LRRF2_RAT
ID LRRF2_RAT Reviewed; 437 AA.
AC Q4V7E8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE Short=LRR FLII-interacting protein 2;
GN Name=Lrrfip2;
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 MRNA].
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-125 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May function as activator of the canonical Wnt signaling
CC pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
CC Positively regulates Toll-like receptor (TLR) signaling in response to
CC agonist probably by competing with the negative FLII regulator for
CC MYD88-binding (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DVL3 and FLII (By similarity). Weakly interacts
CC with MYD88 in resting cells. Following LPS-stimulation, the interaction
CC with MYD88 is rapidly enhanced; the complex gradually dissociates to
CC basal levels after 6 hours of stimulation. Interaction with MYD88 is
CC regulated by LPS-induced phosphorylation. In the presence of LPS,
CC competes with FLII for MYD88-binding (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR EMBL; BC097955; AAH97955.1; -; mRNA.
DR RefSeq; NP_001019932.1; NM_001024761.1.
DR AlphaFoldDB; Q4V7E8; -.
DR SMR; Q4V7E8; -.
DR BioGRID; 256809; 2.
DR IntAct; Q4V7E8; 1.
DR STRING; 10116.ENSRNOP00000052912; -.
DR iPTMnet; Q4V7E8; -.
DR PhosphoSitePlus; Q4V7E8; -.
DR jPOST; Q4V7E8; -.
DR PaxDb; Q4V7E8; -.
DR PRIDE; Q4V7E8; -.
DR Ensembl; ENSRNOT00000056060; ENSRNOP00000052912; ENSRNOG00000021047.
DR GeneID; 301035; -.
DR KEGG; rno:301035; -.
DR UCSC; RGD:1306234; rat.
DR CTD; 9209; -.
DR RGD; 1306234; Lrrfip2.
DR eggNOG; KOG2010; Eukaryota.
DR GeneTree; ENSGT00530000063564; -.
DR HOGENOM; CLU_018871_0_0_1; -.
DR InParanoid; Q4V7E8; -.
DR OMA; CIRIERD; -.
DR OrthoDB; 1434475at2759; -.
DR PhylomeDB; Q4V7E8; -.
DR TreeFam; TF314109; -.
DR PRO; PR:Q4V7E8; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000021047; Expressed in testis and 19 other tissues.
DR Genevisible; Q4V7E8; RN.
DR GO; GO:0030275; F:LRR domain binding; ISO:RGD.
DR GO; GO:0035660; P:MyD88-dependent toll-like receptor 4 signaling pathway; ISO:RGD.
DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR019139; LRRFIP1/2.
DR PANTHER; PTHR19212; PTHR19212; 4.
DR Pfam; PF09738; LRRFIP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT CHAIN 1..437
FT /note="Leucine-rich repeat flightless-interacting protein
FT 2"
FT /id="PRO_0000245248"
FT REGION 33..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000255"
FT COILED 143..239
FT /evidence="ECO:0000255"
FT COILED 282..430
FT /evidence="ECO:0000255"
FT COMPBIAS 33..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91WK0"
SQ SEQUENCE 437 AA; 49773 MW; 5D75A735B51CD4E2 CRC64;
MGTPGSGRKR TPVKDRFSAE DEALSNIARE AEARLAAKRA ARAEARDIRM RELERQQRES
SSKDITGTHW SRASTPKRRD MMYDSIKDRS SRVSSLLDEK SDKQYAENYT RPSSRNSASA
TTPLSGNSSR RGSGDTSSLI DPDTSLSELR ESLSEVEEKY KKAMVSNAQL DNEKNNLIYQ
VDTLKDVIEE QEEQMAEFYR ENEEKSKELE RQKHMCSVLQ HKMDELKEGL RQRDELIEKH
GLVIIPESTP NGDVNHEPVV GAITAVSQEA AQVLESAGEG PLDVRLRKLA EEKDELLSQI
RKLKLQLEEE RQKCSRNDGM SGDLAGLQNG SDLQFIEMQR DANRQISEYK FKLSKAEQDI
ATLEQSISRL EGQVLRYKTA AENAEKIEDE LKAEKRKLQR ELRTAQDKIE EMEMTNSHLA
KRLEKMKANR TALLAQQ
