ID   PSM4A_DANRE             Reviewed;        1833 AA.
AC   F1QFR9; E7F2L9;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Proteasome activator complex subunit 4A;
DE   AltName: Full=Proteasome activator PA200-A;
GN   Name=psme4a;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Associated component of the proteasome that specifically
CC       recognizes acetylated histones and promotes ATP- and ubiquitin-
CC       independent degradation of core histones during DNA damage response.
CC       Recognizes and binds acetylated histones via its bromodomain-like
CC       (BRDL) region and activates the proteasome by opening the gated channel
CC       for substrate entry. Binds to the core proteasome via its C-terminus,
CC       which occupies the same binding sites as the proteasomal ATPases,
CC       opening the closed structure of the proteasome via an active gating
CC       mechanism. involved in DNA damage response in somatic cells: binds to
CC       acetylated histones and promotes degradation of histones (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with the 20S and 26S proteasomes (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Nucleus speckle {ECO:0000250}.
CC   -!- DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and
CC       binds acetylated histones. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BLM10 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; FP067401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX663524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1QFR9; -.
DR   SMR; F1QFR9; -.
DR   STRING; 7955.ENSDARP00000129143; -.
DR   PaxDb; F1QFR9; -.
DR   PRIDE; F1QFR9; -.
DR   ZFIN; ZDB-GENE-091204-452; psme4a.
DR   eggNOG; KOG1851; Eukaryota.
DR   InParanoid; F1QFR9; -.
DR   TreeFam; TF106237; -.
DR   PRO; PR:F1QFR9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR   GO; GO:0016504; F:peptidase activator activity; ISS:UniProtKB.
DR   GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR032430; Blm10_mid.
DR   InterPro; IPR035309; PSME4.
DR   InterPro; IPR021843; PSME4_C.
DR   PANTHER; PTHR32170; PTHR32170; 1.
DR   Pfam; PF16507; BLM10_mid; 1.
DR   Pfam; PF11919; DUF3437; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Nucleus; Proteasome; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1833
FT                   /note="Proteasome activator complex subunit 4A"
FT                   /id="PRO_0000423300"
FT   REPEAT          460..504
FT                   /note="HEAT 1"
FT   REPEAT          983..1022
FT                   /note="HEAT 2"
FT   REPEAT          1164..1202
FT                   /note="HEAT 3"
FT   REPEAT          1344..1382
FT                   /note="HEAT 4"
FT   REPEAT          1626..1664
FT                   /note="HEAT 5"
FT   REPEAT          1670..1708
FT                   /note="HEAT 6"
FT   REGION          1095..1122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1640..1728
FT                   /note="Bromodomain-like (BRDL)"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1108..1122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1833 AA;  211144 MW;  E9427953A48AD8CD CRC64;
     MKKEASELLG FSPQKDIVYN ELLPYKDKLD DESNEILAQI KGNLGRAVQL REVWPGVLFW
     TRKLSTYIRL YGRKFNKEDH VLFVKLLYEL VTIPKLEISM MQSFARLLIT LLKKKELLSR
     EDLELPWRPL YELQDRILYS KTEHLGLNWF PSSVEAVLKV LIKSCRPYFP ESATQEMLDE
     WKPLMCPFDV TMQKAMGYFE LFLPTTLPPE LHDKGFKLWF DDLISLWVSV QNLPSWEVNL
     VSLFARLAND NIGYIDWDPY IPKIFTRILR SLNLPVGSSQ MLVSRYLTNA YDISYVVIWI
     SALLGGPSKQ AQTQLSGLFN GITSFFHPSN HGRWLMKLMK LLQRLPASVV KRLHRERYRT
     PTWLTPIPES HLLSEQDITD FVESIKQPVL LAMFSKTGSL DAAQALQNLA LLRPELVIPP
     VLEKTYPAME TLIEPHQLTA TLSCMIGVAR SLVAGGQRFP EGPKHMLPLL MRALPGVDPN
     DFSKCMITFQ FLATFVTLVP LVDCSSAIHS RNGLTQVEKE LCSASAEFEH FVLQFVDRCF
     ALIDTSTLEQ TREEMEMEKM THLESLVELG LSSTFSTILT QCSMEIFQVA LDKVFNFATT
     SIFETHVAGR MVADMCRATT KCHPAEALKL FLPHCCSAIL QIAANEEVLN EEELDKELMW
     NLQLLSEVVR VDGDQLLLYR SQLVQILQLT LHLKCKQGYS LACKLLYHIL RSMSLIYPRE
     YCSIPGGIQQ HTDTYLPIQD WGRPGELWNL EIQWHVPSTE ETEFVFYLLD LLLKPELQRL
     QKHTEGQQDI SRDDVLQSLS IVHNCFLGAS SLLPPLHGEP VPQLINGMVQ LYETKVYTGV
     DYDMSRENYR EDICKVIRPL LNHTLEHSED DIKSLFSIIK IINDLLHFKG SHKNEFDTRW
     KSFNLIKKSM ENRLHGSKQH IRALLIDRVM LQHELRNLTM EGCSYRSVHQ DLINDLLRLS
     TSRYSQVRCR AQNVLFTALG TYNFCCRDII PVVLKYLDPE RTDVTQQQFK GALYCLLGNH
     SGICLANLQY WDCIALTWPA LVRSGMSPSM SLEKTSIVRL FDDLADKIHR QYETISVNFS
     IPESCVEIAV KMLKSSSPEP NPGAASEQEE LEGRKREEQK NKDAMQKYEK LVADLLDCLH
     DRNIPWKFEQ LTIGFLSLML RDDLPLPSSA VLFFVESLNH DSLLVRNVAI SAVAGILKQL
     KRPHKKVAVS PYDISELKTS LQSPVVSLLT GDRPDNQWLQ YDSSRLPRSQ RDWDECCFIE
     KTHWGYSTWP RKLMLYAPLE EQPKQGQTRE EMNEREQIIY DHFSDQLFID QFIQYLSLED
     RKGKDKFSPR RFCLFKGLFR NFDDAFLPLL KPHMERLVAD SHESPQRCVA EIISGLIRGS
     KHWSYSKVEK LWALLCPLLR KALSNITIET YIDWGTCIAT ACESRDPRKL HWLFEMLMES
     PVTGEGGSFV DACRLYVLQG GLAQQEWRVP ELLHRLLQYL EPKLTQVYKN VRERIGSVLT
     YIFMIDVDLP YTQPTTSPRI REFTERVLAR LKPLTEGEEE IQNHIVEENM EGDQDERTQA
     IKLLKTVLKW LMTSAGRSFS SSVPEQLRLL PLLFKIAPVE NDDSYDEMKT DAKTCLSLMS
     QGLLYSDQIP QVLSALEEIS RSSSWHARYT ILTYLQIMVF YNLFTFLSDA KAVCDVRALV
     LRLLEDEQLE VREMAATTLS GFLQCNFLSI DEPMQAHFES LSKTRLPKRK RRELGSVVDT
     IPSADLVRRH AGVLGLSACI LSSPYDVPTW MPQILMDLSA HLNDTQPIEM TVKKTLSDFR
     RTHHDNWQEH KQKFTDDQLL VLTDLLVSPC YYA