ID   PRS8_XENLA              Reviewed;         461 AA.
AC   P46470; P79961;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=26S proteasome regulatory subunit 8;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE   AltName: Full=Proteasome 26S subunit ATPase 5;
DE   AltName: Full=SUG1 homolog;
DE            Short=xSUG1;
GN   Name=psmc5; Synonyms=sug1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Nacken W.K.F., Kingsman A., Kingsman S., Sablitzky F., Sorg C.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RA   Nacken W.K.F., Sorg C.;
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The 26S proteasome is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins (By similarity). The regulatory
CC       (or ATPase) complex confers ATP dependency and substrate specificity to
CC       the 26S complex (By similarity). {ECO:0000250|UniProtKB:P62195}.
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; X81986; CAA57512.1; -; mRNA.
DR   RefSeq; NP_001081635.1; NM_001088166.1.
DR   AlphaFoldDB; P46470; -.
DR   BMRB; P46470; -.
DR   SMR; P46470; -.
DR   BioGRID; 99304; 3.
DR   MaxQB; P46470; -.
DR   GeneID; 397968; -.
DR   KEGG; xla:397968; -.
DR   CTD; 397968; -.
DR   Xenbase; XB-GENE-17338635; psmc5.S.
DR   OrthoDB; 571919at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 397968; Expressed in neurula embryo and 19 other tissues.
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: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; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; 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   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   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..461
FT                   /note="26S proteasome regulatory subunit 8"
FT                   /id="PRO_0000084725"
FT   BINDING         185..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  52248 MW;  5045D4EFFA4C64A2 CRC64;
     MEQMEMDESR GGTGLRQYYL SKIEDLQLVV NDKSQNLRRL QAQRNELNAK VRLLREELQL
     LQEQGSYVGE VVRAMDKKKV LVKVHPEGKF VVDVDKNIDI NDVTPNCRVA LRNDSYTLHK
     ILPNKVDPLV SLMMVEKVPD STYEMIGGLD KQIKEIKEVI ELPVKHPEHF EALGIAQPKG
     VLLYGPPGTG KTLLARAVAH HTDCTFIRVS GSELVQKFIG EGARMVRELF VMAREHAPSI
     IFMDEIDSIG SRLEGGSGGD SEVQRTMLEL LNQLDGFEAT KNIKVIMATN RIDILDSALL
     RPGRIDRKIE FPPPNEEARL DILKIHSRKM NLTRGINLRK IAELMPGASG AEVKGVCTEA
     GMYALRERRV HVTQEDFEMA VAKVMQKDSE KNMSIKKLWK CFFLVPILCS TVCFQLKPSD
     VYYMGAWLIK PTRFNRRIIT NSYHLQIFKP TIVLANGECH N