ID   PSMD7_BOVIN             Reviewed;         322 AA.
AC   Q3ZBD0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 7;
DE   AltName: Full=26S proteasome regulatory subunit RPN8;
GN   Name=PSMD7;
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=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-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:P51665}.
CC   -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC       The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC       regulatory subunits (RP). The regulatory particle is made of a lid
CC       composed of 9 subunits including PSMD7, a base containing 6 ATPases and
CC       few additional components. Within the complex, PSMD7 interacts with
CC       subunit PSMD4 through their respective MPN domain. Interacts with
CC       TRIM5. {ECO:0000250|UniProtKB:P51665}.
CC   -!- MISCELLANEOUS: Does not bind a metal ion.
CC       {ECO:0000250|UniProtKB:P51665}.
CC   -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR   EMBL; BC103437; AAI03438.1; -; mRNA.
DR   RefSeq; NP_001029595.1; NM_001034423.2.
DR   AlphaFoldDB; Q3ZBD0; -.
DR   SMR; Q3ZBD0; -.
DR   STRING; 9913.ENSBTAP00000024515; -.
DR   MEROPS; M67.973; -.
DR   PaxDb; Q3ZBD0; -.
DR   PRIDE; Q3ZBD0; -.
DR   Ensembl; ENSBTAT00000080934; ENSBTAP00000068694; ENSBTAG00000018425.
DR   GeneID; 512456; -.
DR   KEGG; bta:512456; -.
DR   CTD; 5713; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018425; -.
DR   VGNC; VGNC:33471; PSMD7.
DR   eggNOG; KOG1556; Eukaryota.
DR   GeneTree; ENSGT00950000183073; -.
DR   HOGENOM; CLU_027018_3_0_1; -.
DR   InParanoid; Q3ZBD0; -.
DR   OMA; HAMSIKT; -.
DR   OrthoDB; 1275837at2759; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000018425; Expressed in infraspinatus muscle and 102 other tissues.
DR   ExpressionAtlas; Q3ZBD0; baseline and differential.
DR   GO; GO:0000502; C:proteasome complex; IBA:GO_Central.
DR   GO; GO:0005838; C:proteasome regulatory particle; IEA:InterPro.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd08062; MPN_RPN7_8; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR033858; MPN_RPN7_8.
DR   InterPro; IPR024969; Rpn11/EIF3F_C.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Isopeptide bond; Proteasome; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..322
FT                   /note="26S proteasome non-ATPase regulatory subunit 7"
FT                   /id="PRO_0000330328"
FT   DOMAIN          9..144
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   REGION          281..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51665"
FT   MOD_RES         214
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P51665"
FT   MOD_RES         314
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26516"
FT   MOD_RES         315
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P26516"
FT   CROSSLNK        180
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P51665"
SQ   SEQUENCE   322 AA;  36754 MW;  FB9B2F8A601FB860 CRC64;
     MLELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE
     DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV
     LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK
     DTTVGTLSQR ITNQVHGLKG LNSKLLDIRG YLEKVATGKL PINHQIIYQL QDVFNLLPDV
     SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEDSKKDR
     KDDKEKEKEK SDVKKEEKKE KK