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Database: UniProt
Entry: A2AQW2_MOUSE
LinkDB: A2AQW2_MOUSE
Original site: A2AQW2_MOUSE 
ID   A2AQW2_MOUSE            Unreviewed;      1085 AA.
AC   A2AQW2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=Formin-like 2 {ECO:0000313|Ensembl:ENSMUSP00000117822.3};
GN   Name=Fmnl2 {ECO:0000313|Ensembl:ENSMUSP00000117822.3,
GN   ECO:0000313|MGI:MGI:1918659};
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 {ECO:0000313|Ensembl:ENSMUSP00000117822.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000117822.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117822.3,
RC   ECO:0000313|Proteomes:UP000000589};
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] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000313|Ensembl:ENSMUSP00000117822.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000117822.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   RefSeq; XP_006498398.1; XM_006498335.3.
DR   AlphaFoldDB; A2AQW2; -.
DR   SMR; A2AQW2; -.
DR   jPOST; A2AQW2; -.
DR   PeptideAtlas; A2AQW2; -.
DR   ProteomicsDB; 361603; -.
DR   Antibodypedia; 10309; 127 antibodies from 25 providers.
DR   DNASU; 71409; -.
DR   Ensembl; ENSMUST00000155586.9; ENSMUSP00000117822.3; ENSMUSG00000036053.18.
DR   GeneID; 71409; -.
DR   AGR; MGI:1918659; -.
DR   CTD; 114793; -.
DR   MGI; MGI:1918659; Fmnl2.
DR   VEuPathDB; HostDB:ENSMUSG00000036053; -.
DR   GeneTree; ENSGT00940000155515; -.
DR   HOGENOM; CLU_103503_0_0_1; -.
DR   OrthoDB; 471257at2759; -.
DR   ChiTaRS; Fmnl2; mouse.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000036053; Expressed in indifferent gonad and 225 other cell types or tissues.
DR   ExpressionAtlas; A2AQW2; baseline and differential.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:InterPro.
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; IPR014767; DAD_dom.
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   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; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Proteomics identification {ECO:0007829|MaxQB:A2AQW2,
KW   ECO:0007829|PeptideAtlas:A2AQW2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          23..469
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          615..1006
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1038..1075
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          520..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          980..1011
FT                   /evidence="ECO:0000256|SAM:Coils"
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"
SQ   SEQUENCE   1085 AA;  123194 MW;  2AF842067C197342 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 EDIITVLKTV PFTARTAKRG SRFFCEPVLT
     EEYHY
//
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