ID W5NIN5_LEPOC Unreviewed; 1412 AA.
AC W5NIN5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Formin 2 {ECO:0000313|Ensembl:ENSLOCP00000020494.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000020494.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000020494.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC subfamily. {ECO:0000256|ARBA:ARBA00005271}.
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DR EMBL; AHAT01001713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000020494; -.
DR Ensembl; ENSLOCT00000020529.1; ENSLOCP00000020494.1; ENSLOCG00000016592.1.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000154289; -.
DR HOGENOM; CLU_002670_2_0_1; -.
DR InParanoid; W5NIN5; -.
DR OMA; CNQNAQS; -.
DR Proteomes; UP000018468; Linkage group LG16.
DR Bgee; ENSLOCG00000016592; Expressed in ovary and 10 other cell types or tissues.
DR GO; GO:0005884; C:actin filament; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR001265; Formin_Cappuccino_subfam.
DR PANTHER; PTHR13037; FORMIN; 1.
DR PANTHER; PTHR13037:SF16; FORMIN-2; 1.
DR Pfam; PF02181; FH2; 1.
DR PRINTS; PR00828; FORMIN.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 973..1388
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 651..685
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..836
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 154565 MW; 93B52708B0D03DF9 CRC64;
MGNQDGKLKR AAGESSEATE EAGGPREVEH TKKGLHGKKA HGKHGKGGDS SKKKSKSESK
ASVFSNIRLR KNLSKAKGLS GGSKEDVLET QASQQDELDS ALSIQTKTPD ISLSADELGL
SDTEAERFHL TMESRQATVE TQEGQRASSG SDTDIYSFHS AAEQEDLLSD IQHTIRMQQG
VIISAAEEPS WIAEYKHAGD VKTTPPDSEH VADQEAAFNW ENGHVGELHV SLDSARQESN
LTADVQNGLS EASSKSEKSF CTSPGTKEHK PPSESAQPPA EASGGRGGSP VVTATTANSV
PDLTASFESV EGPEEEEAKV DISSLLKESR AELDGSHEAA LDSSDGTVDG SLELKAEGDD
EDPTVPHRKS SVPFSQWHPE SPLSRLLRTS LTSTSSPTVK PYPPIHPSYI KTTTRQLSSP
NHSPGPSPSQ SPLFRRRYCD LGHRPDRRRV KKQRSSSITG PLSRSADWTD ELSKFRSNKT
GSADYLEYGG SEERLRGGSQ PLCVTRKSSG VQASTCSFHD VFTGRTLLEK FFKQQEDAPP
EEAEKLCSRI LAMGLLLPFS DCFREQYGES TSQVTPKFDQ DQLYTWAAVS QPTHSFDPVE
GRVPGRIQAL WPPPKSGVEE KPGLKYTEAV HAVNRILVLR EESVLKTVKL KEEHVNVIQQ
LEQTIEDLRT KIAELEKQYT PLERDICTKD QECGSGEVAF KDFCDVDLQT EEQIMLSSLE
AKSVQTSPVE ESFKFKVPLQ DGMSSSSSVL PNGTDSVPQL QLGTDTPTYH SEISLVLSPK
TTQGFVCMCQ QQQQPSLPPA SGQSGIQAYP APLPGLPIPP PPPPPPPPPP PPPPPPPLPG
VSVPPPPPLP GCAVPPPPPP PPLPGCAVPP PPPPPPLPGC AVPPPPPPPP LPGCAVPPPP
PPPPLPGAPV PPPPPPPLPG SCPPPPPPLP GMMPPSAPGS AGPPPPPPPF GSLPPPLPAG
LFALGMAQDR GSRKTMIEPP RPMKPLYWTR IQLHARKESS GPLVWEKIEE PSVDFNEFVE
LFSKTAVKEK KKPLSDTYTK SKAKQVVKLL NNKRSQAVGI LMSSLHLDMK DIQQAVLNLD
NTVVDLETLQ ALYENRAQQE EMDKIEKHVK STKEKENSKP LDKPEQFLYE LSQIPNFSSR
VFCIIFQSSF MECISSIVRK LEILQKVCSS LQSSAGVMKI LGLVLAFGNF MNGGNRTRGQ
ADGFALDILP KLNDVKSSDS SRSLLSYIVS YYLRHFDEDA GRESCLFPLP EPQDLFQASQ
MKFEDFQKDL RKLRKDLNAC TTETEKVCRD SSEDHLQPFK NKMEEFLGQA KVDLELQETQ
LTVAHKSFLE LTVFFSVKPK MAEKEVSPNT FFSLWHEFCT DFKDLWKKEN KLILQERLRE
AEECFRQAKE KASYNVRPKH DSGIKAKLSM KI
//