ID Q569X4_MOUSE Unreviewed; 418 AA.
AC Q569X4;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=26S proteasome regulatory subunit 6B {ECO:0000256|ARBA:ARBA00018274};
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3 {ECO:0000256|ARBA:ARBA00030361};
DE AltName: Full=Proteasome 26S subunit ATPase 4 {ECO:0000256|ARBA:ARBA00030935};
GN Name=Psmc4 {ECO:0000313|EMBL:AAH92265.1, ECO:0000313|MGI:MGI:1346093};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH92265.1};
RN [1] {ECO:0000313|EMBL:AAH92265.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Mix FVB/N {ECO:0000313|EMBL:AAH92265.1};
RC TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old
RC {ECO:0000313|EMBL:AAH92265.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. PSMC4 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000256|ARBA:ARBA00002699}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; BC092265; AAH92265.1; -; mRNA.
DR AlphaFoldDB; Q569X4; -.
DR EPD; Q569X4; -.
DR PeptideAtlas; Q569X4; -.
DR AGR; MGI:1346093; -.
DR MGI; MGI:1346093; Psmc4.
DR ChiTaRS; Psmc4; mouse.
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:SF8; 26S PROTEASOME REGULATORY SUBUNIT 6B; 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 {ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000313|EMBL:AAH92265.1}.
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 37..71
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 418 AA; 47382 MW; 6FD2CE46EB1FF1E5 CRC64;
MEEIGILVEK IQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMHADIGGM DIQKQEVREA
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
//
