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 27-MAR-2024, entry version 90.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U43728; AAC46996.1; -; mRNA.
DR AlphaFoldDB; P54814; -.
DR BMRB; P54814; -.
DR SMR; P54814; -.
DR EnsemblMetazoa; XM_030180656.2; XP_030036516.1; LOC115452188.
DR OrthoDB; 360215at2759; -.
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 CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF166; 26S PROTEASOME REGULATORY SUBUNIT 8; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//