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Protein

Formin-like protein 1

Gene

Fmnl1

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

Functioni

Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. May play a role in the control of cell motility and survival of macrophages.2 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • GTPase activating protein binding Source: UniProtKB
  • profilin binding Source: MGI
  • Rac GTPase binding Source: UniProtKB

GO - Biological processi

  • actin filament severing Source: UniProtKB
  • cellular process Source: MGI
  • cortical actin cytoskeleton organization Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • substrate-dependent cell migration Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-like protein 1
Alternative name(s):
Formin-related protein
Gene namesi
Name:Fmnl1
Synonyms:Frl, Frl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1888994. Fmnl1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • phagocytic vesicle Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 10941093Formin-like protein 1PRO_0000194891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei7 – 71PhosphoserineBy similarity
Modified residuei184 – 1841PhosphoserineCombined sources
Modified residuei1021 – 10211PhosphoserineBy similarity

Post-translational modificationi

Myristoylation mediates membrane localization.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9JL26.
MaxQBiQ9JL26.
PaxDbiQ9JL26.
PRIDEiQ9JL26.

PTM databases

iPTMnetiQ9JL26.
PhosphoSiteiQ9JL26.

Expressioni

Tissue specificityi

Highly expressed in the spleen, lymph node and bone marrow cells.1 Publication

Gene expression databases

BgeeiQ9JL26.
CleanExiMM_FMNL1.
ExpressionAtlasiQ9JL26. baseline and differential.
GenevisibleiQ9JL26. MM.

Interactioni

Subunit structurei

Interacts with RAC1, PFN1 and PFN2. Interacts (activated by RAC1) with SRGAP2 (via SH3 domain); regulates the actin filament severing activity of FMNL1.2 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • GTPase activating protein binding Source: UniProtKB
  • profilin binding Source: MGI
  • Rac GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi208325. 1 interaction.
IntActiQ9JL26. 4 interactions.
MINTiMINT-4130216.
STRINGi10090.ENSMUSP00000046296.

Structurei

3D structure databases

ProteinModelPortaliQ9JL26.
SMRiQ9JL26. Positions 31-421, 628-1069.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 464438GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini627 – 1018392FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1049 – 108234DADPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi532 – 61180Pro-richAdd
BLAST

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the N-terminus. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).By similarity

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1923. Eukaryota.
ENOG410Y3DT. LUCA.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000231209.
HOVERGENiHBG053118.
InParanoidiQ9JL26.
OMAiPYIRADT.
OrthoDBiEOG7F7W8J.
PhylomeDBiQ9JL26.
TreeFamiTF325155.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027657. FMNL1.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF188. PTHR23213:SF188. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JL26-1) [UniParc]FASTAAdd to basket

Also known as: Frlalpha

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
MGNAAGSAEQ PAGPTASPPK QPAVPKQPMP AAGELEERFT RVLNCMNLPP
60 70 80 90 100
DKVQLLSQYD NEKKWELICD QERFQVKNPP AAYIQKLKSY LDTGGVSRKV
110 120 130 140 150
ASDWMSNLGF KRRVQESTQV LRELETSLRT NHIGWVQEFL NEENRGLDVL
160 170 180 190 200
LEYLAFAQCS VAYDMESTDS VASGAEKSKP LDQSVEDLSK APPSSVPKSR
210 220 230 240 250
LTIKLTPAHS RKALRNSRIV SQKDDVHVCI MCLRAIMNYQ SGFSLVMNHP
260 270 280 290 300
ACVNEIALSL NNKSPRTKAL VLELLAAVCL VRGGHDIILA AFDNFKEVCG
310 320 330 340 350
EQHRFEKLME YFRHEDSNID FMVACMQFIN IVVHSVENMN FRVFLQYEFT
360 370 380 390 400
HLGLDLYLER LRLTESDKLQ VQIQAYLDNV FDVGTLLEET ETKNAVLEHM
410 420 430 440 450
EELQEQVATL TERLRDTEND SMAKIAELEK QLSQARKELE TLRERFSEST
460 470 480 490 500
PMGTSRRIPE PEKVPVPTVV RPSALELKVE ELEEKGLIRI LRGPGDVVSI
510 520 530 540 550
EILPGAAATP SGDDAQAPRV STDSPSTAES IPEAASPPPP PPPPPPPLPN
560 570 580 590 600
LQSQQEAPPS APPLAPPLPG CAEPPPAPPL PGDLPPPPPP PPLGTDGPVP
610 620 630 640 650
PPPPPPPGGP PDILGGQGPD IGPGVKAKKP IQTKFRMPLL NWVALKPSQI
660 670 680 690 700
TGTVFTELND EKVLQELDMN DFEEHFKTKS QGPCLDISAL KGKASQKAPT
710 720 730 740 750
KTILIEANRA KNLAITLRKG NLGADRICQA IETYDLQTLS LDFLELLTRF
760 770 780 790 800
LPTDYERSLI ARFEKEQRPM EELSEEDRFM LRFSRIQRLP ERMNTLTFLG
810 820 830 840 850
NFPDTAQLLM PQLNAIIAAS MSIKSSDKLR QILEIVLAFG NYMNSSKRGA
860 870 880 890 900
AYGFRLQSLD ALLEMKSTDR KQTLLHYLVK VIAEKYPQLT GFHSDLHFLD
910 920 930 940 950
KAGSVSLDSV LGDVRSLQRG LELTQREFVR QDDCLVLKEF LRANSPTMDK
960 970 980 990 1000
LLADSKTAQE AYESVVEYFG ENPKTTSPSM FFSLFSRFTK AYKKAEQEVE
1010 1020 1030 1040 1050
QWKKEAAADT SGREEPPTPK SPPKARRQQM DLISELKRKQ QKEPLIYESD
1060 1070 1080 1090
RDGAIEDIIT DLRNQPYIRA DTGRRSARRR PPGPPLPVTT DLAL
Length:1,094
Mass (Da):122,060
Last modified:October 1, 2000 - v1
Checksum:i23A4BF24FB8F7A68
GO
Isoform 2 (identifier: Q9JL26-2) [UniParc]FASTAAdd to basket

Also known as: Frlbeta

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     27-30: QPMP → MVGT
     1061-1094: DLRNQPYIRADTGRRSARRRPPGPPLPVTTDLAL → VLKTVPFTARTGKRTSRLLCEASLGEEMTL

Show »
Length:1,064
Mass (Da):119,034
Checksum:iCCD961B3B4E329BC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641K → R in AAD01273 (PubMed:10958683).Curated
Sequence conflicti94 – 941G → D in AAD01273 (PubMed:10958683).Curated
Sequence conflicti111 – 1111K → R in AAD01273 (PubMed:10958683).Curated
Sequence conflicti117 – 1171S → F in AAD01273 (PubMed:10958683).Curated
Sequence conflicti581 – 5811P → H in AAD01273 (PubMed:10958683).Curated
Sequence conflicti620 – 6201D → N in AAD01273 (PubMed:10958683).Curated
Sequence conflicti981 – 9811F → L in AAD01273 (PubMed:10958683).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform 2. 1 PublicationVSP_013978Add
BLAST
Alternative sequencei27 – 304QPMP → MVGT in isoform 2. 1 PublicationVSP_013979
Alternative sequencei1061 – 109434DLRNQ…TDLAL → VLKTVPFTARTGKRTSRLLC EASLGEEMTL in isoform 2. 1 PublicationVSP_013980Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006466 mRNA. Translation: AAD01273.1.
AF215666 mRNA. Translation: AAF25953.1.
AK131173 mRNA. Translation: BAD21423.1.
CCDSiCCDS36348.1. [Q9JL26-1]
PIRiT13963.
RefSeqiNP_001071166.1. NM_001077698.1. [Q9JL26-1]
NP_062653.2. NM_019679.2.
UniGeneiMm.138913.

Genome annotation databases

EnsembliENSMUST00000042286; ENSMUSP00000046296; ENSMUSG00000055805. [Q9JL26-1]
GeneIDi57778.
KEGGimmu:57778.
UCSCiuc007ltv.1. mouse. [Q9JL26-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006466 mRNA. Translation: AAD01273.1.
AF215666 mRNA. Translation: AAF25953.1.
AK131173 mRNA. Translation: BAD21423.1.
CCDSiCCDS36348.1. [Q9JL26-1]
PIRiT13963.
RefSeqiNP_001071166.1. NM_001077698.1. [Q9JL26-1]
NP_062653.2. NM_019679.2.
UniGeneiMm.138913.

3D structure databases

ProteinModelPortaliQ9JL26.
SMRiQ9JL26. Positions 31-421, 628-1069.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208325. 1 interaction.
IntActiQ9JL26. 4 interactions.
MINTiMINT-4130216.
STRINGi10090.ENSMUSP00000046296.

PTM databases

iPTMnetiQ9JL26.
PhosphoSiteiQ9JL26.

Proteomic databases

EPDiQ9JL26.
MaxQBiQ9JL26.
PaxDbiQ9JL26.
PRIDEiQ9JL26.

Protocols and materials databases

DNASUi57778.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042286; ENSMUSP00000046296; ENSMUSG00000055805. [Q9JL26-1]
GeneIDi57778.
KEGGimmu:57778.
UCSCiuc007ltv.1. mouse. [Q9JL26-1]

Organism-specific databases

CTDi752.
MGIiMGI:1888994. Fmnl1.

Phylogenomic databases

eggNOGiKOG1923. Eukaryota.
ENOG410Y3DT. LUCA.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000231209.
HOVERGENiHBG053118.
InParanoidiQ9JL26.
OMAiPYIRADT.
OrthoDBiEOG7F7W8J.
PhylomeDBiQ9JL26.
TreeFamiTF325155.

Enzyme and pathway databases

ReactomeiR-MMU-5663220. RHO GTPases Activate Formins.

Miscellaneous databases

ChiTaRSiFmnl1. mouse.
PROiQ9JL26.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JL26.
CleanExiMM_FMNL1.
ExpressionAtlasiQ9JL26. baseline and differential.
GenevisibleiQ9JL26. MM.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR010472. FH3_dom.
IPR027657. FMNL1.
IPR014768. GBD/FH3_dom.
IPR010473. GTPase-bd.
[Graphical view]
PANTHERiPTHR23213:SF188. PTHR23213:SF188. 1 hit.
PfamiPF06367. Drf_FH3. 1 hit.
PF06371. Drf_GBD. 2 hits.
PF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM01139. Drf_FH3. 1 hit.
SM01140. Drf_GBD. 1 hit.
SM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages."
    Yayoshi-Yamamoto S., Taniuchi I., Watanabe T.
    Mol. Cell. Biol. 20:6872-6881(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH RAC1; PFN1 AND PFN2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-1094.
    Tissue: Natural killer cell.
  3. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung and Spleen.
  5. Cited for: FUNCTION IN ACTIN FILAMENT SEVERING, INTERACTION WITH SRGAP2, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiFMNL1_MOUSE
AccessioniPrimary (citable) accession number: Q9JL26
Secondary accession number(s): Q6KAN4, Q9Z2V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 123 of the entry and version 1 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.