ID   PRS4_CHICK              Reviewed;         440 AA.
AC   Q90732;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=26S proteasome regulatory subunit 4;
DE            Short=P26s4;
DE   AltName: Full=26S proteasome AAA-ATPase subunit RPT2;
DE   AltName: Full=Proteasome 26S subunit ATPase 1;
GN   Name=PSMC1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8806779; DOI=10.1006/abbi.1996.0389;
RA   Singh I., Cai H., Wagner B.J.;
RT   "cDNA cloning of a chick homologue of human ATPase complex subunit 4,
RT   quantitative tissue distribution and tertiary structure comparison of the
RT   ATPase domain to RecA.";
RL   Arch. Biochem. Biophys. 333:260-266(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   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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; U60187; AAC60013.1; -; mRNA.
DR   PIR; S74197; S74197.
DR   RefSeq; NP_990289.1; NM_204958.1.
DR   AlphaFoldDB; Q90732; -.
DR   SMR; Q90732; -.
DR   STRING; 9031.ENSGALP00000017347; -.
DR   PaxDb; Q90732; -.
DR   PRIDE; Q90732; -.
DR   GeneID; 395804; -.
DR   KEGG; gga:395804; -.
DR   CTD; 5700; -.
DR   VEuPathDB; HostDB:geneid_395804; -.
DR   eggNOG; KOG0726; Eukaryota.
DR   InParanoid; Q90732; -.
DR   OrthoDB; 571919at2759; -.
DR   PhylomeDB; Q90732; -.
DR   PRO; PR:Q90732; -.
DR   Proteomes; UP000000539; Unplaced.
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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR005937; 26S_Psome_P45-like.
DR   InterPro; IPR035244; 26S_subunit_4.
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   PANTHER; PTHR23073:SF77; PTHR23073:SF77; 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;
KW   Reference proteome.
FT   CHAIN           1..440
FT                   /note="26S proteasome regulatory subunit 4"
FT                   /id="PRO_0000084680"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          84..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         226..233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   440 AA;  49204 MW;  259F5CA691218527 CRC64;
     MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKPP LVTPHTQCRL
     KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
     AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKLEKAP
     QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
     NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHGPS IVFIDEIDAI GTKRYDSNSG
     GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
     KKRIFQIHTS RMTLADDVTL DELIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
     KSKENFLYKK TEGTPEGLYL