ID A0A3P8XS60_ESOLU Unreviewed; 936 AA.
AC A0A3P8XS60;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Formin-like 3 {ECO:0000313|Ensembl:ENSELUP00000007305.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000007305.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000007305.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000007305.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family.
CC {ECO:0000256|ARBA:ARBA00023449}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P8XS60; -.
DR STRING; 8010.ENSELUP00000007305; -.
DR Ensembl; ENSELUT00000007482.2; ENSELUP00000007305.2; ENSELUG00000008108.2.
DR GeneTree; ENSGT00940000159962; -.
DR Proteomes; UP000265140; LG12.
DR Bgee; ENSELUG00000008108; Expressed in heart and 14 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: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:SF3; FORMIN-LIKE PROTEIN 3; 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; 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:UP000265140}.
FT DOMAIN 1..377
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 463..853
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 402..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..358
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 824..851
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 419..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..936
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 936 AA; 107009 MW; FD8E2217273E5A79 CRC64;
VCHLGHAENS MNLPPDKARL LRQYDNEKKW DLICDQERFQ VKNPPHTYIS KLRSYLDPGV
TRKKFRRRVQ ESTKVLRELE ISLRTNHIGW VREFLNNENR GLDILVEYLS FAQCAVMYGV
APNNKTIKNS RLVSQKDDVH VCIMCLRAIM NYQYGFNLVM SHEHAVNEIA LSLNNKNSRT
KALVLELLAA VCLVRGGHEI ILSAFDNFKE VCKEKHRFEK LMEYFRVEDG NIDFMVACMQ
FINIVVHSVE DMNFRVHLQY EFTKLGLDDY LEKSKHTESD KLSVQIQAYL DNVFDVGGLL
EDAETKNVAL EKVEELEEHL SHVTEKLLDV ENETIMKVAD LEKQLLQKDK DLQVIRETYE
STNTQVNTLR RMIKEKDAAF QRHFNIEKRL LELEQQGTIR LRHSVGPAGP GGPGTSLPSA
SEAPPPPPPP PPPPPLPSAS GTVPPAATLF SAVDLLVAHS IRIKKPIKTK FRLPIFNWTA
LKPNQINGTV FSEIDDERVL EELDVERFEE LFKTKAQGPV VDLSGPKTKV SQKAANKVSL
LDANRSKNLA ITLRKANKST EEICKAIQTF DLKALPVDFV ECLMRFLPTE AEVKLMRQYE
RERRPLDVLT DEDRFMLFFS KIERLTQRMN IITFVGNFSE NINMLTPQLN AIIASSASVK
SSPKLKRMLE IILALGNYMN SGKRGSVYGF KLQSLDLLLD TKSTDRKMTL LHYIAVVVKE
KYPELANFYN ELHFVDKAAA VSLENVLLDV RELGKGMDLI RRECSLHDHS VLKGFLQTSE
TQLDKLQKDA KTAEEAFNNV VNYFGESSKT TPPSVFFPVF VRFIRAYKDA VEDNEQRKKQ
EEAMREKLLA QEAKQHDPKA VKKRQQQHEL IAELRKRQAK DHRPVYEGKD GTIEDIITGG
LDMQPRRQPR SPQPGPSRTA TVPHGRHRRA CGQAIR
//
