ID   PSD12_BOVIN             Reviewed;         456 AA.
AC   Q2KJ25;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 12;
DE   AltName: Full=26S proteasome regulatory subunit RPN5;
GN   Name=PSMD12;
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 MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       This complex plays a key role in the maintenance of protein homeostasis
CC       by removing misfolded or damaged proteins, which could impair cellular
CC       functions, and by removing proteins whose functions are no longer
CC       required. Therefore, the proteasome participates in numerous cellular
CC       processes, including cell cycle progression, apoptosis, or DNA damage
CC       repair. {ECO:0000250|UniProtKB:O00232}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC       (By similarity). The 26S proteasome consists of a 20S core particle
CC       (CP) and two 19S regulatory subunits (RP) (By similarity). The
CC       regulatory particle is made of a lid composed of 9 subunits including
CC       PSMD12, a base containing 6 ATPases and few additional components (By
CC       similarity). Interacts with ERCC6 (By similarity).
CC       {ECO:0000250|UniProtKB:O00232}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit p55 family.
CC       {ECO:0000305}.
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DR   EMBL; BC105555; AAI05556.1; -; mRNA.
DR   RefSeq; NP_001039893.1; NM_001046428.1.
DR   AlphaFoldDB; Q2KJ25; -.
DR   SMR; Q2KJ25; -.
DR   IntAct; Q2KJ25; 1.
DR   STRING; 9913.ENSBTAP00000003145; -.
DR   PaxDb; Q2KJ25; -.
DR   PeptideAtlas; Q2KJ25; -.
DR   PRIDE; Q2KJ25; -.
DR   Ensembl; ENSBTAT00000003145; ENSBTAP00000003145; ENSBTAG00000002423.
DR   GeneID; 538204; -.
DR   KEGG; bta:538204; -.
DR   CTD; 5718; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002423; -.
DR   VGNC; VGNC:33463; PSMD12.
DR   eggNOG; KOG1498; Eukaryota.
DR   GeneTree; ENSGT00940000153510; -.
DR   HOGENOM; CLU_033860_2_0_1; -.
DR   InParanoid; Q2KJ25; -.
DR   OMA; AENEMFK; -.
DR   OrthoDB; 937686at2759; -.
DR   TreeFam; TF105721; -.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000002423; Expressed in oocyte and 103 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031595; C:nuclear proteasome complex; IBA:GO_Central.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035297; PSMD12.
DR   InterPro; IPR040134; PSMD12/CSN4.
DR   InterPro; IPR040896; RPN5_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10855; PTHR10855; 1.
DR   PANTHER; PTHR10855:SF1; PTHR10855:SF1; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18098; RPN5_C; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isopeptide bond; Proteasome; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
FT   CHAIN           2..456
FT                   /note="26S proteasome non-ATPase regulatory subunit 12"
FT                   /id="PRO_0000244600"
FT   DOMAIN          242..420
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
FT   MOD_RES         221
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
FT   MOD_RES         368
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
FT   CROSSLNK        92
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
FT   CROSSLNK        92
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O00232"
SQ   SEQUENCE   456 AA;  53053 MW;  C6144FBC24F304F0 CRC64;
     MADGGSERAD GRIVKMEVDY SATVDQRLPE CEKLAKEGRL QEVIETLLSL EKQTRTASDM
     VSTSRILVAI VKMCYEAKEW DLLNENIMLL SKRRSQLKQA VAKMVQQCCT YVEEITDLPI
     KLRLIDTLRM VTEGKIYVEI ERARLTKTLA TIKEQNGDVK EAASILQELQ VETYGSMEKK
     ERVEFILEQM RLCLAVKDYI RTQIISKKIN TKFFQEENTE KLKLKYYNLM IQLDQHEGSY
     LSICKHYRAI YDTPCIQAES EKWQQALKSV VLYVILAPFD NEQSDLVHRI SGDKKLEEIP
     KYKDLLKLFT TMELMRWSTL VEDYGMELRK GSLESPATDV FGYTEEGEKR WKDLKNRVVE
     HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK TIFAKVDRLA GIINFQRPKD
     PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE MIHNLQ