GenomeNet

Database: UniProt
Entry: G3TTM8_LOXAF
LinkDB: G3TTM8_LOXAF
Original site: G3TTM8_LOXAF 
ID   G3TTM8_LOXAF            Unreviewed;       960 AA.
AC   G3TTM8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Formin like 2 {ECO:0000313|Ensembl:ENSLAFP00000018936.1};
GN   Name=FMNL2 {ECO:0000313|Ensembl:ENSLAFP00000018936.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000018936.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000018936.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018936.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000018936.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000018936.1};
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   AlphaFoldDB; G3TTM8; -.
DR   Ensembl; ENSLAFT00000032005.1; ENSLAFP00000018936.1; ENSLAFG00000001605.3.
DR   GeneTree; ENSGT00940000155515; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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; 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; 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; 1.
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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646}.
FT   DOMAIN          1..403
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          490..881
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          913..950
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          454..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          315..412
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          855..886
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        454..473
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   960 AA;  109950 MW;  A55C1E8889A1FD73 CRC64;
     QERFQVKNPP HTYIQKLKGY LDPAVTRKKF RRRVQESTQV LRELEISLRT NHIGWVREFL
     NEENKGLDVL VEYLSFAQYA VTFDFESVES TVESSMDKSK PWSRSIEDLH RGSNLPSPVG
     SSVSRSGRHS ALRYNTLPSR RTLKNSRLVS KKDDVHVCIM CLRAIMNYQY GFNMVMSHPH
     AVNEIALSLN NKNPRTKALV LELLAAVCLV RGGHEIILSA FDNFKEVCGE KQRFEKLMEH
     FRNEDNNIDF MVASMQFINI VVHSVEDMNF RVHLQYEFTK LGLDEYLDKL KHTESDKLQV
     QIQAYLDNVF DVGALLEDAE TKNAALERVE ELEENISHLS EKLQDTENEA MSKIVELEKQ
     LMQRNKELDV VREIYKDANT QVHTLRKMVK EKEEAIQRQS TLEKKIHELE KQGTIKIQKK
     GDGEIAILPV VASGTLPVGS EVAVAPLPGP AAETVPAPPL PPPPPPSAPP LPGTSSPTVV
     FNSGLAAVKI KKPIKTKFRM PVFNWVALKP NQINGTVFNE IDDERILEDL NVDEFEEIFK
     TKAQGPAIDL SSSKQKITQK GSNKVTLLEA NRAKNLAITL RKAGKTADEI CKAIHVFDLK
     TLPVDFVECL MRFLPTENEV KVLRLYERER KPLENLSDED RFMMQFSKIE RLMQKMTIMA
     FIGNFAESIQ MLTPQLHAVI AASVSIKSSQ KLKKILEIIL ALGNYMNSSK RGAVYGFKLQ
     SLDLLLDTKS TDRKQTLLHY ISNVVKEKYH QVSLFYNELH YVEKAAAVSL ENVLLDVKEL
     QRGMDLTKRE YTMHDHNTLL KDFILNNEGK LKKLQDDAKI AQDAFDDVVK YFGENPKTTP
     PSVFFPVFVR FVKAYKQAEE ENELRKKQEQ ALMEKLLEQE ALMEQQDPKS PSHKSKRQQQ
     ELIAELRRRQ VKDNRHVYEG KDGAIEDIIT VLKTVPFTAR TAKRGSRFFC EPVLTEEYHY
//
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