FMN1_MOUSE
ID FMN1_MOUSE Reviewed; 1466 AA.
AC Q05860; A2AFY9; A2AFZ0; Q05859;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Formin-1;
DE AltName: Full=Limb deformity protein;
GN Name=Fmn1; Synonyms=Fmn, Ld;
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] (ISOFORM 1), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney, and Testis;
RX PubMed=2392150; DOI=10.1038/346850a0;
RA Woychik R.P., Maas R.L., Zeller R., Vogt T.F., Leder P.;
RT "'Formins': proteins deduced from the alternative transcripts of the limb
RT deformity gene.";
RL Nature 346:850-853(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC TISSUE=Embryo;
RX PubMed=1339380; DOI=10.1101/gad.6.1.29;
RA Grusby-Jackson L., Kuo A., Leder P.;
RT "A variant limb deformity transcript expressed in the embryonic mouse limb
RT defines a novel formin.";
RL Genes Dev. 6:29-37(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP PHOSPHORYLATION, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX PubMed=8516300; DOI=10.1073/pnas.90.12.5554;
RA Vogt T.F., Jackson-Grusby L., Rush J., Leder P.;
RT "Formins: phosphoprotein isoforms encoded by the mouse limb deformity
RT locus.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5554-5558(1993).
RN [5]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX PubMed=9119367; DOI=10.1006/geno.1996.4519;
RA Wang C.C., Chan D.C., Leder P.;
RT "The mouse formin (Fmn) gene: genomic structure, novel exons, and genetic
RT mapping.";
RL Genomics 39:303-311(1997).
RN [6]
RP FUNCTION.
RX PubMed=15198975; DOI=10.1101/gad.299904;
RA Zuniga A., Michos O., Spitz F., Haramis A.-P.G., Panman L., Galli A.,
RA Vintersten K., Klasen C., Mansfield W., Kuc S., Duboule D., Dono R.,
RA Zeller R.;
RT "Mouse limb deformity mutations disrupt a global control region within the
RT large regulatory landscape required for Gremlin expression.";
RL Genes Dev. 18:1553-1564(2004).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH ALPHA-CATENIN, AND TISSUE SPECIFICITY.
RX PubMed=14647292; DOI=10.1038/ncb1075;
RA Kobielak A., Pasolli H.A., Fuchs E.;
RT "Mammalian formin-1 participates in adherens junctions and polymerization
RT of linear actin cables.";
RL Nat. Cell Biol. 6:21-30(2004).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TUBULIN.
RX PubMed=16480715; DOI=10.1016/j.yexcr.2005.12.035;
RA Zhou F., Leder P., Martin S.S.;
RT "Formin-1 protein associates with microtubules through a peptide domain
RT encoded by exon-2.";
RL Exp. Cell Res. 312:1119-1126(2006).
CC -!- FUNCTION: Plays a role in the formation of adherens junction and the
CC polymerization of linear actin cables. {ECO:0000269|PubMed:14647292,
CC ECO:0000269|PubMed:15198975}.
CC -!- SUBUNIT: Interacts with alpha-catenin and may interact with tubulin.
CC {ECO:0000269|PubMed:14647292, ECO:0000269|PubMed:16480715}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction, adherens
CC junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
CC Note=Localization to the adherens junctions is alpha-catenin-dependent.
CC Also localizes to F-actin bundles originating from adherens junctions.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.
CC Note=Isoform 2 localizes to microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=IA;
CC IsoId=Q05860-1; Sequence=Displayed;
CC Name=2; Synonyms=IB;
CC IsoId=Q05860-2; Sequence=VSP_027216;
CC Name=3; Synonyms=II;
CC IsoId=Q05860-3; Sequence=VSP_001570;
CC Name=4; Synonyms=III;
CC IsoId=Q05860-4; Sequence=VSP_001571, VSP_001572;
CC Name=5; Synonyms=IV;
CC IsoId=Q05860-5; Sequence=VSP_027214, VSP_027215, VSP_027216;
CC Name=6; Synonyms=V;
CC IsoId=Q05860-6; Sequence=VSP_029424, VSP_029425, VSP_027216;
CC -!- TISSUE SPECIFICITY: It is present in the adult kidney, testis, limb,
CC ovary, brain, small intestine, salivary gland and harderian gland.
CC Isoforms 1, 2 and 5 are detected in skin and keratinocytes. Isoform 5
CC is found throughout the embryo. {ECO:0000269|PubMed:14647292,
CC ECO:0000269|PubMed:2392150}.
CC -!- DEVELOPMENTAL STAGE: It is present throughout the embryo. In the
CC developing limb bud, the protein is expressed in the apical ectodermal
CC ridge and the mesenchymal compartment, predominantly in the posterior
CC region. During kidney morphogenesis, expression is initially restricted
CC to the epithelial compartment of the pronephros and mesonephros.
CC Isoform 5 is found in the apical ectodermal ridge and the mesenchymal
CC compartment of the developing limb bud.
CC -!- PTM: Phosphorylated on serine and possibly threonine residues.
CC {ECO:0000269|PubMed:8516300}.
CC -!- MISCELLANEOUS: Was originally thought to play a role in limb bud
CC development based on the fact that limb deformity (ld) mutants are
CC associated with Fmn1 gene disruption. However, PubMed:15198975 shows
CC that limb deformity mutations rather affects Grem1 cis-regulatory
CC regions localized in Fmn1 gene and that loss of Grem1 (gremlin-1)
CC expression is the cause of limb malformations.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X53599; CAA37668.1; -; mRNA.
DR EMBL; X62379; CAA44244.1; -; mRNA.
DR EMBL; AL672253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16559.1; -. [Q05860-1]
DR CCDS; CCDS71113.1; -. [Q05860-5]
DR PIR; S11515; S11515.
DR PIR; S24407; S24407.
DR RefSeq; NP_001272388.1; NM_001285459.1. [Q05860-5]
DR RefSeq; NP_034360.2; NM_010230.2. [Q05860-1]
DR RefSeq; XP_011237596.1; XM_011239294.1. [Q05860-2]
DR RefSeq; XP_011237597.1; XM_011239295.1. [Q05860-2]
DR PDB; 2JUP; NMR; -; P=881-888.
DR PDB; 2RLY; NMR; -; P=874-881.
DR PDB; 2RM0; NMR; -; P=880-888.
DR PDBsum; 2JUP; -.
DR PDBsum; 2RLY; -.
DR PDBsum; 2RM0; -.
DR AlphaFoldDB; Q05860; -.
DR SMR; Q05860; -.
DR BioGRID; 199711; 13.
DR DIP; DIP-646N; -.
DR ELM; Q05860; -.
DR IntAct; Q05860; 2.
DR MINT; Q05860; -.
DR STRING; 10090.ENSMUSP00000099606; -.
DR iPTMnet; Q05860; -.
DR PhosphoSitePlus; Q05860; -.
DR MaxQB; Q05860; -.
DR PaxDb; Q05860; -.
DR PeptideAtlas; Q05860; -.
DR PRIDE; Q05860; -.
DR ProteomicsDB; 267599; -. [Q05860-1]
DR ProteomicsDB; 267600; -. [Q05860-2]
DR ProteomicsDB; 267601; -. [Q05860-3]
DR ProteomicsDB; 267602; -. [Q05860-4]
DR ProteomicsDB; 267603; -. [Q05860-5]
DR ProteomicsDB; 267604; -. [Q05860-6]
DR Antibodypedia; 51683; 109 antibodies from 19 providers.
DR DNASU; 14260; -.
DR Ensembl; ENSMUST00000081349; ENSMUSP00000080093; ENSMUSG00000044042. [Q05860-5]
DR Ensembl; ENSMUST00000099576; ENSMUSP00000097171; ENSMUSG00000044042. [Q05860-2]
DR Ensembl; ENSMUST00000102547; ENSMUSP00000099606; ENSMUSG00000044042. [Q05860-1]
DR GeneID; 14260; -.
DR KEGG; mmu:14260; -.
DR UCSC; uc008lpk.1; mouse. [Q05860-4]
DR UCSC; uc008lpl.1; mouse. [Q05860-1]
DR UCSC; uc008lpn.2; mouse. [Q05860-5]
DR CTD; 342184; -.
DR MGI; MGI:101815; Fmn1.
DR VEuPathDB; HostDB:ENSMUSG00000044042; -.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000154289; -.
DR HOGENOM; CLU_271027_0_0_1; -.
DR InParanoid; Q05860; -.
DR OMA; TWHERND; -.
DR OrthoDB; 249504at2759; -.
DR PhylomeDB; Q05860; -.
DR TreeFam; TF351317; -.
DR BioGRID-ORCS; 14260; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Fmn1; mouse.
DR EvolutionaryTrace; Q05860; -.
DR PRO; PR:Q05860; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q05860; protein.
DR Bgee; ENSMUSG00000044042; Expressed in lumbar dorsal root ganglion and 177 other tissues.
DR ExpressionAtlas; Q05860; baseline and differential.
DR Genevisible; Q05860; MM.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0035136; P:forelimb morphogenesis; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0060173; P:limb development; IMP:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IDA:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0072092; P:ureteric bud invasion; IMP:MGI.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1466
FT /note="Formin-1"
FT /id="PRO_0000194886"
FT DOMAIN 870..970
FT /note="FH1"
FT DOMAIN 983..1435
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 1..624
FT /note="Microtubule-binding"
FT REGION 150..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..842
FT /note="Mediates interaction with alpha-catenin"
FT REGION 507..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 722..786
FT /evidence="ECO:0000255"
FT COMPBIAS 153..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..897
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..682
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:1339380"
FT /id="VSP_027214"
FT VAR_SEQ 1..623
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_029424"
FT VAR_SEQ 624
FT /note="P -> MVTTGSPPFNTMGACYRYNPRYGQPISVPKVWKCRHRRSVTPDE
FT (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_029425"
FT VAR_SEQ 625..722
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001570"
FT VAR_SEQ 626..627
FT /note="IA -> SV (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001571"
FT VAR_SEQ 628..1466
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001572"
FT VAR_SEQ 683
FT /note="N -> MEEVGNSLSSRDVLEPDKSEAGLEMAQSILSKFSMKSLFGFTNKLDS
FT LEPEEEDAVLKAFRSLEGDPAPERGDPSKGSDQPQAEAPVPPDLKNDGKSARAETGSEG
FT SQGKGRSNTSSPGYELSPATVSVDNEEVIWVRGTLVHTTSDSDSEDGDQEAEEESSLDT
FT QKPTTVVLCEPSQEPKDRAGDSEENTDTGNTDDTELCAEESQRTLPETSSKLELGGDGS
FT HPAEHSPRQDQAAEEGSQIPPAATDQTVGALASTVSKREAPEEKPFQLPAFFSGLRVLK
FT KGATAEAGETITEIKPKDGDLALLKLTQRVQKSLGQGGPQTVKSPGRATDPKATPTLLE
FT QLSQLLNIDMPRTEQKEADPEFHGADEMGYSTDQESHKSPRDAHVQGGQVKARTPETAL
FT EAFKALFIRPPKKGSTADTSELEALKRKMKHEKESLRAVFERSKSRPADSPSDPKS
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:1339380"
FT /id="VSP_027215"
FT VAR_SEQ 1250..1285
FT /note="Missing (in isoform 2, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1339380"
FT /id="VSP_027216"
FT CONFLICT 220
FT /note="V -> A (in Ref. 1; CAA37668)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="G -> E (in Ref. 1; CAA37668 and 2; CAA44244)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="H -> Q (in Ref. 1; CAA37668 and 2; CAA44244)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="G -> GPP (in Ref. 1; CAA37668 and 2; CAA44244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1466 AA; 163581 MW; 5482F8AAB66CBF32 CRC64;
MEGTHCTLQL HNPIAELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC YQVREGPDIT
SLSQQPNEHP GDIFFKQTPT KNILTELYKL TAEKERLLDS LLRSDNILGV SMGSQEGKLQ
ELSVILATGD EYFQSAGNWR RELPVSSLIR RSTQENKKPR RSGRRRESPE ELRQKRTRRK
GRGCQESAFQ MGKDQVCSSS SLSFRARPNL RLLEERGNLV PRGTLTSSLR RRESCPANIL
RTPDADLAFG NSGRTSEDTD LEGPLSPDSS PTEVGDADVG GQLKSSHQQE PPQPNVSESH
GKHAGAERWS SRTRKSKSLE RTCSKKPVSK VVAKIQEPSA PVKRIVRAHH DGKGRVAYGP
ETQTEFIPKA DFLTLPGGET ETHSSGRLEE EQPGIKSLRS SAPERASITK EPASTEAAVN
KVLRKVIESE KLDEATEGKR LGFSLNTRAT HTFPETRSQR KAGLPQSGHK FLLLDLPHTV
GPDSPQPKCD EKKPTPQVPT ALGMVFNNSS PQSSAHKRLS PVPSPLSPRC PSPQQHHRIL
LLPPLPSEGE VVFNEYPSRK NDVSSGFPSA DTLEPSSTTK VTETKGASPT SLRASQTWLV
SEEASEKGLG PEKITAPPQH QLPPGIASEG FPCDNFKEQT AKDLPNKDGG VWVPGYRAGP
PCPFLLHEEK EKTSRSELYL DLNPDQSPTE QDDRTPGRLQ AVWPPPKTKD TEEKVGLKYT
EAEYQAAILH LKREHKEEIE TLQAQFELKT FHIRGEHALV TARLEEAIEN LKQQLGKRRE
GCEEMRDVCI STDDDCSPKA FRNVCIQTDR ETFLKPCDAE SKATRSSQIV PKKLTISLTQ
LSPSKDSKDI HAPFQTREGT SSSSQHKISP PAPPTPPPLP PPLIPPPPPL PPGLGPLPPA
PPIPPVCPVS PPPPPPPPPP TPVPPSDGPP PPPPPPPPLP NVLALPNSGG PPPPPPPPPP
GLAPPPPPGL SFGLSSSSSQ YPRKPAIEPS CPMKPLYWTR IQINDKSQDA APTLWDSLEE
PHIRDTSEFE YLFSKDTTQQ KKKPLSEAYE KKNKVKKIIK LLDGKRSQTV GILISSLHLE
MKDIQQAIFT VDDSVVDLET LAALYENRAQ EDELTKIRKY YETSKEEDLK LLDKPEQFLH
ELAQIPNFAE RAQCIIFRAV FSEGITSLHR KVEIVTRASK GLLHMKSVKD ILALILAFGN
YMNGGNRTRG QADGYSLEIL PKLKDVKSRD NGMNLVDYVV KYYLRYYDQC KHHDQEASCR
GKDLFSLYFH IAVHPQRKSG LELKQEAGTD KSVFPLPEPQ DFFLASQVKF EDLLKDLRKL
KRQLEASEQQ MKLVCKESPR EYLQPFKDKL EEFFKKAKKE HKMEESHLEN AQKSFETTVG
YFGMKPKTGE KEVTPSYVFM VWFEFCSDFK TIWKRESKNI SKERLKMAQA SVSKLTSEKK
VETKKINPTA SLKERLRQKE ASVATN
