ID FMNL2_BOVIN Reviewed; 1095 AA. AC A0A3Q1LSX9; DT 13-SEP-2023, integrated into UniProtKB/Swiss-Prot. DT 10-APR-2019, sequence version 1. DT 29-MAY-2024, entry version 26. DE RecName: Full=Formin-like protein 2 {ECO:0000250|UniProtKB:Q96PY5}; GN Name=FMNL2 {ECO:0000250|UniProtKB:Q96PY5}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] RP INTERACTION WITH TCP11L2, AND SUBCELLULAR LOCATION. RX PubMed=32017087; DOI=10.1002/jcp.29617; RA Li S., Wang Z., Tong H., Li S., Yan Y.; RT "TCP11L2 promotes bovine skeletal muscle-derived satellite cell migration RT and differentiation via FMNL2."; RL J. Cell. Physiol. 235:7183-7193(2020). CC -!- FUNCTION: Plays a role in the regulation of cell morphology and CC cytoskeletal organization. Required in the cortical actin filament CC dynamics. {ECO:0000250|UniProtKB:Q96PY5}. CC -!- SUBUNIT: Interacts with TCP11L2; this interaction promotes muscle- CC derived satellite cell (MDSC) migration and differentiation. CC {ECO:0000269|PubMed:32017087}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32017087}. CC -!- DOMAIN: The DAD domain regulates activation via by an autoinhibitory CC interaction with the GBD/FH3 domain. This autoinhibition is released CC upon competitive binding of an activated GTPase. The release of DAD CC allows the FH2 domain to then nucleate and elongate nonbranched actin CC filaments (By similarity). {ECO:0000250|UniProtKB:Q9VUC6}. CC -!- SIMILARITY: Belongs to the formin homology family. {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; NKLS02000002; -; NOT_ANNOTATED_CDS; Genomic_RNA. DR AlphaFoldDB; A0A3Q1LSX9; -. DR SMR; A0A3Q1LSX9; -. DR STRING; 9913.ENSBTAP00000063529; -. DR VEuPathDB; HostDB:ENSBTAG00000026851; -. DR InParanoid; A0A3Q1LSX9; -. DR OMA; MMPGFSP; -. DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins. DR Reactome; R-BTA-9013106; RHOC GTPase cycle. DR Proteomes; UP000009136; Chromosome 2. DR Bgee; ENSBTAG00000026851; Expressed in hypothalamus and 106 other cell types or tissues. DR ExpressionAtlas; A0A3Q1LSX9; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central. DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015425; FH2_Formin. DR InterPro; IPR042201; FH2_Formin_sf. DR InterPro; IPR010472; FH3_dom. DR InterPro; IPR043592; FMNL_animal. DR InterPro; IPR014768; GBD/FH3_dom. DR InterPro; IPR010473; GTPase-bd. DR PANTHER; PTHR45857; FORMIN-LIKE PROTEIN; 1. DR PANTHER; PTHR45857:SF5; FORMIN-LIKE PROTEIN 2; 1. DR Pfam; PF06367; Drf_FH3; 1. DR Pfam; PF06371; Drf_GBD; 2. DR Pfam; PF02181; FH2; 1. DR PRINTS; PR01217; PRICHEXTENSN. DR SMART; SM01139; Drf_FH3; 1. DR SMART; SM01140; Drf_GBD; 1. DR SMART; SM00498; FH2; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR PROSITE; PS51444; FH2; 1. DR PROSITE; PS51232; GBD_FH3; 1. PE 1: Evidence at protein level; KW Actin-binding; Coiled coil; Cytoplasm; Reference proteome. FT CHAIN 1..1095 FT /note="Formin-like protein 2" FT /id="PRO_0000458825" FT DOMAIN 23..469 FT /note="GBD/FH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579" FT DOMAIN 617..1008 FT /note="FH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774" FT REGION 521..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 381..478 FT /evidence="ECO:0000255" FT COMPBIAS 521..537 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 546..600 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1095 AA; 124214 MW; 410E9DE51208AB03 CRC64; MGNAGSMDSQ QTDFRAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTVES SVDKSKPWSR SIEDLHRGSN LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT IKIQKKGDGD IAILPVVASG TLPTGSEVAV GNFVGPVMGA PSSGPLPPPP PPLPLSSDAP EAVQNGPATP PVPPPPPPPP PPPPPPPPPP PPPLPGPAAE TLPAPPLPPP PPPSAPPLPG TSSPTVVFNS GLAAVKIKKP IKTKFRMPVF NWVALKPNQI NGTVFNEIDD ERILEDLNVD EFEEIFKTKA QGPAIDLSSS KQKITQKGSN KVTLLEANRA KNLAITLRKA GKTAEEICKA IHVFDLKTLP VDFVECLMRF LPTENEVKVL RLYERERKPL ENLSDEDRFM MQFSKIERLM QKMTIMAFIG NFTESIQMLT PQLHSIIAAS VSIKSSQKLK KILEIILALG NYMNSSKRGA VYGFKLQSLD LLLDTKSTDR KQTLLHYISN VVKEKYQQVS LFYNELHYVE KAAAVSLENV LLDVKELQRG MDLTKREYTM HDHNTLLKEF IFNNEGKLKK LQDDAKIAQD AFDDVVKYFG ENPKTTPPSV FFPVFVRFVK AYKQAEEENE LRKKQEQALM EKLLEQEALL EQQDPKSPSH KSKRQQQELI AELRRRQVKD NRHVYEGKDG AIEDIITALK KNNITKFPNV HSRVRISSST PVVEDTQSWQ ASLFT //