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Database: UniProt
Entry: A0A3Q4HF62_NEOBR
LinkDB: A0A3Q4HF62_NEOBR
Original site: A0A3Q4HF62_NEOBR 
ID   A0A3Q4HF62_NEOBR        Unreviewed;      1015 AA.
AC   A0A3Q4HF62;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Formin-like protein 2-like {ECO:0000313|Ensembl:ENSNBRP00000020591.1};
GN   Name=FMNL2 {ECO:0000313|Ensembl:ENSNBRP00000020591.1};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000020591.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000020591.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC       {ECO:0000256|ARBA:ARBA00023449}.
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DR   AlphaFoldDB; A0A3Q4HF62; -.
DR   STRING; 32507.ENSNBRP00000020591; -.
DR   Ensembl; ENSNBRT00000021148.1; ENSNBRP00000020591.1; ENSNBRG00000015789.1.
DR   GeneTree; ENSGT00940000155515; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000015789; Expressed in camera-type eye and 6 other cell types or tissues.
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:0060857; P:establishment of glial blood-brain barrier; IEA:Ensembl.
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; 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   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580}.
FT   DOMAIN          22..469
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          620..1011
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          488..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..478
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          900..954
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        525..544
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..594
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1015 AA;  114861 MW;  99A856787985A46E CRC64;
     MGNAGSMDHH TDLRGHNMPL KLPMPDAGEL EERFAIVLNS MNLPPDKARL LRQYDNEKKW
     ELICDQERFQ VKNPPHTYLQ KLRSYLDPAV TRKKFRRRVQ ESTQVLRELE ISLRTNHIGW
     VREFLNEENK GLDVLVDYLS FAQYAVTFDG ECLENNPEAA MDKSKPWSRS IEDLHGGSTL
     PSPITGNGIT RVGRHSTLRF NTLPSRRTLK NSRLVCKKDD VHVCIMCLRA IMNYQYGFNM
     VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCMEEQRF
     EKLMEYFKNE DNNIDFMVAC MQFINIVVHS VEDMNFRVHL QYDFTKLCLD DYLDKLKHTE
     SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHMTEKLQ DMENEAMAKI
     VELEKQLMQR NKELESIREV YKDASSQVHS LRQMLKEKDE AIQRQSKLEK KIHELEKQGT
     IKIHKKGDGD ISILTSPPSA TEGSPGAVIG GNGVAVSPNH VALMAGTPVP PPPPPPPPPL
     PMNGTLSNGP TSTIPAAAPP PPPPPPPPPP PPPGMPTETS APLPPPPPPV APPLPGCGTP
     TVIMNSGLAE GPIKLFSVKI KKPIKTKFRM PVFNWVALKP NQINGTVFNE IDDERILEDL
     NVDEFEEMFK TKAQGPPIDL TASKQKVIQK GPNKVALLDS NRAKNLAITL RKVGKTPEEI
     CKAIQLFDLR TLPVDFVECL MRFQPTENEI KVLRQFEKER KPLESLTDED RFMMQFSKIE
     RLMQKMTIMA FIGNFAESVQ MLTPQLHAVI AASVSIKSSQ KLKKILEIIL ALGNYMNSSK
     RGAVYGFKLQ SLDLLLDTKS TDRKQTLLHY IANVVKEKYT QVSLFYNEMH YVEKAAAVSL
     ENVLLDVKEL QRGMELTKRE YSMHGHNTML KEFIAHNESK LKKLQDDAKI AQDAFDEVVK
     FFGENAKTTP PSVFFPVFVR FVKAYRVSWI LASHIGQKQT KHTLLSMINS SLHFI
//
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