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Database: UniProt
Entry: M3XSK9_MUSPF
LinkDB: M3XSK9_MUSPF
Original site: M3XSK9_MUSPF 
ID   M3XSK9_MUSPF            Unreviewed;      1019 AA.
AC   M3XSK9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Diaphanous related formin 2 {ECO:0000313|Ensembl:ENSMPUP00000002059.1};
GN   Name=DIAPH2 {ECO:0000313|Ensembl:ENSMPUP00000002059.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000002059.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000002059.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR   EMBL; AEYP01088041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01088050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3XSK9; -.
DR   STRING; 9669.ENSMPUP00000002059; -.
DR   Ensembl; ENSMPUT00000002102.1; ENSMPUP00000002059.1; ENSMPUG00000002080.1.
DR   eggNOG; KOG1924; Eukaryota.
DR   GeneTree; ENSGT00940000157822; -.
DR   HOGENOM; CLU_002356_0_0_1; -.
DR   InParanoid; M3XSK9; -.
DR   OMA; FHHCIES; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        951..984
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        996..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          87..460
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          627..1019
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          377..404
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          507..534
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        29..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..591
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1019 AA;  115488 MW;  4D9D7B474057DEB0 CRC64;
     MEQPGAAATG AGGGSEEPGG GRSNKRSAGN RAANEEETKN KPKLRDRITS FRKSTVKKEK
     PLIQHPIDSQ VTMSEFPAAQ PLYDERSLNL SEKEVLDLFE KMMEDMNLNE DRKAPLRNKD
     FTTKREMVVQ YISATAKSIV GSKVMGGLKN SKHECTLSSQ EYVHELRSGI SDEKLLNCLE
     SLRVSLTSNP VSWVNNFGHE GLGLLLDVLE KLLDKKQQEN IDKKNQYKLI QCLKAFMNNK
     FGLQRILGDE RSLLLLARAI DPKQPNMMTE IVKILSAICI VGEENILDKL LGAITTAAER
     NNRERFSPIV EGLENHEALQ LQVACMQFIN ALVTSPYELD FRIHLRNEFL RSGLKTMLPD
     LKEKENDELD IQLKVFDENK EDDLNELSHR LNDIRAEMDD MNEVYHLLYN MLKDTAAENY
     LLSILQHFLL IRNDYYIRPQ YYKIIEECVS QIVLHCSGMD PDFKYRQRLD VDFTHLIDSC
     VNKAKVEESE QKAVEFSKKF DEEFTARQEA QAELQRREEK IKELETEIQQ LRTQGYGLSG
     SSGIPGPPPP PLLPGGGSSP PPPPPPPPPA PPLPGGALPP PPPPLPGMIG IPPPPPLFGG
     PPPPFPLGGG ILPFPEVPLD LPYGMKQKKL YKPEVPMKRI NWSKIEPKEL SENCFWLKVK
     EDKFENPDLF AKLALNFATQ MKVQKNVEAS EEKKILPAKK KVKELRILDP KTAQNLSIFL
     GSYRMPYEDI KNIILEVNED MLNEALIQNL VKHLPEQKVL SELAQLRNEY HDLCEPEQFG
     VVMSSVKMLQ PRLENILFKL TFEEHVNNIK PSIIAVTLAC EELKKSESFN RLLELVLLVG
     NYMNSGSRNA QSLGFKINFL CKIRDTKSAD QKTTLLHFIA EICEEKYRDI LKFPDELEHV
     ESASKVSAQI LKSNLTAMEQ QIINLERDIK KFPETEDQHD KFVEKMTISF IYSSILFISF
     SLNLFLSLSL SASVCVCVCV CVCVRLHARA CKCTHAYAQG ICIYCVVLNL PVYLFRLSA
//
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