ID   PRS10_ICTTR             Reviewed;         389 AA.
AC   P62335; P49719; Q92524;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=26S proteasome regulatory subunit 10B;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE   AltName: Full=Conserved ATPase domain protein 44;
DE            Short=CADp44;
DE   AltName: Full=Proteasome 26S subunit ATPase 6;
DE   AltName: Full=Proteasome subunit p42;
GN   Name=PSMC6; Synonyms=SUG2;
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS   tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8973309; DOI=10.1016/s0378-1119(96)00463-5;
RA   Bauer V.W., Swaffield J.C., Johnston S.A., Andrews M.T.;
RT   "CADp44: a novel regulatory subunit of the 26S proteasome and the mammalian
RT   homolog of yeast Sug2p.";
RL   Gene 181:63-69(1996).
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.
CC   -!- SUBUNIT: Found in the multi-protein complexes: the 26S proteasome
CC       (formed from the 20S proteasome and PA700), and the modulator. PA700
CC       consists of 28 subunits arranged to form a cylinder-shaped complex by
CC       four stacked rings, each containing seven subunits. Interacts with
CC       PAAF1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; U36395; AAB40354.1; -; mRNA.
DR   PIR; JC5349; JC5349.
DR   RefSeq; NP_001269189.1; NM_001282260.1.
DR   AlphaFoldDB; P62335; -.
DR   SMR; P62335; -.
DR   STRING; 43179.ENSSTOP00000012983; -.
DR   Ensembl; ENSSTOT00000014492; ENSSTOP00000012983; ENSSTOG00000014494.
DR   GeneID; 101969826; -.
DR   CTD; 5706; -.
DR   eggNOG; KOG0651; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_2_1; -.
DR   InParanoid; P62335; -.
DR   OMA; YNMTTFE; -.
DR   OrthoDB; 571919at2759; -.
DR   TreeFam; TF106229; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0036402; F:proteasome-activating activity; IEA:InterPro.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
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; IPR035263; PSMC6.
DR   PANTHER; PTHR23073:SF76; PTHR23073:SF76; 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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome.
FT   CHAIN           1..389
FT                   /note="26S proteasome regulatory subunit 10B"
FT                   /id="PRO_0000084734"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         72
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62333"
FT   MOD_RES         206
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62333"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62333"
SQ   SEQUENCE   389 AA;  44173 MW;  B26421295742CACD CRC64;
     MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
     LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
     NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
     TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
     RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
     IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD
     FVVQEDFMKA VRKVADSKKL ESKLDYKPV