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Database: UniProt
Entry: G3QJM9_GORGO
LinkDB: G3QJM9_GORGO
Original site: G3QJM9_GORGO 
ID   G3QJM9_GORGO            Unreviewed;      1184 AA.
AC   G3QJM9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Diaphanous related formin 1 {ECO:0000313|Ensembl:ENSGGOP00000002628.3};
GN   Name=DIAPH1 {ECO:0000313|Ensembl:ENSGGOP00000002628.3};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000002628.3, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000002628.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000002628.3, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000002628.3}
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   EMBL; CABD030041382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030041383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030041384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030041385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030041386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3QJM9; -.
DR   Ensembl; ENSGGOT00000002682.3; ENSGGOP00000002628.3; ENSGGOG00000002660.3.
DR   eggNOG; KOG1924; Eukaryota.
DR   GeneTree; ENSGT00940000159910; -.
DR   HOGENOM; CLU_002356_0_0_1; -.
DR   TreeFam; TF315383; -.
DR   Proteomes; UP000001519; Chromosome 5.
DR   Bgee; ENSGGOG00000002660; Expressed in liver and 5 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   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:SF4; PROTEIN DIAPHANOUS HOMOLOG 1; 1.
DR   Pfam; PF06346; Drf_FH1; 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:UP000001519}.
FT   DOMAIN          40..401
FT                   /note="GBD/FH3"
FT                   /evidence="ECO:0000259|PROSITE:PS51232"
FT   DOMAIN          677..1083
FT                   /note="FH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51444"
FT   DOMAIN          1106..1134
FT                   /note="DAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51231"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          426..520
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          950..977
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1060..1104
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..584
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..658
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  132619 MW;  A5BCE1C1F27D73AF CRC64;
     MADELERFTS MRIKKEKEKP NSAHRNSSAS YGDDPTAQSL QDVSDEQVLV LFEQMLLDMN
     LNEEKQQPLR EKDIIIKREM VSQYLYTSKA GMSQKESSKS AMMYIQELRS GLRDMPLLSC
     LESLRVSLNN NPVSWVQTFG AEGLASLLDI LKRLHDEKEE TAGSYDSRNK HEIIRCLKAF
     MNNKFGIKTM LETEEGILLL VRAMDPAVPN MMIDAAKLLS ALCILPQPED MNERVLEAMT
     ERAEMDEVER FQPLLDGLKS GTTIALKVGC LQLINALITP AEELDFRVHI RSELMRLGLH
     QVLQLRFLTT EDTFGVQLNV FDEQGEEDSY DLKGRLDDIR MEMEYPFILL NTVRDSNAEP
     HFLSILQHLL LVRNDYEARP QYYKLIEECI SQIVLHKNGA DPDFKCRHLQ IEIEGLIDQM
     IDKTKVEKSE AKAAELEKKL DSELTARHEL QVEMKKMESD FEQKLQDLQG EKDALHSEKQ
     QIATEKQDLE AEVSQLTGEV AKLTKELEDA KKEMASLSAA AITVPPSVPS RAPVPPAPPL
     PGDSGTIIPP PPAPGDSTAI SPPPPLSGDA TISPPPPLPE GVGIPSPSSL PGGTAIPPPP
     PLPGSAGIPP PPPPLPGEAG MPPPPPPLPG GPGIPPPPPF PGGPGIPPPP PGMGMPPPPP
     FGFGVPAAPV LPFGLTPKKL YKPEVQLRRP NWSKLVAEDL SQDCFWTKVK EDRFENNELF
     AKLTLTFSAQ TKTKKDQEGG EEKKSVQKKK VKELKVLDSK TAQNLSIFLG SFRMPYQDIK
     NVILEVNEAV LTESMIQNLI KQMPEPEQLK MLSELKDEYD DLAESEQFGV VMGTVPRLRP
     RLNAILFKLQ FSEQVENIKP EIVSVTAACE ELRKSESFSS LLEITLLVGN YMNAGSRNAG
     AFGFNISFLC KLRDTKSTDQ KMTLLHFLAE LCENDYPDVL KFPDELAHVE KASRVSAENL
     QKNLDQMKKQ ISDVERDVQN FPAATDEKDK FVEKMTISSL ERRDFVKDAQ EQYNKLRMMH
     SNMETLYKEL GEYFLFDPKK LSVEEFFMDL HNFRNMFLQA VKENQKRRET EEKMRRAKLA
     KEKAEKERLE KQQKREQLID MNAEGDETGV MDSLLEALQS GAAFRRKRGP RQANRKAGCA
     VTSLLASELT KDDAMAAVPA KVSKNSETFP TILEEAKELV GRAS
//
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