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PSD11_BOVIN
ID   PSD11_BOVIN             Reviewed;         422 AA.
AC   Q2KI42; A1L5A1; F1MXM5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 11;
DE   AltName: Full=26S proteasome regulatory subunit RPN6;
GN   Name=PSMD11;
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 [MRNA] (ISOFORM 2).
RX   PubMed=12140684; DOI=10.1007/s00335-001-2145-4;
RA   Sonstegard T.S., Capuco A.V., White J., Van Tassell C.P., Connor E.E.,
RA   Cho J., Sultana R., Shade L., Wray J.E., Wells K.D., Quackenbush J.;
RT   "Analysis of bovine mammary gland EST and functional annotation of the Bos
RT   taurus gene index.";
RL   Mamm. Genome 13:373-379(2002).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) 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. In the complex, PSMD11 is required for proteasome assembly.
CC       Plays a key role in increased proteasome activity in embryonic stem
CC       cells (ESCs): its high expression in ESCs promotes enhanced assembly of
CC       the 26S proteasome, followed by higher proteasome activity.
CC       {ECO:0000250|UniProtKB:O00231}.
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 PSMD11, a base containing 6 ATPases
CC       and few additional components. {ECO:0000250|UniProtKB:O00231}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2KI42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2KI42-2; Sequence=VSP_044398, VSP_044399;
CC   -!- PTM: Phosphorylated by AMPK. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S9 family. {ECO:0000305}.
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DR   EMBL; BT029888; ABM06138.1; -; mRNA.
DR   EMBL; DAAA02048509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DAAA02048510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC112777; AAI12778.1; -; mRNA.
DR   RefSeq; NP_001039613.1; NM_001046148.1. [Q2KI42-1]
DR   AlphaFoldDB; Q2KI42; -.
DR   SMR; Q2KI42; -.
DR   STRING; 9913.ENSBTAP00000025152; -.
DR   PaxDb; Q2KI42; -.
DR   PeptideAtlas; Q2KI42; -.
DR   PRIDE; Q2KI42; -.
DR   Ensembl; ENSBTAT00000025152; ENSBTAP00000025152; ENSBTAG00000018897. [Q2KI42-1]
DR   Ensembl; ENSBTAT00000054679; ENSBTAP00000051244; ENSBTAG00000018897. [Q2KI42-2]
DR   Ensembl; ENSBTAT00000077447; ENSBTAP00000059925; ENSBTAG00000018897. [Q2KI42-1]
DR   GeneID; 513461; -.
DR   KEGG; bta:513461; -.
DR   CTD; 5717; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018897; -.
DR   eggNOG; KOG1463; Eukaryota.
DR   GeneTree; ENSGT00530000063301; -.
DR   HOGENOM; CLU_029573_2_1_1; -.
DR   InParanoid; Q2KI42; -.
DR   OMA; LYFDTGM; -.
DR   OrthoDB; 1052430at2759; -.
DR   TreeFam; TF106230; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000018897; Expressed in oocyte and 104 other tissues.
DR   ExpressionAtlas; Q2KI42; baseline.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR   GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0043248; P:proteasome assembly; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR035295; PSMD11.
DR   InterPro; IPR040780; Rpn6_C_helix.
DR   InterPro; IPR040773; Rpn6_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10678:SF6; PTHR10678:SF6; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF18503; RPN6_C_helix; 1.
DR   Pfam; PF18055; RPN6_N; 1.
DR   SMART; SM00088; PINT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50250; PCI; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   CHAIN           2..422
FT                   /note="26S proteasome non-ATPase regulatory subunit 11"
FT                   /id="PRO_0000244592"
FT   DOMAIN          224..392
FT                   /note="PCI"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O00231"
FT   VAR_SEQ         377
FT                   /note="I -> E (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12140684"
FT                   /id="VSP_044398"
FT   VAR_SEQ         378..422
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12140684"
FT                   /id="VSP_044399"
SQ   SEQUENCE   422 AA;  47464 MW;  CE113054CBEBDB05 CRC64;
     MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT
     GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE
     KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL
     SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD
     SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA
     DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD
     VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK
     LT
 
 
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