ID F6SZ26_CALJA Unreviewed; 1099 AA.
AC F6SZ26;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Diaphanous related formin 2 {ECO:0000313|Ensembl:ENSCJAP00000024889.4};
GN Name=DIAPH2 {ECO:0000313|Ensembl:ENSCJAP00000024889.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000024889.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000024889.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000024889.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR AlphaFoldDB; F6SZ26; -.
DR STRING; 9483.ENSCJAP00000024889; -.
DR Ensembl; ENSCJAT00000026314.4; ENSCJAP00000024889.4; ENSCJAG00000013479.5.
DR GeneTree; ENSGT00940000157822; -.
DR InParanoid; F6SZ26; -.
DR OMA; FHHCIES; -.
DR Proteomes; UP000008225; Chromosome X.
DR Bgee; ENSCJAG00000013479; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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; IPR014767; DAD_dom.
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; PS51231; DAD; 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:UP000008225}.
FT DOMAIN 98..464
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 629..1029
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT DOMAIN 1049..1079
FT /note="DAD"
FT /evidence="ECO:0000259|PROSITE:PS51231"
FT REGION 520..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 203..230
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 381..408
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1006..1047
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 546..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 125969 MW; 4398C4DA47FF3E17 CRC64;
XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXNIQIKT LADDVRDRIT
SFRKSTVKKE KPLIQHPIDS QVAMSEFPAA QPLYDERSLN LSEKEVLDLF EKMMEDMNLN
EEKKAPLRNK DFTTKREMVV QYISATAKSG GLKNSKHECT LSSQEYVHEL RSGISDEKLL
NCLESLRVSL TSNPVSWVNN FGHEGLGLLL DELEKLLDKK QQENIDKKNQ YKLIQCLKAF
MNNKFGLQRI LGDERSLLLL ARAIDPKQPN MMTEIVKILS AICIVGEENI LDKLLGAITT
AAERNNRERF SPIVEGLENQ EALQLQVACM QFINALVTSP YELDFRIHLR NEFLRSGLKT
MLPDLKEKEN NELDIQLKVF DENKEDDLTE LSHRLNDIRA EMDDMNEVYH LLYNMLKDTA
AENYFLSILQ HFLLIRNDYY IRPQYYKIIE ECVSQIVLHC SGMDPDFKYR QRLDIDFTHL
IDSCVNKAKV EESEQKAAEF SKKFDEEFTA RQEAQAELQK RDEKIKELEA EIQQLRTQAQ
VPSNSSRIPG PPPPPPLPGA GPPPPPPPPP LPGGAPPPPP PPPPPPLPGM AGIPPPPPLL
FGGPPPPPPL GGVPCPPGLS VDLPYGMKQK KIYKPEVSMK RINWSKVEPT ELSENCFWLK
VKEDKFENPD LFAKLALNFA TQIKVQKNAE TLEEKKTVPT KKKVKELRIL DPKTAQNLSI
FLGSYRMPYE EIRNIILEVK EDMLSEALIQ NLVKHLPEQK VLNELAELKD EYDDLCEPEQ
FGVVMSSVKM LQPRLSSILF KLTFEEHVNN IKPSIIAVTL ACEELKKSES FNRLLELVLL
VGNYMNSGSR NAQSLGFKIN FLCKIRDTKS ADQKTTLLHF IADICEEKYR DILKFPEELE
HVESASKVSA QILKSNLASM EQQIVLLERD IKKFPQAESQ HDKFVEKMTS FTKSAREQYE
KLSTMHNNML KLYENLGEYF IFDSKSVSIE EFFGDLNNFR TLFLRENNKR REMEEKTRRA
KLAKEKAEQE KLERQKKKKQ LIDINKEGDE TGVMDNLLEA LQSGAAFRDR RKRIPRNPDN
RRVPLERSRS RHNGAISSK
//
