ID   PSME3_CHICK             Reviewed;         254 AA.
AC   Q5F3J5; P84176; Q5ZLM3;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Proteasome activator complex subunit 3;
DE   AltName: Full=Activator of multicatalytic protease subunit 3;
DE   AltName: Full=Proteasome activator 28 subunit gamma;
DE            Short=PA28g;
DE            Short=PA28gamma;
GN   Name=PSME3 {ECO:0000250|UniProtKB:P61290};
GN   ORFNames=RCJMB04_15e19, RCJMB04_5i13;
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] {ECO:0000305, ECO:0000312|EMBL:CAH65289.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAH65289.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAH65289.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, AND MASS SPECTROMETRY.
RC   TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX   PubMed=16287166; DOI=10.1002/pmic.200402056;
RA   Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA   Schneider J., Palomar M.A., Linares R.;
RT   "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT   development.";
RL   Proteomics 5:4946-4957(2005).
CC   -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC       efficient antigen processing. The PA28 activator complex enhances the
CC       generation of class I binding peptides by altering the cleavage pattern
CC       of the proteasome (By similarity). {ECO:0000250|UniProtKB:P61290}.
CC   -!- SUBUNIT: Homoheptamer. {ECO:0000250}.
CC   -!- PTM: Acetylation at the major site Lys-195 is important for
CC       oligomerization and ability to degrade its target substrates.
CC       Deacetylated by SIRT1 (By similarity). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=29602; Mass_error=2; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16287166};
CC   -!- SIMILARITY: Belongs to the PA28 family. {ECO:0000255}.
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; AJ719711; CAG31370.1; -; mRNA.
DR   EMBL; AJ851655; CAH65289.1; -; mRNA.
DR   RefSeq; NP_001012568.1; NM_001012550.2.
DR   AlphaFoldDB; Q5F3J5; -.
DR   SMR; Q5F3J5; -.
DR   STRING; 9031.ENSGALP00000038984; -.
DR   Ensembl; ENSGALT00000039775; ENSGALP00000038984; ENSGALG00000002937.
DR   GeneID; 420017; -.
DR   KEGG; gga:420017; -.
DR   CTD; 10197; -.
DR   VEuPathDB; HostDB:geneid_420017; -.
DR   eggNOG; KOG4470; Eukaryota.
DR   GeneTree; ENSGT00950000183098; -.
DR   HOGENOM; CLU_062515_1_0_1; -.
DR   InParanoid; Q5F3J5; -.
DR   OMA; PCNKPLC; -.
DR   OrthoDB; 1251022at2759; -.
DR   PhylomeDB; Q5F3J5; -.
DR   PRO; PR:Q5F3J5; -.
DR   Proteomes; UP000000539; Chromosome 27.
DR   Bgee; ENSGALG00000002937; Expressed in spermatid and 13 other tissues.
DR   ExpressionAtlas; Q5F3J5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR   GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR   GO; GO:0010950; P:positive regulation of endopeptidase activity; IBA:GO_Central.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR   Gene3D; 1.20.120.180; -; 1.
DR   Gene3D; 1.20.5.120; -; 1.
DR   InterPro; IPR003186; PA28_C.
DR   InterPro; IPR036997; PA28_C_sf.
DR   InterPro; IPR036996; PA28_N_sf.
DR   InterPro; IPR009077; Proteasome_activ_PA28.
DR   InterPro; IPR003185; Proteasome_activ_PA28_N.
DR   InterPro; IPR036252; Proteasome_activ_sf.
DR   PANTHER; PTHR10660; PTHR10660; 1.
DR   Pfam; PF02251; PA28_alpha; 1.
DR   Pfam; PF02252; PA28_beta; 1.
DR   SUPFAM; SSF47216; SSF47216; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Proteasome; Reference proteome.
FT   CHAIN           1..254
FT                   /note="Proteasome activator complex subunit 3"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000223499"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         14
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         195
FT                   /note="N6-acetyllysine; by P300/CBP"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        117
FT                   /note="D -> A (in Ref. 1; CAG31370)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   254 AA;  29481 MW;  1901CCB7A1B16B87 CRC64;
     MASLLKVDPE VKLKVDSFRE RITSEAEDLV ANFFPKKLLE LDGFLKEPIL NIHDLTQIHS
     DMNLPVPDPI LLTNSHDGLD GPNMKKRKLE DREETFQGTK VFVMPNGMLK SNQQLVDIIE
     KVKPEIRLLI EKCNTVKMWV QLLIPRIEDG NNFGVSIQEE TVAELRTVES EAASYLDQIS
     RYYITRAKLV SKIAKYPHVE DYRRTVTEID EKEYISLRLI ISELRNQYVT LHDMILKNIE
     KIKRPRSSNA ETLY