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Protein

Leucine-rich repeat flightless-interacting protein 1

Gene

Lrrfip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Lrrfip1
Synonyms:Flap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1342770. Lrrfip1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 729728Leucine-rich repeat flightless-interacting protein 1PRO_0000248393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei16 – 161PhosphoserineBy similarity
Modified residuei83 – 831PhosphoserineCombined sources
Modified residuei84 – 841PhosphoserineCombined sources
Modified residuei88 – 881PhosphoserineCombined sources
Modified residuei92 – 921PhosphoserineCombined sources
Modified residuei302 – 3021PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineCombined sources
Modified residuei348 – 3481PhosphoserineCombined sources
Modified residuei538 – 5381PhosphoserineBy similarity
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei614 – 6141PhosphoserineCombined sources
Modified residuei670 – 6701PhosphoserineBy similarity
Isoform 2 (identifier: Q3UZ39-2)
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3UZ39.
MaxQBiQ3UZ39.
PaxDbiQ3UZ39.
PRIDEiQ3UZ39.

PTM databases

iPTMnetiQ3UZ39.
PhosphoSiteiQ3UZ39.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiQ3UZ39.
ExpressionAtlasiQ3UZ39. baseline and differential.
GenevisibleiQ3UZ39. MM.

Interactioni

Subunit structurei

Homodimer. May also form higher oligomers. Interacts with FLII. Interacts with MYD88 (By similarity). Competes with FLII for MyD88-binding, even in the absence of LPS (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
chBcatO424862EBI-2270972,EBI-972394From a different organism.
Grip1Q925T62EBI-2270972,EBI-537752

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201207. 5 interactions.
IntActiQ3UZ39. 6 interactions.
MINTiMINT-4105320.
STRINGi10090.ENSMUSP00000095254.

Structurei

3D structure databases

ProteinModelPortaliQ3UZ39.
SMRiQ3UZ39. Positions 111-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni465 – 567103DNA-bindingBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili94 – 194101By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi530 – 56334Lys-richAdd
BLAST

Domaini

The DNA-binding domain is intrinsically unstructured.By similarity
The coiled coil mediates dimerization.By similarity

Sequence similaritiesi

Belongs to the LRRFIP family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2010. Eukaryota.
ENOG4111H1S. LUCA.
GeneTreeiENSGT00530000063564.
HOGENOMiHOG000294125.
HOVERGENiHBG081935.
InParanoidiQ3UZ39.
OMAiAREEVGN.
OrthoDBiEOG7DNNTX.
PhylomeDBiQ3UZ39.
TreeFamiTF314109.

Family and domain databases

InterProiIPR019139. LRRFIP1/2.
[Graphical view]
PANTHERiPTHR19212. PTHR19212. 1 hit.
PfamiPF09738. DUF2051. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UZ39-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTSPEGAQNK EIDCLSPEAQ RLAEARLAAK RAARAEAREI RMKELERQQK
60 70 80 90 100
EVEERPDKDF AEKGSRNMPS LSAATLASLG GTSSRRGSGD TSISMDTEAS
110 120 130 140 150
IREIKDSLAE VEEKYKKAMV SNAQLDNEKT NFMYQVDTLK DMLLELEEQL
160 170 180 190 200
AESQRQYEEK NKEFEREKHA HSILQFQFAE VKEALRQREE MLEKHGIILN
210 220 230 240 250
SEIATNGETS DTVNDVGYQA PTKITKEELN ALKSAGEGTL GKAKEVEVKK
260 270 280 290 300
EIVEKVGQRE TLQNSEQEQP KPNTGKDCVD RGVSHPGEKA ENQRPAEDSA
310 320 330 340 350
LSPGPLAGAK CEQQVQSQDQ ENTSDLKNSE QIESHKVTNK SDSRASNSPE
360 370 380 390 400
QSSCLEGLDS EVPGPTEDLK TDLGKGSFEP CPDYILGQTA EIDKVTCTDS
410 420 430 440 450
RGTGGNQRED EVQAGDTTVE DQVGTVASGP AKQSKGTENH GESCLKDGLG
460 470 480 490 500
QSSERELTQE VAEPEEAIVQ IPQAGGENTI TKADDAEGRD EKPIQAEAQA
510 520 530 540 550
SPGAPINQSG HQDTTGPGST DAQRTPPHAK ERKKQGKSEQ QAEALDSPQK
560 570 580 590 600
KTKNKKKKNK KKKAATPAET CRDANEELNC QDPDVGDMEE EERLQVTDKK
610 620 630 640 650
QASGSPEQKI RAGSREPVED PQSGSSGKQN KVEEDGPTEG PTDILDQNSP
660 670 680 690 700
QCEDREISPV GEKGPQCDTS QIGSEEGHVT SQHGGQAVEN HNLDNSDLSG
710 720
QLEGFNSESG GQAREEVGNS KSKEDCTMS
Note: No experimental confirmation available.
Length:729
Mass (Da):79,249
Last modified:September 5, 2006 - v2
Checksum:i6BCCA3E8C976BF44
GO
Isoform 2 (identifier: Q3UZ39-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:628
Mass (Da):71,303
Checksum:i66533602CD9CF191
GO
Isoform 3 (identifier: Q3UZ39-3) [UniParc]FASTAAdd to basket

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

Show »
Length:490
Mass (Da):52,383
Checksum:i302E8EA7BD513A13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti122 – 1221N → K in BAE22022 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 239239Missing in isoform 3. 1 PublicationVSP_020266Add
BLAST
Alternative sequencei51 – 511E → EIYQVQKKYYGLDTKWGDIE QWMEDSERYSRRFRRNTSAS DEDERLSVGSRGSLRTNGYD GDYCGSQSLSRRSGRGLSCS NLGLPSSGLASKPLSTQNGS RASMLDESSLYGARRGSACG SRAPSEYGSHLNSSSRASSR ASSARASPV in isoform 2. 1 PublicationVSP_020267
Alternative sequencei104 – 1041I → IKELNELKDQIQDVEGKYMQ GLKEM in isoform 2. 1 PublicationVSP_020268
Alternative sequencei193 – 1931E → EEIRQLQQKQAGFIREISDL QETIEWKDKKIGALERQKEF FDSIRSERDDLREETVKLKE ELK in isoform 2. 1 PublicationVSP_020269
Alternative sequencei240 – 2401L → M in isoform 3. 1 PublicationVSP_020270
Alternative sequencei241 – 394154GKAKE…AEIDK → DVRLKKLIDERECLLEQIKK LKGQLEGRQKNNKLDLLRAE DGILENGTDAHVMDLQRDAN RQISDLKFKLAKSEQEITAL EQNVIRLESQVTRYRSAAEN AEKIEDELKAEKRKLQRELR SALDKTEELEVSNGHLVKRL EKMKANRSALLSQQ in isoform 2. 1 PublicationVSP_020271Add
BLAST
Alternative sequencei395 – 729335Missing in isoform 2. 1 PublicationVSP_020272Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045573 mRNA. Translation: AAC40072.1.
AK134120 mRNA. Translation: BAE22022.1.
AK162191 mRNA. Translation: BAE36781.1.
CCDSiCCDS35662.1. [Q3UZ39-2]
CCDS48320.1. [Q3UZ39-1]
RefSeqiNP_001104781.1. NM_001111311.1. [Q3UZ39-1]
NP_001104782.1. NM_001111312.1.
NP_032541.1. NM_008515.4. [Q3UZ39-2]
XP_011246233.1. XM_011247931.1. [Q3UZ39-3]
UniGeneiMm.45039.

Genome annotation databases

EnsembliENSMUST00000097649; ENSMUSP00000095254; ENSMUSG00000026305. [Q3UZ39-1]
ENSMUST00000097650; ENSMUSP00000095255; ENSMUSG00000026305. [Q3UZ39-2]
GeneIDi16978.
KEGGimmu:16978.
UCSCiuc007bzr.2. mouse. [Q3UZ39-1]
uc007bzs.2. mouse. [Q3UZ39-2]
uc007bzu.2. mouse. [Q3UZ39-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF045573 mRNA. Translation: AAC40072.1.
AK134120 mRNA. Translation: BAE22022.1.
AK162191 mRNA. Translation: BAE36781.1.
CCDSiCCDS35662.1. [Q3UZ39-2]
CCDS48320.1. [Q3UZ39-1]
RefSeqiNP_001104781.1. NM_001111311.1. [Q3UZ39-1]
NP_001104782.1. NM_001111312.1.
NP_032541.1. NM_008515.4. [Q3UZ39-2]
XP_011246233.1. XM_011247931.1. [Q3UZ39-3]
UniGeneiMm.45039.

3D structure databases

ProteinModelPortaliQ3UZ39.
SMRiQ3UZ39. Positions 111-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201207. 5 interactions.
IntActiQ3UZ39. 6 interactions.
MINTiMINT-4105320.
STRINGi10090.ENSMUSP00000095254.

PTM databases

iPTMnetiQ3UZ39.
PhosphoSiteiQ3UZ39.

Proteomic databases

EPDiQ3UZ39.
MaxQBiQ3UZ39.
PaxDbiQ3UZ39.
PRIDEiQ3UZ39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097649; ENSMUSP00000095254; ENSMUSG00000026305. [Q3UZ39-1]
ENSMUST00000097650; ENSMUSP00000095255; ENSMUSG00000026305. [Q3UZ39-2]
GeneIDi16978.
KEGGimmu:16978.
UCSCiuc007bzr.2. mouse. [Q3UZ39-1]
uc007bzs.2. mouse. [Q3UZ39-2]
uc007bzu.2. mouse. [Q3UZ39-3]

Organism-specific databases

CTDi9208.
MGIiMGI:1342770. Lrrfip1.

Phylogenomic databases

eggNOGiKOG2010. Eukaryota.
ENOG4111H1S. LUCA.
GeneTreeiENSGT00530000063564.
HOGENOMiHOG000294125.
HOVERGENiHBG081935.
InParanoidiQ3UZ39.
OMAiAREEVGN.
OrthoDBiEOG7DNNTX.
PhylomeDBiQ3UZ39.
TreeFamiTF314109.

Miscellaneous databases

NextBioi291052.
PROiQ3UZ39.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UZ39.
ExpressionAtlasiQ3UZ39. baseline and differential.
GenevisibleiQ3UZ39. MM.

Family and domain databases

InterProiIPR019139. LRRFIP1/2.
[Graphical view]
PANTHERiPTHR19212. PTHR19212. 1 hit.
PfamiPF09738. DUF2051. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-84; SER-88; SER-92; SER-346; SER-348; SER-547 AND SER-614, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-97 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiLRRF1_MOUSE
AccessioniPrimary (citable) accession number: Q3UZ39
Secondary accession number(s): O70323, Q3TS94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: April 13, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.