PSME4_XENLA
ID PSME4_XENLA Reviewed; 1828 AA.
AC Q6NRP2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Proteasome activator complex subunit 4;
DE AltName: Full=Proteasome activator PA200;
GN Name=psme4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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; BC070702; AAH70702.1; -; mRNA.
DR RefSeq; NP_001084866.1; NM_001091397.1.
DR AlphaFoldDB; Q6NRP2; -.
DR SMR; Q6NRP2; -.
DR DNASU; 431915; -.
DR GeneID; 431915; -.
DR KEGG; xla:431915; -.
DR CTD; 431915; -.
DR Xenbase; XB-GENE-5841450; psme4.L.
DR OMA; GKDWSDE; -.
DR OrthoDB; 83617at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 431915; Expressed in egg cell and 19 other tissues.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cytoplasm; DNA damage; DNA repair; Nucleus; Proteasome; Reference proteome;
KW Repeat.
FT CHAIN 1..1828
FT /note="Proteasome activator complex subunit 4"
FT /id="PRO_0000280720"
FT REPEAT 462..506
FT /note="HEAT 1"
FT REPEAT 985..1024
FT /note="HEAT 2"
FT REPEAT 1164..1202
FT /note="HEAT 3"
FT REPEAT 1339..1377
FT /note="HEAT 4"
FT REPEAT 1621..1659
FT /note="HEAT 5"
FT REPEAT 1665..1703
FT /note="HEAT 6"
FT REGION 1635..1723
FT /note="Bromodomain-like (BRDL)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1828 AA; 210002 MW; 2133ACB3DC18271A CRC64;
MGAGEERPEA LGFNPQKEIV YNLLLPYAHR LDRESNELLA QIKGSLGRAV RLRELWPGVL
FWTRKLTTYI RLYGRKFSKE DHVLFVKLLY ELVTIPKLEI SMMQGFARLL ISLLKKKELL
SREDLQLPWR PLYEMLERIL YSKTEHLGLN WFPNSVEGVL KTLVKACRPY FPDDATAEML
QEWLPLMCPF DVTMQKAISY LELFLPTSLP PDLHCKGFRL WFDEFLTLWV SVQNLPQWEG
HLVNLFARLA NDNIGYIDWD PYVPKIFTRI LRSLNLPVGS NQVLVPRQLA NAYDIGHAVI
WITALMGGPS KTVQKHLTGL FNSITSFYHP SNNGRWLTKL MKLLQRLPCC IIRRLHRERY
KKPSWLTPVP ESHRLTDQDV TDFVESIMQP VLLAMFSKTG SLEAAQALQN LALMRPELVI
PPVLEKTYPA LETLTEPHQL TATLSCVIGV ARSLVSGGRW FPEGPTHMLP LLMRALPGVD
PNDFSKCMIT FQFIATFSTL VPLVDCSSLL QERNDLSEVE RELCSATAEF EDFVLQFMDR
CFALIESSAL EQTREETETE KMTHLESLVE LGLSSTFSTI LTQCSKEIFK VALEKVFNFA
VSNIFETRVS GRMVADLCRA AVKCCPVESL KLFLPHCCNV ISHLTINDDV MNDEELDKEL
LWKLQLLSEI TRVDGEKLLP YKEQLVQILH RTLHFTCKQG YTLSCNLLHH LLRSSTLIYP
TEYCSVPGGF DKPLSDYFPI KDWGKPGDLW NLNIKWHVPS AEEMDFAYYL LDTFLRPELQ
KLDLYSSGEL EMSRDEVQQC LAIVHNCLTG SGNLLPPLHG ERVTHLVTSM VSLNETKLFT
GIDHDHSREN YRELISKTLR KLLHYILDHS EDDTKSLFLI IKIISDLLQF QGSHKHEFDS
RWKSFTLVKK SMENRLHGKK RHIRALLIDR VMLQHELRTL TVEGCEYKKV HQDMLRDLLR
LSTSSYGQVR NKAQQAFFTA LGTYNFCCRD LIPLVLEFLR PERQDVTQQQ FKGALYCLLG
NHGGVCLANL HDWECIVQTW PAMISSGLSK AMSLEKPSIV RLFDDLAEKI HRQYETIGLD
FSVPEKCIEI AILLQHAAST SSQLPHPEEL ALAIKRQGEK NVEAVQNYER LVNTLLDCVT
QRNLPWKFEH IGIGFLSLLL RDDYVLPVRA IRYLVQCLNH DALIVRKMAI STVAGILKQL
KRTHVKETIC PYKISGCPKP ESKLVGDRPD NQWLLYDSSN LPNTKEAWES CCFVEKTHWG
YSSWPQNMLV YAPADQQPKV GRSREEMSEA EQIIYDHFTD EKFVDQLIKF LSLEDRKGKD
KFNPRRFCLF KGLFRNYDDA FLPIIKPHLE RLVADSHEST QRCAAEIVAG LIRGSKHWTF
EKVENLWNFL CELLRTALSN ITVETYSDWG TCIATSCESR DPRKLHWLFE LLLESPVSGE
GGSFVDACRL YVLQGGLAQQ EWRVPELLHR LLMCLEPKLT QVYKNVRERI GSVLTYIFMI
DVSLPNTAPT KSPHISDFTG RILGKLKPLM DADEEIQNHV MEENGVGEQD ERTQAIKLMK
TILKWIMASA GRSFCTGVTE QMQLLPLLFK IAPVENDTNY DELKRDAKTC LSLMSQGLLL
PVQVPLVLDV LRQTARSSSW HARYTVLTYI QTMVFYNLFI FIHNEESVQG VRWLILQLME
DEQLEVREMA ATTLSGLLQC NFLTMDAAMQ AHFEALCKTR LPKKRKRESG MVGDTIPSGD
LVKRHAGVLG LSACILSSPY DVPTWMPQLL MDLSVHLNDP QPIEMTVKKT LSNFRRTHHD
NWQEHKQQFT DDQLIVLTDL LVSPCYYA