ID A0A3Q0S507_AMPCI Unreviewed; 1085 AA.
AC A0A3Q0S507;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Formin-like 1a {ECO:0000313|Ensembl:ENSACIP00000015500.1};
GN Name=FMNL1 {ECO:0000313|Ensembl:ENSACIP00000015500.1};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000015500.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000015500.1}
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; A0A3Q0S507; -.
DR STRING; 61819.ENSACIP00000015500; -.
DR Ensembl; ENSACIT00000015911.1; ENSACIP00000015500.1; ENSACIG00000011998.1.
DR GeneTree; ENSGT00940000156292; -.
DR OMA; AQKGPMM; -.
DR Proteomes; UP000261340; 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; 1.
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; 1.
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}.
FT DOMAIN 46..496
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 621..1012
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 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..152
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 454..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 121401 MW; E6FE3A9F7874915D CRC64;
MGNAAGGGLE HEPAEGREAR NSVGTASTMS DPAPALQKKQ PPQPKLPMPP EKELEELMFR
LNSKFCYVLS CMNLPPDKLE LLSQYDNEKK WELVCDQERF QVKSPPSTYL TKIKSFYQDQ
GGVSRRVCRK KKEKLKKKIQ DATQVLKNLE ISLRTNHIGW AQEFLNEQNK GLDVLVEYLS
YAQSDSSVEN GGILSDKGKS AERSMEDLTK SSSSHQSHGM SRAARALTVS KIHRKSHLNN
QRDDVHVCIM CLRAIMNYQS GFNLVMTHPR CVNEITLSLN SRNPRTKALV LELLAAVCLV
RGGHDIILSA FDNFKEVSKE KNRFEKLMEY FVHDDNNIDF MVACMQFINI VVHSVENMNF
RVHLQYEFTH LGLDKYLETL KLTESEKLQV QIQAYLDNVL DVGALLEDAE HRGGVLEHVD
ELHEHNLNSR LQEIESQTAE RISELETQLM QATKEGELER ELDREREKDR ERLGVAGPQA
PSELEQKIQE LQDQGLIRLG RTASGNLDIQ VVPVTVVEYV QSSAPATQPS APDAVDSTSS
QSGLPSSAPI PPPPPPGGSE HTVSPPPPPP PPPPPPSLPG GPAPPPPPPP PPPGVCPPPP
PPPPGAGPPP PPPPPGAGIK SRKPIQTKFR MPLLNWQALK PNQVTGTVFN ELDDEQILGE
LNMEMFEEQF KTRAQGNSAD LSKIKKKTAN KAPTKTSLID ANKAKNLAIT LRKGGMSPAK
ICTAIETYDQ QSLSIDFLEL LEPFIPSDFE MKLLKNYEKD GRPLDELTDE DQFILRFGKI
PRLNQRINTL TFMGNFPDTV KRLQPQLNSI IAASMSLKSS DKLKKILEIV LAFGNYMNSS
KRGAACGFRL QSLDLLLETK STDRSQTLLH FITNIIQEKY PDLVNFHTEL HFVDKAALVS
LDGILQDIRS LERGMEMTKK EFLVQDDSPV LKEFIKTNSE QLDTLIKDSK TAQEAYGSVV
EYFGENPKTT QPSMFFPMFG RFLKAYKTAQ QELEQKKKME SEMREVKESP SPNKAGSQKM
DLIAELKKRQ VKPPVREGKD GALEDIITDL RNSPYRRADG RRGLNPPPGH FLHVFPRLSL
PAFLS
//
