ID   PRS8_MANSE              Reviewed;         402 AA.
AC   P54814;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=26S proteasome regulatory subunit 8;
DE   AltName: Full=Protein 18-56;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8606008; DOI=10.1006/dbio.1996.0043;
RA   Sun D., Sathyanarayana U.G., Johnston S.A., Schwartz L.M.;
RT   "A member of the phylogenetically conserved CAD family of transcriptional
RT   regulators is dramatically up-regulated during the programmed cell death of
RT   skeletal muscle in the tobacco hawkmoth Manduca sexta.";
RL   Dev. Biol. 173:499-509(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 (By similarity). {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; U43728; AAC46996.1; -; mRNA.
DR   AlphaFoldDB; P54814; -.
DR   BMRB; P54814; -.
DR   SMR; P54814; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
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   InterPro; IPR035261; PSMC5.
DR   PANTHER; PTHR23073:SF102; PTHR23073:SF102; 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   ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome.
FT   CHAIN           1..402
FT                   /note="26S proteasome regulatory subunit 8"
FT                   /id="PRO_0000084728"
FT   BINDING         186..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   402 AA;  45338 MW;  4DE3F57F51FE235C CRC64;
     MTLTKMEVDS TKGEGFRPYY ITKIEELQLI VAEKSQNLRR LQAQRNELNA KVRMLREELQ
     LLQEQGSYVG EVVKPMDKKK VLVKVHPEGK FVVDLDKNVD INDVTANCRV ALRNESYTLH
     KILPNKVDPL VSLMMVEKVP DSTYEMVGGL DKQIKEIKEV IELPVKHPEL FDALGIAQPK
     GVLLYGPPGT GKTLLARAVA HHTECTFIRV SGSELVQKFI GEGSRMVREL FVMAREHAPS
     IIFMDEIDSI GSSRIESGSG GDSEVQRTML ELLNQLDGFE ATKNIKVIMA TNRIDILDPA
     LLRPGRIDRK IEFPPPNEEA RLDILKIHSR KMNLTRGINL RKIAELMPGA SGAEVKGVCT
     EAGMYALRER RVHVTQEDFE MAVAKVMQKD SEKNMSIKKL WK