ID A0A493U467_ANAPP Unreviewed; 1085 AA.
AC A0A493U467;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Diaphanous related formin 2 {ECO:0000313|Ensembl:ENSAPLP00000032916.1};
GN Name=DIAPH2 {ECO:0000313|Ensembl:ENSAPLP00000032916.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000032916.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000032916.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000032916.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR AlphaFoldDB; A0A493U467; -.
DR Ensembl; ENSAPLT00000034199.1; ENSAPLP00000032916.1; ENSAPLG00000003882.2.
DR GeneTree; ENSGT00940000157822; -.
DR Proteomes; UP000016666; Chromosome 10.
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 Gene3D; 1.20.58.630; -; 1.
DR Gene3D; 6.10.30.30; -; 1.
DR Gene3D; 1.10.20.40; Formin, diaphanous GTPase-binding domain; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous 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; IPR044933; DIA_GBD_sf.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR PANTHER; PTHR45691:SF3; PROTEIN DIAPHANOUS HOMOLOG 2; 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|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT DOMAIN 95..461
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 700..1085
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 981..1008
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 26..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 121944 MW; 21EE0A2E446D3965 CRC64;
MEGQGAPGAG GGGEEPLGSG RMNPKRGGRA AEEESRNKPK LNIQIKTLAD DVRDRITSFR
KSAVKKEKPL IQHPIDAQPT ISEIPLSQAL VDERCMNLSE KEVMDLFEKM MEDMNLNEDR
KAPLRDKDLT TKREMVVQYI SATAKSGGLK NSKHECTLSS QEYIHELRSG IAEEKLLNCL
ESLRVSLTSN PVSWVNNFGH EGLGLMLDVL ERLLDKKQQE NIDKKNQHKL IQCLKAFMNN
KYGLQRILGD ERSLLLLSRA IDPRQPHMMT ETVKILSALC IVGEENMLDK LLGAITTAAE
RNNRERFSQI VEGLENHEFL QLQVACMQLI NALVTSPEEL DFRIHLRNEF LRCGLKKILP
ALKDKENEEL DIQLKVFDEN KDEDLIELSH RLNDIRAEMD DMNEVFHLLY NMLKDTTSEG
YLLSILQHFL LIRNDYYVRP QYYKIIEECV SQIVLHSSGM DPDFKCRGRM DVDFTHLVDA
CVDKAKVEES EKKAAEFSRK FDEEFTARQE AQAELQKREE KIKELETEIK QLRTQAPVQT
SQQREAAPLP PIPTENVTPP PPAPPPPPPL PGEAVPPPPP PPPPPPLPGT QAVPPSLTLS
AVVPPPPPLP GTTPIPPPPP PLPGAGSTPP PPPPLPGAVL PPPPPPLPGG SLPPPPPPLP
GAAVPPPPPL FGGPPMPPPL GGVPFAPFAV IPALPHGMKE KKKYKLEVSM KRINWSKVEP
QEIAESSFWV KAEEDKFESP ELFAKLAITF GTQVKAKKAI EETEEKKVAQ SKKKIKELRV
LDGKTAQNLS IFLGSFRLPY EEIKNIILEV DEEKLSESLI QNLVKNLPEQ KELNALAELK
DEYNDLAESE QFGVVMSSVK MLRSRLNGIL FRLMFEEHVN NIKPDIMAVT MACEELKKSE
SFSRLLELVL FLGNYMNSGS RNAQSLGFNI SFLCKIRDTK STDQKTTLLH FLAEICEENY
RDILKFPDEL QHVESASKVS AQTLKSNLDS MNQQIQRLEN DIENFPKTQD EHDKFVEKMS
ISFLHVYTAD INVNFVWLSI SQHLKLSFKS LLPCFCSSGE KSMSEYAECK KTRKPLTKLN
LMFYS
//
