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PP1RB_XENLA
ID   PP1RB_XENLA             Reviewed;         119 AA.
AC   Q6DDH0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2
CC       at 'Lys-754' leading to its degradation by the proteasome. Inhibitor of
CC       protein phosphatase 1. {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.
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DR   EMBL; BC077596; AAH77596.1; -; mRNA.
DR   RefSeq; NP_001086878.1; NM_001093409.1.
DR   AlphaFoldDB; Q6DDH0; -.
DR   DNASU; 446713; -.
DR   GeneID; 446713; -.
DR   KEGG; xla:446713; -.
DR   CTD; 446713; -.
DR   Xenbase; XB-GENE-999523; ppp1r11.L.
DR   OMA; MKSKCCC; -.
DR   OrthoDB; 1599272at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 446713; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
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; IEA:InterPro.
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   Protein phosphatase inhibitor; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..119
FT                   /note="E3 ubiquitin-protein ligase PPP1R11"
FT                   /id="PRO_0000239625"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          55..65
FT                   /note="Atypical RING finger domain 1"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   REGION          87..96
FT                   /note="Atypical RING finger domain 2"
FT                   /evidence="ECO:0000250|UniProtKB:O60927"
FT   REGION          96..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   119 AA;  13032 MW;  421F7B64B6F42BC6 CRC64;
     MAETSGPTAA GGSTSSTVTT ESETQPEHRS LTLKLRKRKP DKKVEWTCDT VDNENLGRRS
     SKCCCIYEKP RPFGESSSES EDDDDCCESA HCIRGHKKAT SGSKETPSSH HDKTGSMQH
 
 
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