory subunit 6A homolog"
FT                   /id="PRO_0000388374"
FT   BINDING         209..216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   421 AA;  46870 MW;  9D6B54C31113E8DF CRC64;
     MSNKRTTTKD ESLPQAEKEA VIPDEIFQMT ADEVNRKAKL LENETKVLRS EHISKHLEMD
     SIQKRIKENN DKLQVNTQLP HLVANVVEII DMVLDGETQP SKCVVVKAST RQTIFLAYPG
     IVDVDKLRPG DLVGINKDSY IILDTLPPEY DSRVKAMEID EKPTEEYSDI GGLDKQIQEL
     VEAVVLPMTH KERFESIGIK PPKGVLMYGP PGTGKTLLAR ACAAQTNSTY LKLAGPQLVQ
     MFIGDGAKLV RDAFALAKEK GPTIIFIDEL DAIGTKRFDS EVSGDREVQR TMLELLNQLD
     GFSSDANIKV IAATNRIDIL DPALLRSGRL DRKIEFPLPN EEARAHILQI HSRKMNVSAD
     VNFDELARSS EDFNGAQLKA VCVEAGMIAL RRGGTELIHN DFVEGCVEVM AKKKKTLEYY
     A