FMNL1_MOUSE
ID FMNL1_MOUSE Reviewed; 1094 AA.
AC Q9JL26; Q6KAN4; Q9Z2V7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Formin-like protein 1;
DE AltName: Full=Formin-related protein;
GN Name=Fmnl1; Synonyms=Frl, Frl1;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP RAC1; PFN1 AND PFN2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10958683; DOI=10.1128/mcb.20.18.6872-6881.2000;
RA Yayoshi-Yamamoto S., Taniuchi I., Watanabe T.;
RT "FRL, a novel formin-related protein, binds to Rac and regulates cell
RT motility and survival of macrophages.";
RL Mol. Cell. Biol. 20:6872-6881(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-1094.
RC TISSUE=Natural killer cell;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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).
RN [5]
RP FUNCTION IN ACTIN FILAMENT SEVERING, INTERACTION WITH SRGAP2, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21148482; DOI=10.1074/jbc.m110.190397;
RA Mason F.M., Heimsath E.G., Higgs H.N., Soderling S.H.;
RT "Bi-modal regulation of a formin by srGAP2.";
RL J. Biol. Chem. 286:6577-6586(2011).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the cortical actin filament
CC dynamics and cell shape. May play a role in the control of cell
CC motility and survival of macrophages. {ECO:0000269|PubMed:10958683,
CC ECO:0000269|PubMed:21148482}.
CC -!- SUBUNIT: Interacts with RAC1, PFN1 and PFN2. Interacts (activated by
CC RAC1) with SRGAP2 (via SH3 domain); regulates the actin filament
CC severing activity of FMNL1. {ECO:0000269|PubMed:10958683,
CC ECO:0000269|PubMed:21148482}.
CC -!- INTERACTION:
CC Q9JL26; D0ZIB5: steC; Xeno; NbExp=6; IntAct=EBI-772250, EBI-27033646;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane; Lipid-
CC anchor. Cytoplasmic vesicle, phagosome. Note=Recruited to actin-rich
CC phagosomes during phagocytosis. Translocates to the plasma membrane
CC upon activation by RAC1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Frlalpha;
CC IsoId=Q9JL26-1; Sequence=Displayed;
CC Name=2; Synonyms=Frlbeta;
CC IsoId=Q9JL26-2; Sequence=VSP_013978, VSP_013979, VSP_013980;
CC -!- TISSUE SPECIFICITY: Highly expressed in the spleen, lymph node and bone
CC marrow cells. {ECO:0000269|PubMed:10958683}.
CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory
CC interaction with the N-terminus. This autoinhibition is released upon
CC competitive binding of an activated GTPase. The release of DAD allows
CC the FH2 domain to then nucleate and elongate nonbranched actin
CC filaments (By similarity). {ECO:0000250}.
CC -!- PTM: Myristoylation mediates membrane localization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; AF006466; AAD01273.1; -; mRNA.
DR EMBL; AF215666; AAF25953.1; -; mRNA.
DR EMBL; AK131173; BAD21423.1; -; mRNA.
DR CCDS; CCDS36348.1; -. [Q9JL26-1]
DR PIR; T13963; T13963.
DR RefSeq; NP_001071166.1; NM_001077698.1. [Q9JL26-1]
DR RefSeq; NP_062653.2; NM_019679.2.
DR AlphaFoldDB; Q9JL26; -.
DR SMR; Q9JL26; -.
DR BioGRID; 208325; 20.
DR IntAct; Q9JL26; 5.
DR MINT; Q9JL26; -.
DR STRING; 10090.ENSMUSP00000046296; -.
DR iPTMnet; Q9JL26; -.
DR PhosphoSitePlus; Q9JL26; -.
DR SwissPalm; Q9JL26; -.
DR EPD; Q9JL26; -.
DR jPOST; Q9JL26; -.
DR MaxQB; Q9JL26; -.
DR PaxDb; Q9JL26; -.
DR PeptideAtlas; Q9JL26; -.
DR PRIDE; Q9JL26; -.
DR ProteomicsDB; 267368; -. [Q9JL26-1]
DR ProteomicsDB; 267369; -. [Q9JL26-2]
DR Antibodypedia; 17595; 186 antibodies from 32 providers.
DR DNASU; 57778; -.
DR Ensembl; ENSMUST00000042286; ENSMUSP00000046296; ENSMUSG00000055805. [Q9JL26-1]
DR GeneID; 57778; -.
DR KEGG; mmu:57778; -.
DR UCSC; uc007ltv.1; mouse. [Q9JL26-1]
DR CTD; 752; -.
DR MGI; MGI:1888994; Fmnl1.
DR VEuPathDB; HostDB:ENSMUSG00000055805; -.
DR eggNOG; KOG1923; Eukaryota.
DR GeneTree; ENSGT00940000156292; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR InParanoid; Q9JL26; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; Q9JL26; -.
DR TreeFam; TF325155; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 57778; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Fmnl1; mouse.
DR PRO; PR:Q9JL26; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JL26; protein.
DR Bgee; ENSMUSG00000055805; Expressed in granulocyte and 79 other tissues.
DR ExpressionAtlas; Q9JL26; baseline and differential.
DR Genevisible; Q9JL26; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0032794; F:GTPase activating protein binding; IDA:UniProtKB.
DR GO; GO:0005522; F:profilin binding; IDA:MGI.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IDA:UniProtKB.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0006929; P:substrate-dependent cell migration; IMP:MGI.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014767; DAD_dom.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR027657; FMNL1.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR PANTHER; PTHR45857:SF2; PTHR45857:SF2; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF06371; Drf_GBD; 2.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51231; DAD; 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95466"
FT CHAIN 2..1094
FT /note="Formin-like protein 1"
FT /id="PRO_0000194891"
FT DOMAIN 27..464
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 627..1018
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1049..1082
FT /note="DAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00577"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95466"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95466"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95466"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O95466"
FT VAR_SEQ 1..26
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10958683"
FT /id="VSP_013978"
FT VAR_SEQ 27..30
FT /note="QPMP -> MVGT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10958683"
FT /id="VSP_013979"
FT VAR_SEQ 1061..1094
FT /note="DLRNQPYIRADTGRRSARRRPPGPPLPVTTDLAL -> VLKTVPFTARTGKR
FT TSRLLCEASLGEEMTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10958683"
FT /id="VSP_013980"
FT CONFLICT 64
FT /note="K -> R (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> D (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> R (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="S -> F (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="P -> H (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 620
FT /note="D -> N (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="F -> L (in Ref. 1; AAD01273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1094 AA; 122060 MW; 23A4BF24FB8F7A68 CRC64;
MGNAAGSAEQ PAGPTASPPK QPAVPKQPMP AAGELEERFT RVLNCMNLPP DKVQLLSQYD
NEKKWELICD QERFQVKNPP AAYIQKLKSY LDTGGVSRKV ASDWMSNLGF KRRVQESTQV
LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VAYDMESTDS VASGAEKSKP
LDQSVEDLSK APPSSVPKSR LTIKLTPAHS RKALRNSRIV SQKDDVHVCI MCLRAIMNYQ
SGFSLVMNHP ACVNEIALSL NNKSPRTKAL VLELLAAVCL VRGGHDIILA AFDNFKEVCG
EQHRFEKLME YFRHEDSNID FMVACMQFIN IVVHSVENMN FRVFLQYEFT HLGLDLYLER
LRLTESDKLQ VQIQAYLDNV FDVGTLLEET ETKNAVLEHM EELQEQVATL TERLRDTEND
SMAKIAELEK QLSQARKELE TLRERFSEST PMGTSRRIPE PEKVPVPTVV RPSALELKVE
ELEEKGLIRI LRGPGDVVSI EILPGAAATP SGDDAQAPRV STDSPSTAES IPEAASPPPP
PPPPPPPLPN LQSQQEAPPS APPLAPPLPG CAEPPPAPPL PGDLPPPPPP PPLGTDGPVP
PPPPPPPGGP PDILGGQGPD IGPGVKAKKP IQTKFRMPLL NWVALKPSQI TGTVFTELND
EKVLQELDMN DFEEHFKTKS QGPCLDISAL KGKASQKAPT KTILIEANRA KNLAITLRKG
NLGADRICQA IETYDLQTLS LDFLELLTRF LPTDYERSLI ARFEKEQRPM EELSEEDRFM
LRFSRIQRLP ERMNTLTFLG NFPDTAQLLM PQLNAIIAAS MSIKSSDKLR QILEIVLAFG
NYMNSSKRGA AYGFRLQSLD ALLEMKSTDR KQTLLHYLVK VIAEKYPQLT GFHSDLHFLD
KAGSVSLDSV LGDVRSLQRG LELTQREFVR QDDCLVLKEF LRANSPTMDK LLADSKTAQE
AYESVVEYFG ENPKTTSPSM FFSLFSRFTK AYKKAEQEVE QWKKEAAADT SGREEPPTPK
SPPKARRQQM DLISELKRKQ QKEPLIYESD RDGAIEDIIT DLRNQPYIRA DTGRRSARRR
PPGPPLPVTT DLAL
