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Q3UZ39 (LRRF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich repeat flightless-interacting protein 1
Short name=LRR FLII-interacting protein 1
Alternative name(s):
FLI-LRR-associated protein 1
Short name=Flap-1
H186 FLAP
Gene names
Name:Lrrfip1
Synonyms:Flap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length729 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'-AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. May control smooth muscle cells proliferation following artery injury through PDGFA repression. May also bind double-stranded RNA By similarity. Positively regulates Toll-like receptor (TLR) signaling in response to agonist probably by competing with the negative FLII regulator for MYD88-binding By similarity.

Subunit structure

Interacts with FLII. Interacts with MYD88 By similarity. Competes with FLII for MyD88-binding, even in the absence of LPS By similarity. Ref.1

Subcellular location

Nucleus. Cytoplasm By similarity.

Tissue specificity

Ubiquitously expressed. Ref.1

Sequence similarities

Belongs to the LRRFIP family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

chBcatO424862EBI-2270972,EBI-972394From a different organism.
Grip1Q925T62EBI-2270972,EBI-537752

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UZ39-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q3UZ39-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-51: E → EIYQVQKKYY...RASSARASPV
     104-104: I → IKELNELKDQIQDVEGKYMQGLKEM
     193-193: E → EEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELK
     241-394: GKAKEVEVKK...ILGQTAEIDK → DVRLKKLIDE...ANRSALLSQQ
     395-729: Missing.
Isoform 3 (identifier: Q3UZ39-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-239: Missing.
     240-240: L → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 729728Leucine-rich repeat flightless-interacting protein 1
PRO_0000248393

Regions

Region465 – 567103DNA-binding By similarity
Coiled coil94 – 194101 Potential
Compositional bias530 – 56334Lys-rich

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue161Phosphoserine By similarity
Modified residue831Phosphoserine By similarity
Modified residue881Phosphoserine Ref.4
Modified residue911Phosphothreonine Ref.3
Modified residue3021Phosphoserine Ref.4
Modified residue5381Phosphoserine By similarity

Natural variations

Alternative sequence1 – 239239Missing in isoform 3.
VSP_020266
Alternative sequence511E → EIYQVQKKYYGLDTKWGDIE QWMEDSERYSRRFRRNTSAS DEDERLSVGSRGSLRTNGYD GDYCGSQSLSRRSGRGLSCS NLGLPSSGLASKPLSTQNGS RASMLDESSLYGARRGSACG SRAPSEYGSHLNSSSRASSR ASSARASPV in isoform 2.
VSP_020267
Alternative sequence1041I → IKELNELKDQIQDVEGKYMQ GLKEM in isoform 2.
VSP_020268
Alternative sequence1931E → EEIRQLQQKQAGFIREISDL QETIEWKDKKIGALERQKEF FDSIRSERDDLREETVKLKE ELK in isoform 2.
VSP_020269
Alternative sequence2401L → M in isoform 3.
VSP_020270
Alternative sequence241 – 394154GKAKE…AEIDK → DVRLKKLIDERECLLEQIKK LKGQLEGRQKNNKLDLLRAE DGILENGTDAHVMDLQRDAN RQISDLKFKLAKSEQEITAL EQNVIRLESQVTRYRSAAEN AEKIEDELKAEKRKLQRELR SALDKTEELEVSNGHLVKRL EKMKANRSALLSQQ in isoform 2.
VSP_020271
Alternative sequence395 – 729335Missing in isoform 2.
VSP_020272

Experimental info

Sequence conflict1221N → K in BAE22022. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 6BCCA3E8C976BF44

FASTA72979,249
        10         20         30         40         50         60 
MTSPEGAQNK EIDCLSPEAQ RLAEARLAAK RAARAEAREI RMKELERQQK EVEERPDKDF 

        70         80         90        100        110        120 
AEKGSRNMPS LSAATLASLG GTSSRRGSGD TSISMDTEAS IREIKDSLAE VEEKYKKAMV 

       130        140        150        160        170        180 
SNAQLDNEKT NFMYQVDTLK DMLLELEEQL AESQRQYEEK NKEFEREKHA HSILQFQFAE 

       190        200        210        220        230        240 
VKEALRQREE MLEKHGIILN SEIATNGETS DTVNDVGYQA PTKITKEELN ALKSAGEGTL 

       250        260        270        280        290        300 
GKAKEVEVKK EIVEKVGQRE TLQNSEQEQP KPNTGKDCVD RGVSHPGEKA ENQRPAEDSA 

       310        320        330        340        350        360 
LSPGPLAGAK CEQQVQSQDQ ENTSDLKNSE QIESHKVTNK SDSRASNSPE QSSCLEGLDS 

       370        380        390        400        410        420 
EVPGPTEDLK TDLGKGSFEP CPDYILGQTA EIDKVTCTDS RGTGGNQRED EVQAGDTTVE 

       430        440        450        460        470        480 
DQVGTVASGP AKQSKGTENH GESCLKDGLG QSSERELTQE VAEPEEAIVQ IPQAGGENTI 

       490        500        510        520        530        540 
TKADDAEGRD EKPIQAEAQA SPGAPINQSG HQDTTGPGST DAQRTPPHAK ERKKQGKSEQ 

       550        560        570        580        590        600 
QAEALDSPQK KTKNKKKKNK KKKAATPAET CRDANEELNC QDPDVGDMEE EERLQVTDKK 

       610        620        630        640        650        660 
QASGSPEQKI RAGSREPVED PQSGSSGKQN KVEEDGPTEG PTDILDQNSP QCEDREISPV 

       670        680        690        700        710        720 
GEKGPQCDTS QIGSEEGHVT SQHGGQAVEN HNLDNSDLSG QLEGFNSESG GQAREEVGNS 


KSKEDCTMS

« Hide

Isoform 2 [UniParc].

Checksum: 66533602CD9CF191
Show »

FASTA62871,303
Isoform 3 [UniParc].

Checksum: 302E8EA7BD513A13
Show »

FASTA49052,383

References

« Hide 'large scale' references
[1]"Identification of the binding partners for flightless I, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies."
Liu Y.-T., Yin H.L.
J. Biol. Chem. 273:7920-7927(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH FLII, TISSUE SPECIFICITY.
Tissue: Skeletal muscle.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
Tissue: Egg and Thymus.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, MASS SPECTROMETRY.
Tissue: Liver.
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88 AND SER-302, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF045573 mRNA. Translation: AAC40072.1.
AK134120 mRNA. Translation: BAE22022.1.
AK162191 mRNA. Translation: BAE36781.1.
IPIIPI00117277.
IPI00654388.
IPI00785324.
RefSeqNP_001104781.1. NM_001111311.1.
NP_001104782.1. NM_001111312.1.
NP_032541.1. NM_008515.4.
UniGeneMm.395990.
Mm.45039.

3D structure databases

ProteinModelPortalQ3UZ39.
SMRQ3UZ39. Positions 111-193.
ModBaseSearch...

Protein-protein interaction databases

IntActQ3UZ39. 3 interactions.
MINTMINT-4105320.

PTM databases

PhosphoSiteQ3UZ39.

Proteomic databases

PaxDbQ3UZ39.
PRIDEQ3UZ39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000097649; ENSMUSP00000095254; ENSMUSG00000026305.
ENSMUST00000097650; ENSMUSP00000095255; ENSMUSG00000026305.
GeneID16978.
KEGGmmu:16978.
UCSCuc007bzr.2. mouse.
uc007bzs.2. mouse.
uc007bzu.2. mouse.

Organism-specific databases

CTD9208.
MGIMGI:1342770. Lrrfip1.

Phylogenomic databases

eggNOGNOG296572.
GeneTreeENSGT00530000063564.
HOGENOMHOG000294125.
HOVERGENHBG081935.
InParanoidQ3UZ39.
OMAAREEVGN.
OrthoDBEOG4J9N06.

Gene expression databases

ArrayExpressQ3UZ39.
BgeeQ3UZ39.
GenevestigatorQ3UZ39.
GermOnlineENSMUSG00000026305. Mus musculus.

Family and domain databases

InterProIPR019139. Leu-rich_rep_flightless-int_pr.
[Graphical view]
PANTHERPTHR19212. PTHR19212. 1 hit.
PfamPF09738. DUF2051. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio291052.
SOURCESearch...

Entry information

Entry nameLRRF1_MOUSE
AccessionPrimary (citable) accession number: Q3UZ39
Secondary accession number(s): O70323, Q3TS94
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 29, 2013
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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