PELI3_MOUSE
ID PELI3_MOUSE Reviewed; 445 AA.
AC Q8BXR6; Q8K329;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=E3 ubiquitin-protein ligase pellino homolog 3;
DE Short=Pellino-3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase pellino homolog 3 {ECO:0000305};
GN Name=Peli3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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: E3 ubiquitin ligase catalyzing the covalent attachment of
CC ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-
CC 1 signaling pathways via interaction with the complex containing IRAK
CC kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of
CC IRAK1. Can activate AP1/JUN and ELK1. Not required for NF-kappa-B
CC activation. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TRAF6, IRAK1, MAP3K14 and MAP3K7.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by IRAK1 enhancing its E3 ligase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pellino family. {ECO:0000305}.
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DR EMBL; AK044418; BAC31913.1; -; mRNA.
DR EMBL; BC028931; AAH28931.1; -; mRNA.
DR CCDS; CCDS37888.1; -.
DR RefSeq; NP_766423.3; NM_172835.3.
DR RefSeq; XP_006531808.1; XM_006531745.1.
DR AlphaFoldDB; Q8BXR6; -.
DR SMR; Q8BXR6; -.
DR BioGRID; 232208; 2.
DR STRING; 10090.ENSMUSP00000025834; -.
DR PhosphoSitePlus; Q8BXR6; -.
DR MaxQB; Q8BXR6; -.
DR PaxDb; Q8BXR6; -.
DR PRIDE; Q8BXR6; -.
DR ProteomicsDB; 287825; -.
DR DNASU; 240518; -.
DR GeneID; 240518; -.
DR KEGG; mmu:240518; -.
DR UCSC; uc012bgq.1; mouse.
DR CTD; 246330; -.
DR MGI; MGI:1924963; Peli3.
DR eggNOG; KOG3842; Eukaryota.
DR InParanoid; Q8BXR6; -.
DR OrthoDB; 837213at2759; -.
DR PhylomeDB; Q8BXR6; -.
DR TreeFam; TF314338; -.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-937039; IRAK1 recruits IKK complex.
DR Reactome; R-MMU-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 240518; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Peli3; mouse.
DR PRO; PR:Q8BXR6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BXR6; protein.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:MGI.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IGI:MGI.
DR GO; GO:0045751; P:negative regulation of Toll signaling pathway; IGI:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IMP:MGI.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IMP:MGI.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IMP:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0070428; P:regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; IMP:MGI.
DR InterPro; IPR006800; Pellino_fam.
DR PANTHER; PTHR12098; PTHR12098; 1.
DR Pfam; PF04710; Pellino; 1.
DR PIRSF; PIRSF038886; Pellino; 1.
PE 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..445
FT /note="E3 ubiquitin-protein ligase pellino homolog 3"
FT /id="PRO_0000194177"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N2H9"
FT CONFLICT 353
FT /note="R -> Q (in Ref. 1; BAC31913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 48168 MW; 4C09BE147D5BD941 CRC64;
MVLEGNPDVG SPRTSDLQHP GSQGSCILSC PGEEALAGEE PIKYGELIVL GYNGCLASGD
KGRRRSRLAL SRRPHANGVK PDVMHHISTP LVSKALSNRG QHSISFTLSR SHSVIVEYTH
DSDKDMFQIG RSTENMIDFV VTDTSPGGGA TEGPSAQSTI SRYACRILCD RRPPYTARIY
AAGFDASSNI FLGERAAKWR TPDGLMDGLT TNGVLVMHPA GGFSEDSAPG VWREISVCGN
VYTLRDSRSA QQRGKLVENE SNVLQDGSLI DLCGATLLWR TPAGLLRAPT LKQLEAQRQE
ANAARPQCPV GLSTLAFPSP ARGRTAPDKQ QPWVYVRCGH VHGYHGWGCR RERGPQEREC
PLCRLVGPYV PLWLGQEAGL CLDPGPPSHA FAPCGHVCSE KTARYWAQTP LPHGTHAFHA
ACPFCGAWLT GELGCVRLIF QGPLD
