ID   PP1RB_MACMU             Reviewed;         126 AA.
AC   Q5TM51;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=E3 ubiquitin-protein ligase PPP1R11;
DE            EC=2.3.2.27;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 11;
GN   Name=PPP1R11;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(2004).
CC   -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2
CC       at 'Lys-754' leading to its degradation by the proteasome. Plays a role
CC       in regulating inflammatory cytokine release and gram-positive bacterial
CC       clearance by functioning, in part, through the ubiquitination and
CC       degradation of TLR2. Inhibitor of protein phosphatase 1.
CC       {ECO:0000250|UniProtKB:O60927}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:O60927};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with TLR2 and UBE2D2.
CC       {ECO:0000250|UniProtKB:Q8K1L5}.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O60927}.
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DR   EMBL; AB128049; BAD69775.1; -; Genomic_DNA.
DR   RefSeq; NP_001040601.1; NM_001047136.1.
DR   AlphaFoldDB; Q5TM51; -.
DR   STRING; 9544.ENSMMUP00000015891; -.
DR   Ensembl; ENSMMUT00000016969; ENSMMUP00000015892; ENSMMUG00000012122.
DR   GeneID; 712286; -.
DR   KEGG; mcc:712286; -.
DR   CTD; 6992; -.
DR   VEuPathDB; HostDB:ENSMMUG00000012122; -.
DR   VGNC; VGNC:82209; PPP1R11.
DR   eggNOG; KOG4102; Eukaryota.
DR   GeneTree; ENSGT00390000001153; -.
DR   HOGENOM; CLU_098333_6_2_1; -.
DR   InParanoid; Q5TM51; -.
DR   OMA; CILGHSR; -.
DR   OrthoDB; 1599272at2759; -.
DR   TreeFam; TF352541; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000006718; Chromosome 4.
DR   Bgee; ENSMMUG00000012122; Expressed in spermatid and 22 other tissues.
DR   ExpressionAtlas; Q5TM51; baseline.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0001818; P:negative regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PTHR20835; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   3: Inferred from homology;
KW   Acetylation; Phosphoprotein; Protein phosphatase inhibitor;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   CHAIN           2..126
FT                   /note="E3 ubiquitin-protein ligase PPP1R11"
FT                   /id="PRO_0000239620"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..62
FT                   /note="Atypical RING finger domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   REGION          70..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..94
FT                   /note="Atypical RING finger domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   COMPBIAS        9..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..126
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
SQ   SEQUENCE   126 AA;  13953 MW;  D6788A5AAC073549 CRC64;
     MAEAGAGLSE TVTETTVTVT TEPENRSLTI KLRKRKPEKK VEWTSDTVDN EHMGRRSSKC
     CCIYEKPRAF GESSTESDEE EEEGCGHTHC VRGHRKGRRR ATLGPTPTTP PQPPDPSQPP
     PGPMQH