ID   PSM4B_DANRE             Reviewed;        1825 AA.
AC   F1R2X6;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2013, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Proteasome activator complex subunit 4B;
DE   AltName: Full=Proteasome activator PA200-B;
GN   Name=psme4b;
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}.
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DR   EMBL; AL935052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU459175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1R2X6; -.
DR   SMR; F1R2X6; -.
DR   STRING; 7955.ENSDARP00000127351; -.
DR   PaxDb; F1R2X6; -.
DR   ZFIN; ZDB-GENE-100316-4; psme4b.
DR   eggNOG; KOG1851; Eukaryota.
DR   InParanoid; F1R2X6; -.
DR   TreeFam; TF106237; -.
DR   Reactome; R-DRE-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-DRE-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-DRE-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-DRE-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-DRE-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-DRE-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-DRE-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR   Reactome; R-DRE-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-DRE-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-DRE-382556; ABC-family proteins mediated transport.
DR   Reactome; R-DRE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DRE-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-DRE-4641257; Degradation of AXIN.
DR   Reactome; R-DRE-4641258; Degradation of DVL.
DR   Reactome; R-DRE-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-DRE-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-DRE-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-DRE-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-DRE-5632684; Hedgehog 'on' state.
DR   Reactome; R-DRE-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-DRE-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-DRE-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DRE-5689603; UCH proteinases.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   Reactome; R-DRE-68949; Orc1 removal from chromatin.
DR   Reactome; R-DRE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-DRE-69481; G2/M Checkpoints.
DR   Reactome; R-DRE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-DRE-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-DRE-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-DRE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-DRE-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-DRE-8951664; Neddylation.
DR   Reactome; R-DRE-9755511; KEAP1-NFE2L2 pathway.
DR   Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:F1R2X6; -.
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..1825
FT                   /note="Proteasome activator complex subunit 4B"
FT                   /id="PRO_0000423301"
FT   REPEAT          458..502
FT                   /note="HEAT 1"
FT   REPEAT          981..1020
FT                   /note="HEAT 2"
FT   REPEAT          1162..1200
FT                   /note="HEAT 3"
FT   REPEAT          1336..1374
FT                   /note="HEAT 4"
FT   REPEAT          1618..1656
FT                   /note="HEAT 5"
FT   REPEAT          1662..1700
FT                   /note="HEAT 6"
FT   REGION          1632..1720
FT                   /note="Bromodomain-like (BRDL)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1825 AA;  209069 MW;  08AF21D72729BAD4 CRC64;
     MKKEQAEILG FVPQKEIVYN KLLPYADQLD RESNDILAQI KGNLGRAVQL RELWPGVLFW
     TRKLSTYLRL YGRKFSKEDH VLFIKLLYEL VTIPKLEISM MQSFARLLVN LLKKKELLSR
     DDLELPWRPL YDLYESILYS KTEHLGLNWF PNSVENVLKT LVKSCRVPES ATQEMLDEWR
     PLLCPFDVTM QKAIGYFELF LPTIMPPEQH DKGFKLWFDE MMNLWVSVQN LPAWEGNLVN
     LFARLANDNI GYVNWDPYIP KIFTRILRSF NLPVGTSQMV VPRYLTNSYD IGHVVLWISS
     MLGGPQNQSQ KQLNGLFSSI ASFYHPSNNG RWLMKLMKLL QRLPASIVRR LHRERYKKPC
     WITPVPSTHK LTDQDVTDFV ESMKQPVLMA MFSKTGSMDA AQALQNLALM RPELVIPPVL
     EKTYPAMETL TEPHQLTATL SCMIGMARSL LSGGRHYPEG PAHVLPLLMR ALPGVDPNDF
     SKCMITFQFI ATFTTLVPLV DCSSALHDKN DLTEMERELC SASAEFEDFV LQFMDRCFAL
     IDSSTLEQTR EETETEKMTH LESLVELGLS STFSTILTQC SMEIFKVALE KVFNFATTNI
     FETRVAGRMV ADMCRAASKC HPAESLRLFV PHCCNAITHL TANEDVSNEE ELDKELLWNL
     QLLSEVTRVD GEKLLPYRTQ LVQILQLTLR LRCKQGYSLA CNLLHHVLRS TALIYPTDYC
     SVPGGFSRPL QEYLPIKDWG RPGDLWNLEI QWHVPSTEET AFVFYVLDLL LQPELQRLQR
     YAQGEQEMSR DDVLQSLCIV QHCLLGAGSM LPPLDGSTVT GLVPSMVNLE ETKLYIGVDY
     DQSRENYREA VCKVMRQLLH YILEHSEDDT KSLFAIIKII SDLMHFKGSH KHEFDSRWKS
     FTLVKKSMEN RLHGKKQHIR ALLIDRVLLQ HEMRKLLVEG CEYKTVHQDL LRDLLRLSTS
     TYSQVRSKAQ NVLFTALGTY NFCCRDITPR VLEFLEPTRT DVTQQQFKGA LYCLLGNHCG
     VCLANLHDWD CIAQTWPAIV RSGLSSAMSL EKPSIVRLFD DLADKVHRQY ETIGIDFTVP
     ENAVFLGRSI TNSSQPTPHM GTPEDQELQQ GLAVQQAKNR EAEQKYEKLV KDLLECLDDR
     DLPWKFEHIA IGFLSLLLRD DYPLPAPAVF FFVQSLNHDA LVVRKMAIAA VAGILKQLKR
     PRKKIPVNPC DISGVTEPEE LEAGDRPGND WLQYHSESLP NSQQDWDAFC FVEKTHWGYY
     SWPKKLMVYA PAAEQPKDLA PDTMSEREAI INDHFTDPTF INQLIKFLSL EDRKGKDKFN
     PRRFCLFKGL FRNYSDAFLP VLKPHMERLA NDSHESTQRC VAEIIAGLIR GSKHWSFGKV
     EALWAFLIPL MRTALSNITV ETYADWGTCV ATACESRDPR KLHWLLEMLM ECPLSGEGGS
     FVDACHLYVL QGGLAQQEWR VPELLHRLLS YLEPKLTQVY KNVRERIGSV LTYIFMIDVA
     LPYTLPTKSP HIAEFTERIL SQLKPLIEGD EEIQNHVVEE NGVGEQDERT QAIKLLKTVL
     KWLMASAGRS FSTPVPQQLQ LLPLLFKIAP VENDDSYDEL KRDAKTCLSL MSQGLLYPEQ
     IPMVLAVLHE IAGSSSWHAR YSVLTYLQTM VFYNLFTILS SEQCVQGVRA LVIRLLEDEQ
     LEVREMAATT LSGFLQCNFL AMDSSMQTHF EALCKTRLPK KRKRDVGSVM DTIPSVDLVR
     RHAGVLGLSA CILSSPYDVP TWMPQLLMDL SAHLNDTQPI EMTVKKTLSN FRRTHHDNWL
     EHKQQFTDDQ LVVLTDLLVS PCYYA