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Protein

Protein flightless-1 homolog

Gene

Flii

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

Functioni

May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling (By similarity). Essential for early embryonic development. May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation.By similarity4 Publications

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin filament severing Source: MGI
  • multicellular organism development Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein flightless-1 homolog
Gene namesi
Name:Flii
Synonyms:Fli1, Fliih
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1342286. Flii.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: UniProtKB
  • cytoplasm Source: MGI
  • focal adhesion Source: UniProtKB-SubCell
  • microtubule organizing center Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Disruption phenotypei

Increases the percentage of focal complex positive cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12711271Protein flightless-1 homologPRO_0000218751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Modified residuei406 – 4061PhosphoserineBy similarity
Modified residuei436 – 4361Phosphoserine; by SGK3By similarity
Modified residuei860 – 8601PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JJ28.
MaxQBiQ9JJ28.
PaxDbiQ9JJ28.
PeptideAtlasiQ9JJ28.
PRIDEiQ9JJ28.

PTM databases

iPTMnetiQ9JJ28.
PhosphoSiteiQ9JJ28.

Expressioni

Tissue specificityi

Expressed in blastocyst.1 Publication

Inductioni

Up-regulated in response to wounding.1 Publication

Gene expression databases

BgeeiQ9JJ28.
CleanExiMM_FLI1.
MM_FLII.
GenevisibleiQ9JJ28. MM.

Interactioni

Subunit structurei

Interacts with actin, ACTL6A, NCOA2 and MYD88 (By similarity). Interacts with LRRFIP1 and LRRFIP2. Upon LPS stimulation, LRRFIP2 competes for MYD88-binding. LRRFIP1 constitutively blocks the interaction with MyD88, even in the absence of LPS (By similarity). Interacts with the nuclear receptors ESR1 and THRB (By similarity). Interacts with CARM1. Interacts with SGK3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Camk2dQ6PHZ25EBI-7996161,EBI-2308458

GO - Molecular functioni

Protein-protein interaction databases

BioGridi199703. 4 interactions.
DIPiDIP-47641N.
IntActiQ9JJ28. 5 interactions.
MINTiMINT-4095146.
STRINGi10090.ENSMUSP00000002889.

Structurei

3D structure databases

ProteinModelPortaliQ9JJ28.
SMRiQ9JJ28. Positions 7-416, 485-1267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati7 – 3226LRR 1Add
BLAST
Repeati33 – 5523LRR 2Add
BLAST
Repeati56 – 7823LRR 3Add
BLAST
Repeati80 – 10324LRR 4Add
BLAST
Repeati104 – 12623LRR 5Add
BLAST
Repeati127 – 14923LRR 6Add
BLAST
Repeati150 – 17324LRR 7Add
BLAST
Repeati175 – 19622LRR 8Add
BLAST
Repeati197 – 22226LRR 9Add
BLAST
Repeati223 – 24523LRR 10Add
BLAST
Repeati247 – 26822LRR 11Add
BLAST
Repeati269 – 29123LRR 12Add
BLAST
Repeati293 – 31624LRR 13Add
BLAST
Repeati318 – 33922LRR 14Add
BLAST
Repeati340 – 36324LRR 15Add
BLAST
Repeati501 – 55959Gelsolin-like 1Add
BLAST
Repeati640 – 67031Gelsolin-like 2Add
BLAST
Repeati755 – 79844Gelsolin-like 3Add
BLAST
Repeati1070 – 111748Gelsolin-like 4Add
BLAST
Repeati1178 – 122043Gelsolin-like 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 427427Interaction with LRRFIP1 and LRRFIP2By similarityAdd
BLAST
Regioni495 – 827333Interaction with ACTL6ABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi892 – 98089Glu-richAdd
BLAST

Sequence similaritiesi

Contains 5 gelsolin-like repeats.Curated
Contains 15 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG0444. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000016110.
HOVERGENiHBG051627.
InParanoidiQ9JJ28.
OMAiQMKADLT.
OrthoDBiEOG7C2R0C.
PhylomeDBiQ9JJ28.
TreeFamiTF313468.

Family and domain databases

Gene3Di3.40.20.10. 7 hits.
3.80.10.10. 2 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029919. FliI.
IPR007123. Gelsolin-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF42. PTHR11977:SF42. 2 hits.
PfamiPF00626. Gelsolin. 4 hits.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00369. LRR_TYP. 9 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF82754. SSF82754. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJ28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE
60 70 80 90 100
ELAALQKLEH LSVSHNHLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI
110 120 130 140 150
FKLDDLSVLD LSHNQLTECP RELENAKNML VLNLSHNGID SIPNQLFINL
160 170 180 190 200
TDLLYLDLSE NRLESLPPQM RRLVHLQTLV LNGNPLLHAQ LRQLPAMMAL
210 220 230 240 250
QTLHLRNTQR TQSNLPTSLE GLSNLSDVDL SCNDLTRVPE CLYTLPSLRR
260 270 280 290 300
LNLSSNQIAE LSLCIDQWVH LETLNLSRNQ LTSLPSAICK LTKLKKLYLN
310 320 330 340 350
SNKLDFDGLP SGIGKLTSLE EFMAANNNLE LIPESLCRCP KLKKLVLNKN
360 370 380 390 400
RLVTLPEAIH FLTEIQVLDV RENPSLVMPP KPADRTAEWY NIDFSLQNQL
410 420 430 440 450
RLAGASPATV AAAAAVGSGS KDPLARKMRL RRRKDSAQDV QAKQVLKGMS
460 470 480 490 500
DVAQEKNKNQ EESIDARAPG GKVRRWDQGL EKPRLDYSEF FTEDVGQLPG
510 520 530 540 550
LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS LNWEIYYWIG
560 570 580 590 600
GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY
610 620 630 640 650
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGS SLDPRFVFLL
660 670 680 690 700
DQGLDIYVWR GAQATLSNTT KARLFAEKIN KNERKGKAEI TLLVQGQEPP
710 720 730 740 750
GFWDVLGGEP SEIKNHVPDD FWPPQPKLYK VGLGLGYLEL PQINYKLSVE
760 770 780 790 800
HKKRPKVELM PGMRLLQSLL DTRCVYILDC WSDVFIWLGR KSPRLVRAAA
810 820 830 840 850
LKLGQELCGM LHRPRHTVVS RSLEGTEAQV FKAKFKNWDD VLTVDYTRNA
860 870 880 890 900
EAVLQGQGLS GKVKRDTEKT DQMKADLTAL FLPRQPPMPL AEAEQLMEEW
910 920 930 940 950
NEDLDGMEGF VLEGRKFTRL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE
960 970 980 990 1000
KTEDKEGKAS AEAREGEEAA AEAEEKQPEE DFQCIVYFWQ GREASNMGWL
1010 1020 1030 1040 1050
TFTFSLQKKF ESLFPGKLEV VRMTQQQENP KFLSHFKRKF IIHRGKRKVT
1060 1070 1080 1090 1100
QGTLQPTLYQ IRTNGSALCT RCIQINTDSS LLNSEFCFIL KVPFESEDNQ
1110 1120 1130 1140 1150
GIVYAWVGRA SDPDEAKLAE DILNTMFDAS YSKQVINEGE EPENFFWVGI
1160 1170 1180 1190 1200
GAQKPYDDDA EYMKHTRLFR CSNEKGYFAV TEKCSDFCQD DLADDDIMLL
1210 1220 1230 1240 1250
DNGQEVYMWV GTQTSQVEIK LSLKACQVYI QHTRSKEHER PRRLRLVRKG
1260 1270
NEQRAFTRCF HAWSTFRQAP A
Length:1,271
Mass (Da):144,803
Last modified:October 1, 2000 - v1
Checksum:iA9642B10FEBF8769
GO

Sequence cautioni

The sequence AAH32282.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti849 – 8491N → D in AAL36557 (PubMed:10902907).Curated
Sequence conflicti1057 – 10571T → I in AAH32282 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142329 Genomic DNA. Translation: AAF78453.1.
AF287264 mRNA. Translation: AAL36557.1.
AL596215 Genomic DNA. Translation: CAI35270.1.
BC027744 mRNA. Translation: AAH27744.1.
BC032282 mRNA. Translation: AAH32282.1. Different initiation.
CCDSiCCDS24795.1.
RefSeqiNP_071292.1. NM_022009.2.
UniGeneiMm.339755.

Genome annotation databases

EnsembliENSMUST00000002889; ENSMUSP00000002889; ENSMUSG00000002812.
GeneIDi14248.
KEGGimmu:14248.
UCSCiuc007jgh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF142329 Genomic DNA. Translation: AAF78453.1.
AF287264 mRNA. Translation: AAL36557.1.
AL596215 Genomic DNA. Translation: CAI35270.1.
BC027744 mRNA. Translation: AAH27744.1.
BC032282 mRNA. Translation: AAH32282.1. Different initiation.
CCDSiCCDS24795.1.
RefSeqiNP_071292.1. NM_022009.2.
UniGeneiMm.339755.

3D structure databases

ProteinModelPortaliQ9JJ28.
SMRiQ9JJ28. Positions 7-416, 485-1267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199703. 4 interactions.
DIPiDIP-47641N.
IntActiQ9JJ28. 5 interactions.
MINTiMINT-4095146.
STRINGi10090.ENSMUSP00000002889.

PTM databases

iPTMnetiQ9JJ28.
PhosphoSiteiQ9JJ28.

Proteomic databases

EPDiQ9JJ28.
MaxQBiQ9JJ28.
PaxDbiQ9JJ28.
PeptideAtlasiQ9JJ28.
PRIDEiQ9JJ28.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002889; ENSMUSP00000002889; ENSMUSG00000002812.
GeneIDi14248.
KEGGimmu:14248.
UCSCiuc007jgh.2. mouse.

Organism-specific databases

CTDi2314.
MGIiMGI:1342286. Flii.

Phylogenomic databases

eggNOGiKOG0444. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000016110.
HOVERGENiHBG051627.
InParanoidiQ9JJ28.
OMAiQMKADLT.
OrthoDBiEOG7C2R0C.
PhylomeDBiQ9JJ28.
TreeFamiTF313468.

Miscellaneous databases

ChiTaRSiFlii. mouse.
PROiQ9JJ28.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJ28.
CleanExiMM_FLI1.
MM_FLII.
GenevisibleiQ9JJ28. MM.

Family and domain databases

Gene3Di3.40.20.10. 7 hits.
3.80.10.10. 2 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR029919. FliI.
IPR007123. Gelsolin-like_dom.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR007122. Villin/Gelsolin.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF42. PTHR11977:SF42. 2 hits.
PfamiPF00626. Gelsolin. 4 hits.
PF12799. LRR_4. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00369. LRR_TYP. 9 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF82754. SSF82754. 1 hit.
PROSITEiPS51450. LRR. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fliih, the murine homologue of the Drosophila melanogaster flightless I gene: nucleotide sequence, chromosomal mapping and overlap with Llglh."
    Campbell H.D., Fountain S., Young I.G., Weitz S., Lichter P., Hoheisel J.D.
    DNA Seq. 11:29-40(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: BALB/cJ.
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney and Liver.
  4. "The flightless I protein localizes to actin-based structures during embryonic development."
    Davy D.A., Ball E.E., Matthaei K.I., Campbell H.D., Crouch M.F.
    Immunol. Cell Biol. 78:423-429(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. Cited for: FUNCTION.
  6. "Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity."
    Lee Y.-H., Campbell H.D., Stallcup M.R.
    Mol. Cell. Biol. 24:2103-2117(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CARM1.
  7. "The flightless I protein colocalizes with actin- and microtubule-based structures in motile Swiss 3T3 fibroblasts: evidence for the involvement of PI 3-kinase and Ras-related small GTPases."
    Davy D.A., Campbell H.D., Fountain S., de Jong D., Crouch M.F.
    J. Cell Sci. 114:549-562(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  9. "Regulation of focal adhesions by flightless i involves inhibition of paxillin phosphorylation via a Rac1-dependent pathway."
    Kopecki Z., O'Neill G.M., Arkell R.M., Cowin A.J.
    J. Invest. Dermatol. 131:1450-1459(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY WOUND, DISRUPTION PHENOTYPE.
  10. "Flightless I is a focal adhesion-associated actin-capping protein that regulates cell migration."
    Mohammad I., Arora P.D., Naghibzadeh Y., Wang Y., Li J., Mascarenhas W., Janmey P.A., Dawson J.F., McCulloch C.A.
    FASEB J. 26:3260-3272(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFLII_MOUSE
AccessioniPrimary (citable) accession number: Q9JJ28
Secondary accession number(s): Q8K095, Q8VI44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Flii deficiency causes lethality during early embryogenesis at a stage preceding gastrulation.

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.