FMNL2_MOUSE
ID FMNL2_MOUSE Reviewed; 1086 AA.
AC A2APV2; A2AQW1; Q69Z73; Q7TPA8; Q80VH6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Formin-like protein 2;
DE AltName: Full=Protein Man;
GN Name=Fmnl2; Synonyms=Kiaa1902, Man;
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 [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 409-1082 (ISOFORM 2).
RC STRAIN=CD-1; TISSUE=Limb;
RA Cui Y., Harland R.M.;
RT "Cloning of Man, a formin homology domain containing gene, and its
RT expression in the mouse limb.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 614-1086 (ISOFORM 1).
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-1086 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
CC -!- FUNCTION: Plays a role in the regulation of cell morphology and
CC cytoskeletal organization. Required in the cortical actin filament
CC dynamics (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2APV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2APV2-2; Sequence=VSP_025888, VSP_025890, VSP_025891;
CC Name=3;
CC IsoId=A2APV2-3; Sequence=VSP_025889;
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}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP87551.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAM19613.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL844859; CAM19034.1; -; Genomic_DNA.
DR EMBL; AL844510; CAM19034.1; JOINED; Genomic_DNA.
DR EMBL; AL845170; CAM19034.1; JOINED; Genomic_DNA.
DR EMBL; AL845170; CAM19616.1; -; Genomic_DNA.
DR EMBL; AL844510; CAM19616.1; JOINED; Genomic_DNA.
DR EMBL; AL844859; CAM19616.1; JOINED; Genomic_DNA.
DR EMBL; AL844510; CAM25963.1; -; Genomic_DNA.
DR EMBL; AL844859; CAM25963.1; JOINED; Genomic_DNA.
DR EMBL; AL845170; CAM25963.1; JOINED; Genomic_DNA.
DR EMBL; AL845170; CAM19613.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF513716; AAP87551.1; ALT_INIT; mRNA.
DR EMBL; BC048004; AAH48004.1; -; mRNA.
DR EMBL; AK173293; BAD32571.1; -; mRNA.
DR RefSeq; NP_765997.2; NM_172409.2.
DR RefSeq; XP_006498396.1; XM_006498333.3. [A2APV2-3]
DR AlphaFoldDB; A2APV2; -.
DR SMR; A2APV2; -.
DR BioGRID; 214689; 10.
DR IntAct; A2APV2; 1.
DR STRING; 10090.ENSMUSP00000088472; -.
DR iPTMnet; A2APV2; -.
DR PhosphoSitePlus; A2APV2; -.
DR SwissPalm; A2APV2; -.
DR jPOST; A2APV2; -.
DR MaxQB; A2APV2; -.
DR PaxDb; A2APV2; -.
DR PeptideAtlas; A2APV2; -.
DR PRIDE; A2APV2; -.
DR ProteomicsDB; 267370; -. [A2APV2-1]
DR ProteomicsDB; 267371; -. [A2APV2-2]
DR ProteomicsDB; 267372; -. [A2APV2-3]
DR Antibodypedia; 10309; 103 antibodies from 24 providers.
DR DNASU; 71409; -.
DR Ensembl; ENSMUST00000090952; ENSMUSP00000088472; ENSMUSG00000036053. [A2APV2-3]
DR Ensembl; ENSMUST00000127122; ENSMUSP00000118658; ENSMUSG00000036053. [A2APV2-1]
DR GeneID; 71409; -.
DR KEGG; mmu:71409; -.
DR CTD; 114793; -.
DR MGI; MGI:1918659; Fmnl2.
DR VEuPathDB; HostDB:ENSMUSG00000036053; -.
DR eggNOG; KOG1923; Eukaryota.
DR GeneTree; ENSGT00940000155515; -.
DR HOGENOM; CLU_003597_0_0_1; -.
DR InParanoid; A2APV2; -.
DR OrthoDB; 288325at2759; -.
DR PhylomeDB; A2APV2; -.
DR TreeFam; TF325155; -.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR BioGRID-ORCS; 71409; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Fmnl2; mouse.
DR PRO; PR:A2APV2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2APV2; protein.
DR Bgee; ENSMUSG00000036053; Expressed in indifferent gonad and 222 other tissues.
DR ExpressionAtlas; A2APV2; baseline and differential.
DR Genevisible; A2APV2; MM.
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; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR Gene3D; 1.20.58.2220; -; 1.
DR Gene3D; 1.25.10.10; -; 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; IPR027656; FMNL2.
DR InterPro; IPR043592; FMNL_animal.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45857; PTHR45857; 1.
DR PANTHER; PTHR45857:SF5; PTHR45857:SF5; 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; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Lipoprotein; Myristate; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..1086
FT /note="Formin-like protein 2"
FT /id="PRO_0000289094"
FT DOMAIN 23..469
FT /note="GBD/FH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00579"
FT DOMAIN 615..1006
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT DOMAIN 1038..1077
FT /note="DAD"
FT REGION 520..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..598
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PY5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 554..588
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025888"
FT VAR_SEQ 1056..1086
FT /note="ALKKNNITKFPNVHSRVRISSSTPVVEDTQS -> DLRNQPYRRADAVRRSV
FT RRRFDDQNLRSVNGAEITM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025889"
FT VAR_SEQ 1056..1067
FT /note="ALKKNNITKFPN -> VLETNPTDEPMR (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025890"
FT VAR_SEQ 1068..1086
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025891"
FT CONFLICT 557..591
FT /note="Missing (in Ref. 2; AAP87551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1086 AA; 123101 MW; 0E5BBC192FCF8ACA CRC64;
MGNAGSMDSQ QTDFKAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK
WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG
WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTMES TVDKSKPWSR 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 IAILPVMASG TLSTGSELAV GNYVGSVPGA TTSGPSVPPP PPLPPSSDTS
EAAQNGTASP PMSPPPPPPP PPPPPPPPPP PLPGPAAETS PAPPLPPPPP PSAPPLPGTS
SPTVVFNSGL AAVKIKKPIK TKFRMPVFNW VALKPNQING TVFNEIDDER ILEDLNVDEF
EEIFKTKAQG PAIDLSSSKQ KITQKASSKV TLLEANRAKN LAITLRKAGK SADEICKAIH
VFDLKTLPVD FVECLMRFLP TENEVKVLRL YERERKPLEN LSDEDRFMMQ FSKIERLLQK
MTIMAFIGNF TESIQMLTPQ LHAIIAASVS IKSSQKLKKI LEIILALGNY MNSSKRGAVY
GFKLQSLDLL LDTKSTDRKQ TLLHYISNVV KEKYQQVTLF YNELHYVEKA AAVSLENVLL
DVKELQRGMD LTKREYTMHD HNTLLKEFLL HNEGKLKKLQ EDAKIAQDAF DDVVKYFGEN
PKTTPPSVFF PVFVRFVKAY KQAEEENELR KKQEQALMEK LLEQEALMEQ QDAKSPSHKS
KRQQQELIAE LRRRQVKDNR HVYEGKDGAI EDIITALKKN NITKFPNVHS RVRISSSTPV
VEDTQS
