ID   PSME4_BOVIN             Reviewed;        1845 AA.
AC   F1MKX4;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Proteasome activator complex subunit 4;
DE   AltName: Full=Proteasome activator PA200;
GN   Name=PSME4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [2]
RP   STRUCTURE OF THE PROTEASOME BY ELECTRON MICROSCOPY.
RX   PubMed=15713476; DOI=10.1016/j.jmb.2004.12.049;
RA   Ortega J., Heymann J.B., Kajava A.V., Ustrell V., Rechsteiner M.,
RA   Steven A.C.;
RT   "The axial channel of the 20S proteasome opens upon binding of the PA200
RT   activator.";
RL   J. Mol. Biol. 346:1221-1227(2005).
RN   [3]
RP   IDENTIFICATION IN THE PROTEASOME.
RX   PubMed=16275339; DOI=10.1016/s0076-6879(05)98026-9;
RA   Ustrell V., Pratt G., Gorbea C., Rechsteiner M.;
RT   "Purification and assay of proteasome activator PA200.";
RL   Methods Enzymol. 398:321-329(2005).
RN   [4]
RP   IDENTIFICATION IN THE SPERMATOPROTEASOME.
RX   PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
RA   Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F.,
RA   Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B.,
RA   Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y., Komatsu T.,
RA   Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L.,
RA   Goldberg A.L., Shen Y., Qiu X.B.;
RT   "Acetylation-mediated proteasomal degradation of core histones during DNA
RT   repair and spermatogenesis.";
RL   Cell 153:1012-1024(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 spermatogenesis and DNA
CC       damage response. Recognizes and binds acetylated histones via its
CC       bromodomain-like (BRDL) region and activates the proteasome by opening
CC       the gated channel for substrate entry. Binds to the core proteasome via
CC       its C-terminus, which occupies the same binding sites as the
CC       proteasomal ATPases, opening the closed structure of the proteasome via
CC       an active gating mechanism. Component of the spermatoproteasome, a form
CC       of the proteasome specifically found in testis: binds to acetylated
CC       histones and promotes degradation of histones, thereby participating
CC       actively to the exchange of histones during spermatogenesis. Also
CC       involved in DNA damage response in somatic cells, by promoting
CC       degradation of histones following DNA double-strand breaks (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Component of the spermatoproteasome, a form of the
CC       proteasome specifically found in testis (By similarity). Interacts with
CC       the 20S and 26S proteasomes. {ECO:0000250, ECO:0000269|PubMed:16275339,
CC       ECO:0000269|PubMed:23706739}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Found in nuclear
CC       foci following treatment with ionizing radiation, but not with
CC       ultraviolet irradiation or H(2)O(2). {ECO:0000250}.
CC   -!- DOMAIN: The bromodomain-like (BRDL) region specifically recognizes and
CC       binds acetylated histones. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BLM10 family. {ECO:0000305}.
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DR   EMBL; DAAA02030893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02030894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F1MKX4; -.
DR   SMR; F1MKX4; -.
DR   IntAct; F1MKX4; 1.
DR   STRING; 9913.ENSBTAP00000027001; -.
DR   PaxDb; F1MKX4; -.
DR   PRIDE; F1MKX4; -.
DR   eggNOG; KOG1851; Eukaryota.
DR   HOGENOM; CLU_000772_2_0_1; -.
DR   InParanoid; F1MKX4; -.
DR   OrthoDB; 83617at2759; -.
DR   TreeFam; TF106237; -.
DR   Proteomes; UP000009136; 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   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; DNA damage; DNA repair;
KW   Nucleus; Phosphoprotein; Proteasome; Reference proteome; Repeat;
KW   Spermatogenesis.
FT   CHAIN           1..1845
FT                   /note="Proteasome activator complex subunit 4"
FT                   /id="PRO_0000423299"
FT   REPEAT          475..519
FT                   /note="HEAT 1"
FT   REPEAT          1000..1039
FT                   /note="HEAT 2"
FT   REPEAT          1181..1219
FT                   /note="HEAT 3"
FT   REPEAT          1356..1394
FT                   /note="HEAT 4"
FT   REPEAT          1638..1676
FT                   /note="HEAT 5"
FT   REPEAT          1682..1720
FT                   /note="HEAT 6"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1652..1740
FT                   /note="Bromodomain-like (BRDL)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14997"
FT   MOD_RES         1616
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14997"
SQ   SEQUENCE   1845 AA;  211600 MW;  C2F31C84FCFD4FF4 CRC64;
     MEPAERAGGR DPLEPGGRPG PDPQGFVPQK EIVYNKLLPY AERLDAESDL QLAQIKSNLG
     RAVQLQELWP GGLFWTRKLS TYHRLYGRKF SKEDHVLFIK LLYELVSIPK LEISMMQGFA
     RLLINLLKKK ELLSRDDLEL PWRPLYDMVE RILYSKTEHL GLNWFPNSVE NVLKTLVKSC
     RPYFPADATA EMLEEWRPLM CPFDVTMQKA ITYFEIFLPT SLPPELHHKG FKLWFDELIG
     LWVSVQNLPQ WEGQLVNLFA RLATDNIGYI DWDPYVPKVF TRILRSLNLP VGSSQVLVPR
     FLTNAYDIGH AVVWITAMMG GPSKLVQKHL AGLFNSITSF YHPSNNGRWL NKLMKLLQRL
     PNSVVRRLHR ERYKKPSWLT PVPDSHKLTD QDVTDFVQCI IQPVLLAMFS KTGSLEAAQA
     LQNLALMRPE LVIPPVLERT YPALETLTEP HQLTATLSCV IGVARSLVSG GRWFPEGPTH
     MLPLLMRALP GVDPNDFSKC MITFQFIATF STLVPLVDCS SVLQERNDLT EVERELCSAT
     AEFEDFVLQF MDRCFGLIES STLEQTREET ETEKMTHLES LVELGLSSTF STILTQCSKE
     IFMVALQKVF NFSISHIFET RVAGRMVADM CRAAVKCCPE ESLKLFVPHC CGVITQLTMN
     DDVLNEEELD KELLWNLQLL SEITRVDGKK LLLYREQLVK ILQRTLHLTC KQGYTLSCNL
     LHHLLRSTTL IYPTEYCSVP GGFDKPPSEY FPIKDWGKPG DLWNLGIQWH VPSSEEVAFA
     FYLLDSFLQP ELIKLQRCGD GELEMSRDDV LQSLTIVHNC LIGSGNLLPP LKGEPVTNLV
     PSMVSLEETK LYTGLEYEID LSRENYRETI ARVIRKLLNH ILNNSEDDTK SLFLIIKIIG
     DLLQFQGSHK HEFDSRWKSF NLVKKSMENR LHGKKQHIRA LLIDRVMLQH ELRTLTVEGC
     EYKKIHQEMI RDLLRLSTSS YSQVRNKAQQ TFFAALGAYN FCCRDIIPLV LGFLRPDRQD
     VTQQQFKGAL YCLLGNHSGV CLANLHDWDC IVQTWPAIVS SGLSQAMSLE KPSIVRLFDD
     LAEKIHRQYE TIGLDFTVSK SCVGIAELLQ QSKNPSINQT MLSSEEIKEG LKRQQGRNVD
     ALRNYENLVN TLLDGVEQRN LPWKFEHIGI GLLSLLLRDD RVLPLRAIRF FVENLNHDAI
     VVRKMAISAV AGILKQLKRT HKKLTISPYE ISGYPKPTQI VAGDRPDNHW LHYDSKSIPR
     TKKEWESSCF VEKTHWGYYT WPQNMVVYAG VEEQPKLGRS REDLTEAEQI IFDHFSDPKF
     VEQLITFLSL EDRKGKDKFN PRRFCLFKGI FRNFDDAFLP VLKPHLERLV ADSHESTQRC
     VAEIIAGLIR GSKHWTFEKV EKLWELLCPL LRTALSNITV ETYNDWGTCI ATSCESRDPR
     KLHWLFELLL ESPLSGEGGS FVDACRLYVL QGGLAQQEWR VPELLHRLLK YLEPKLTQVY
     KNVRERIGSV LTYIFMIDVS LPNTAPTASP RVPEFTARIL EKLKPLMDVD EEIQNHVMEE
     NGIGEEDERT QGIKLLKTIL KWLMASAGRS FSTAVAEQLQ LLPLFFKIAP VENDNSYDEL
     KRDAKLCLSL MSQGLLYPHQ VPLVLQVLNQ TARSSSWHAR YTVLTYLQTM VFYNLFIFLN
     NEDAVKDIRW LVISLLEDEQ LEVREMAATT LSGLLQCNFL TMDSPMQIHF EQLCKTKLPK
     KRKRDPGFVG DTIPSAELVK RHAGVLGLGA CVLSSPYDVP TWMPQLLMNL SAHLNDPQPI
     EMTVKKTLSN FRRTHHDNWQ EHKQQFTDDQ LLVLTDLLVS PCYYA