ID   LRRF2_BOVIN             Reviewed;         400 AA.
AC   Q2T9W6;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE            Short=LRR FLII-interacting protein 2;
GN   Name=LRRFIP2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Following LPS-stimulation,
CC       the interaction with MYD88 is rapidly enhanced; the complex gradually
CC       dissociates to basal levels after 6 hours of stimulation (By
CC       similarity). Interaction with MYD88 is regulated by LPS-induced
CC       phosphorylation. In the presence of LPS, competes with FLII for MYD88-
CC       binding (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR   EMBL; BC111234; AAI11235.1; -; mRNA.
DR   RefSeq; NP_001033159.1; NM_001038070.2.
DR   AlphaFoldDB; Q2T9W6; -.
DR   SMR; Q2T9W6; -.
DR   PRIDE; Q2T9W6; -.
DR   GeneID; 510368; -.
DR   KEGG; bta:510368; -.
DR   CTD; 9209; -.
DR   InParanoid; Q2T9W6; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR019139; LRRFIP1/2.
DR   PANTHER; PTHR19212; PTHR19212; 3.
DR   Pfam; PF09738; LRRFIP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein; Reference proteome; Wnt signaling pathway.
FT   CHAIN           1..400
FT                   /note="Leucine-rich repeat flightless-interacting protein
FT                   2"
FT                   /id="PRO_0000245245"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..71
FT                   /evidence="ECO:0000255"
FT   COILED          106..202
FT                   /evidence="ECO:0000255"
FT   COILED          245..393
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT   MOD_RES         99
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WK0"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q91WK0"
SQ   SEQUENCE   400 AA;  45494 MW;  7A601EA5211843C9 CRC64;
     MGTPGSGRKR TPVKDRFSAE DEALSNIDRE AEARLAAKRA ARAEARDIRM RELERQQKEL
     DEKSDKQYAE NYTRPSSRNS ASATTPLSGN SSRRVSGDTS SLIDPDTSLS ELRESLSEVE
     EKYKKAMVSN AQLDNEKNNL IYQVDTLKDV IEEQEEQMAE FYRENEEKSK ELERQKHMCS
     VLQHKMDELK EGLRQRDELI EKHGLVIIPD GTPNGDVHQE PAVGAITVVS QEAAQVLESA
     GEGPLDVRLR KLAGEKEELL SQIRKLKLQL EEERQKCSGR DGTAGDLAEL QNGSDLQLIE
     MQRDANRQIS EYKFKLSKAE QDITTLEQSI SRLEGQVLRY RTAAENAEKV EDELKAEKRK
     LQRELRTALD KIEEMEMTNS HLAKRLEKMK ANRTALLAQQ