LRRF2_MOUSE
ID LRRF2_MOUSE Reviewed; 415 AA.
AC Q91WK0; Q8BVD1; Q9CU89;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE Short=LRR FLII-interacting protein 2;
GN Name=Lrrfip2;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Intestine, and Olfactory bulb;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-111; THR-114; SER-115
RP AND SER-116, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WK0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WK0-2; Sequence=VSP_019678;
CC -!- SIMILARITY: Belongs to the LRRFIP family. {ECO:0000305}.
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DR EMBL; AK017217; BAB30640.1; -; mRNA.
DR EMBL; AK078881; BAC37441.1; -; mRNA.
DR EMBL; BC014761; AAH14761.1; -; mRNA.
DR CCDS; CCDS23583.1; -. [Q91WK0-2]
DR CCDS; CCDS52941.1; -. [Q91WK0-1]
DR RefSeq; NP_001158310.1; NM_001164838.1.
DR RefSeq; NP_082018.1; NM_027742.3.
DR AlphaFoldDB; Q91WK0; -.
DR SMR; Q91WK0; -.
DR BioGRID; 214592; 11.
DR IntAct; Q91WK0; 4.
DR MINT; Q91WK0; -.
DR STRING; 10090.ENSMUSP00000035078; -.
DR iPTMnet; Q91WK0; -.
DR PhosphoSitePlus; Q91WK0; -.
DR EPD; Q91WK0; -.
DR jPOST; Q91WK0; -.
DR MaxQB; Q91WK0; -.
DR PaxDb; Q91WK0; -.
DR PeptideAtlas; Q91WK0; -.
DR PRIDE; Q91WK0; -.
DR ProteomicsDB; 292369; -. [Q91WK0-1]
DR ProteomicsDB; 292370; -. [Q91WK0-2]
DR GeneID; 71268; -.
DR KEGG; mmu:71268; -.
DR UCSC; uc009rvm.2; mouse. [Q91WK0-2]
DR CTD; 9209; -.
DR MGI; MGI:1918518; Lrrfip2.
DR eggNOG; KOG2010; Eukaryota.
DR InParanoid; Q91WK0; -.
DR OrthoDB; 1434475at2759; -.
DR PhylomeDB; Q91WK0; -.
DR BioGRID-ORCS; 71268; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Lrrfip2; mouse.
DR PRO; PR:Q91WK0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91WK0; protein.
DR GO; GO:0030275; F:LRR domain binding; ISO:MGI.
DR GO; GO:0035660; P:MyD88-dependent toll-like receptor 4 signaling pathway; IDA:MGI.
DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; IDA:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Leucine-rich repeat flightless-interacting protein
FT 2"
FT /id="PRO_0000245247"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000255"
FT COILED 121..217
FT /evidence="ECO:0000255"
FT COILED 260..408
FT /evidence="ECO:0000255"
FT COMPBIAS 69..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y608"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 60..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019678"
FT CONFLICT 105
FT /note="Q -> N (in Ref. 1; BAC37441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47148 MW; 9A877ACA5A7264B8 CRC64;
MGTPGSGRKR TPVKDRFSAE DEALSNIARE AEARLAAKRA ARAEARDIRM RELERQQREG
VEDTLSLRSL GSHRLDEKSD KQYAENYTRP SSRNSASATT PLSGQSSRRG SGDTSSLIDP
DTSLSELRES LSEVEEKYKK AMVSNAQLDN EKNNLIYQVD TLKDVIEEQE EQMAEFYREN
EEKSKELERQ KHMCSVLQHK MDELKEGLRQ RDELIEKHGL VIIPDSTPNG DVHHEPVVGA
ITAVSQEAAQ VLESAGEGPL DVRLRKLAGE KDELLSQIRK LKLQLEEERQ KCSRNDGMSG
DLAGLQNGSD LQFIEMQRDA NRQISEYKFK LSKAEQDIAT LEQSISRLEG QVLRYKTAAE
NAEKIEDELK AERRKLQREL RTAQDKIEEM EMTNSHLAKR LEKMKANRTA LLAQQ
