PP1RB_RAT
ID PP1RB_RAT Reviewed; 127 AA.
AC Q6MFY6; Q6AXZ8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 2).
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6MFY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6MFY6-2; Sequence=VSP_019247;
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O60927}.
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DR EMBL; BX883051; CAE84061.1; -; Genomic_DNA.
DR EMBL; BC079252; AAH79252.1; -; mRNA.
DR RefSeq; NP_997707.2; NM_212542.3. [Q6MFY6-1]
DR AlphaFoldDB; Q6MFY6; -.
DR STRING; 10116.ENSRNOP00000001013; -.
DR iPTMnet; Q6MFY6; -.
DR PhosphoSitePlus; Q6MFY6; -.
DR PaxDb; Q6MFY6; -.
DR PRIDE; Q6MFY6; -.
DR GeneID; 294207; -.
DR KEGG; rno:294207; -.
DR UCSC; RGD:1303163; rat. [Q6MFY6-1]
DR CTD; 6992; -.
DR RGD; 1303163; Ppp1r11.
DR VEuPathDB; HostDB:ENSRNOG00000000780; -.
DR eggNOG; KOG4102; Eukaryota.
DR HOGENOM; CLU_098333_6_2_1; -.
DR InParanoid; Q6MFY6; -.
DR OMA; CILGHSR; -.
DR OrthoDB; 1599272at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6MFY6; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000780; Expressed in testis and 20 other tissues.
DR Genevisible; Q6MFY6; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Phosphoprotein;
KW Protein phosphatase inhibitor; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT CHAIN 2..127
FT /note="E3 ubiquitin-protein ligase PPP1R11"
FT /id="PRO_0000239623"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..63
FT /note="Atypical RING finger domain 1"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT REGION 70..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..95
FT /note="Atypical RING finger domain 2"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..127
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 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 76
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60927"
FT VAR_SEQ 25
FT /note="E -> VRNAGRGA (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_019247"
SQ SEQUENCE 127 AA; 13936 MW; AB29CF553C6158A6 CRC64;
MAEAGAGGLS ETVTETTVTV TTEPENRSLT IKLRKRKPEK KVEWSSDTVD NEHMGRRSSK
CCCIYEKPRA FGESSTESDE DEEEGCGHTH CVRGHRKGRR PTTPGPTPTT PPQPPDPSQP
PPGPMQH
