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Database: UniProt
Entry: A0A3Q3BKB7_HAPBU
LinkDB: A0A3Q3BKB7_HAPBU
Original site: A0A3Q3BKB7_HAPBU 
ID   A0A3Q3BKB7_HAPBU        Unreviewed;      1105 AA.
AC   A0A3Q3BKB7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Formin-like protein 1 {ECO:0000313|Ensembl:ENSHBUP00000001366.1};
GN   Name=FMNL1 {ECO:0000313|Ensembl:ENSHBUP00000001366.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000001366.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000001366.1}
RP   IDENTIFICATION.
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; A0A3Q3BKB7; -.
DR   STRING; 8153.ENSHBUP00000001366; -.
DR   Ensembl; ENSHBUT00000013906.1; ENSHBUP00000001366.1; ENSHBUG00000002557.1.
DR   GeneTree; ENSGT00940000156292; -.
DR   OMA; AQKGPMM; -.
DR   Proteomes; UP000264840; Unplaced.
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; 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:SF2; FORMIN-LIKE PROTEIN 1; 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:UP000264840}.
FT   DOMAIN          46..480
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          657..1048
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          416..461
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        23..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        555..650
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1045
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  122909 MW;  298D91F514D239C9 CRC64;
     MGNAAGGGLE HEPAEGREAR NSVSAASAMN DSAPTLQKKQ PPQPKLPMPP EKELEERFNT
     VLSSMNLPPD KLQLLSQYDN EKKWELVCDQ ERFQVKSPPS TYLTKIKSLY QDQGGVSRRL
     KKRIQDATQV LKNLEISLRT NHIGWAQEFL NEQNKGLDVL VEYLSYAQSD SSFEVEAIEN
     GGSLSDRGKS AERSMEDLTK SSSSHQSHGM TRAARALTVR ISTTLVNKMH KKSHINNQRD
     DVHVCIMCLR AIMNYQSGFN LVMTHPRCVN EITLSLNSRN PRTKALVLEL LAAVCLVRGG
     HDIILSAFDN FKEVSKEKNR FEKLMEYFVN DDNNIDFMVA CMQFINIVVH SVENMNFRVH
     LQYEFTHLGL DKYLETLKLT ESEKLQVQIQ AYLDNVLDVG ALLEDAENRG GVLEHVDELQ
     EHNVQLSARL QEIENQTADR ITELETQLMQ ATKEAELLKE SLRESCSQVS TLQQRERERE
     LDREREKDRE RLGITGPQGP SELEQKIQEL QDKGLIRVGR TASGSLDVQV MPVTVVEYIQ
     SPAPANQASA PTSPSSSIPS PPPPPPLPGG SEQTVSPPPP PPSLPGGPAP PPPPPPPPPP
     PLSGSATAPP PPPPLPGTGP PPPPPPPGAG PPPPPPPPGG GPPPPPGAPS ADSGAKSRKP
     IQTKFRMPLL NWQALKPNQV TGTVFNELDD EQVLGELNME MFEEHFKTRA QGNPADLSKV
     KKKMTSKAPT KTSLIDGNKA KNLAITLRKG GMSPADICTA IEMYDQQSLS IDFLELLEPF
     IPSDFEMKLL ANYEKDGRPL DELTNEDQFM LRFGKIPRLN QRINTLTFMG NFPDSVKRLQ
     PQLNSIISAS MSLKSSTKLK KILEIVLAFG NYMNSSKRGA ACGFRLQSLD LLLDTKSTDR
     SQTLLHFITN IIQEKYPDLV NFHTELHFVD KAGLVSLDSI LQDIRSLERG MEMTKKEFLV
     QDDSPVLKEF IKTNSEQLDT LIKDSKTAQE AYGSVVEYFG ENPKTTQPSM FFPMFGRFIK
     AYKTAQQEIE QKKKMESESR EVKESPSPNK AGPQKGPMMP KMPQMDLIAE LKKRQVKPPV
     REGKDGALED IITGTVTCFL LENHF
//
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