ID   FGD1_MOUSE              Reviewed;         960 AA.
AC   P52734; Q921L2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=FYVE, RhoGEF and PH domain-containing protein 1;
DE   AltName: Full=Faciogenital dysplasia 1 protein homolog;
DE   AltName: Full=Rho/Rac guanine nucleotide exchange factor FGD1;
DE            Short=Rho/Rac GEF;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 3;
GN   Name=Fgd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8535076; DOI=10.1007/bf00352375;
RA   Pasteris N.G., de Gouyon B., Cadle A.B., Campbell K., Herman G.E.,
RA   Gorski J.L.;
RT   "Cloning and regional localization of the mouse faciogenital dysplasia
RT   (Fgd1) gene.";
RL   Mamm. Genome 6:658-661(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBNL AND CTTN, AND
RP   MUTAGENESIS OF PRO-159; PRO-162 AND LYS-164.
RX   PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA   Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B., Gorski J.L.;
RT   "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT   interacts with cortactin and mAbp1 to modulate cell shape.";
RL   Hum. Mol. Genet. 12:1981-1993(2003).
RN   [5]
RP   POSSIBLE INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/mcb.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the Rho
RT   guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710 AND SER-714, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Heart;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and
CC       Rac proteins, by exchanging bound GDP for free GTP. Plays a role in
CC       regulating the actin cytoskeleton and cell shape.
CC       {ECO:0000269|PubMed:12913069}.
CC   -!- SUBUNIT: Interacts with DBNL/ABP1 and CTTN. Binds CDC42 (By
CC       similarity). May interact with CCPG1. {ECO:0000250,
CC       ECO:0000269|PubMed:12913069}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12913069}. Cell
CC       projection, lamellipodium {ECO:0000269|PubMed:12913069}. Cell
CC       projection, ruffle {ECO:0000269|PubMed:12913069}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:12913069}. Note=Associated with
CC       membrane ruffles and lamellipodia.
CC   -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U22325; AAA96001.1; -; mRNA.
DR   EMBL; AL805937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011462; AAH11462.1; -; mRNA.
DR   CCDS; CCDS30467.1; -.
DR   RefSeq; NP_032027.2; NM_008001.4.
DR   AlphaFoldDB; P52734; -.
DR   SMR; P52734; -.
DR   BioGRID; 199637; 2.
DR   IntAct; P52734; 2.
DR   MINT; P52734; -.
DR   STRING; 10090.ENSMUSP00000026296; -.
DR   iPTMnet; P52734; -.
DR   PhosphoSitePlus; P52734; -.
DR   jPOST; P52734; -.
DR   MaxQB; P52734; -.
DR   PaxDb; 10090-ENSMUSP00000026296; -.
DR   ProteomicsDB; 271562; -.
DR   Pumba; P52734; -.
DR   Antibodypedia; 376; 85 antibodies from 21 providers.
DR   DNASU; 14163; -.
DR   Ensembl; ENSMUST00000026296.8; ENSMUSP00000026296.8; ENSMUSG00000025265.15.
DR   GeneID; 14163; -.
DR   KEGG; mmu:14163; -.
DR   UCSC; uc009uow.2; mouse.
DR   AGR; MGI:104566; -.
DR   CTD; 2245; -.
DR   MGI; MGI:104566; Fgd1.
DR   VEuPathDB; HostDB:ENSMUSG00000025265; -.
DR   eggNOG; KOG4424; Eukaryota.
DR   GeneTree; ENSGT00940000159438; -.
DR   InParanoid; P52734; -.
DR   OMA; QQRWMAV; -.
DR   OrthoDB; 5385125at2759; -.
DR   PhylomeDB; P52734; -.
DR   TreeFam; TF316247; -.
DR   Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   BioGRID-ORCS; 14163; 6 hits in 75 CRISPR screens.
DR   ChiTaRS; Fgd1; mouse.
DR   PRO; PR:P52734; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; P52734; Protein.
DR   Bgee; ENSMUSG00000025265; Expressed in rostral migratory stream and 240 other cell types or tissues.
DR   ExpressionAtlas; P52734; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0046847; P:filopodium assembly; ISO:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR   CDD; cd15741; FYVE_FGD1_2_4; 1.
DR   CDD; cd01219; PH1_FGD1; 1.
DR   CDD; cd13236; PH2_FGD1-4; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR035941; FGD1-4_PH2.
DR   InterPro; IPR035939; FGD1_PH1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR   PANTHER; PTHR12673:SF79; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   Genevisible; P52734; MM.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..960
FT                   /note="FYVE, RhoGEF and PH domain-containing protein 1"
FT                   /id="PRO_0000080941"
FT   DOMAIN          372..560
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          589..688
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          820..920
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         729..789
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          1..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          226..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          701..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          922..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           171..187
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        132..190
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..254
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..299
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..351
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         735
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         738
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         752
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         755
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         760
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         763
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         781
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         784
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P98174"
FT   MOD_RES         205
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P98174"
FT   MOD_RES         710
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MUTAGEN         159
FT                   /note="P->A: Abolishes binding to DBNL."
FT                   /evidence="ECO:0000269|PubMed:12913069"
FT   MUTAGEN         162
FT                   /note="P->A: Abolishes binding to DBNL."
FT                   /evidence="ECO:0000269|PubMed:12913069"
FT   MUTAGEN         164
FT                   /note="K->E: No effect on binding to DBNL."
FT                   /evidence="ECO:0000269|PubMed:12913069"
FT   CONFLICT        504
FT                   /note="G -> R (in Ref. 1; AAA96001)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        633
FT                   /note="S -> T (in Ref. 1; AAA96001)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   960 AA;  106365 MW;  E3E489BA2F3AE056 CRC64;
     MHGHRVPGGP GPSDPERSAA NTPGAAPLAC ADSDPGALEP GLPVSRGSGT ALGGPLDPQF
     VGPSDASLGA PPSSRVLPCG PSPQHHRALR FSYHLEGSQP RPGLHQGNRI LVKSLSLDPG
     QSLEPHPEGP QRLRSDPGPP TEIPGPRPSP LKRAPGPKPQ VPPKPSYLQM PRVLPPPEPI
     PPPPSRPLPA DPRVAKGLVP RAEASTSSAA VSSLIEKFER EPVIVASDRP APGPCPVPPE
     PAMLPQPPPQ PTGSQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
     SDDGPPIHSL CPGPPALASM PVALADPHRP GSQEVDSDLE EEEEEEEEEK EREIPVPPME
     RQESVELTVQ QKVFHIANEL LQTEKAYVSR LHLLDQVFCA RLLEEARNRS SFPADVVHGI
     FSNICSIYCF HQQFLLPELE KRMEEWDRYP RIGDILQKLA PFLKMYGEYV KNFDRAVELV
     NTWTERSTQF KVIIHEVQKE EACGNLTLQH HMLEPVQRIP RYELLLKDYL LKLPHGSPDS
     KDAQKSLELI ATAAEHSNAA IRKMERMHKL LKVYELLGGE EDIVSPTKEL IKEGHILKLS
     AKNGTTQDRY LILFNDRLLY CVPRLRLLGQ KFSVRARIDV DGMELKESSN LNMPRTFLVS
     GKQRSLELQA RTEEEKKDWV QAINSTLLKH EQTLETFKLL NSTNRDDEDT PPNSPNVDLG
     KRAPTPIREK EVTMCMRCQE PFNSITKRRH HCKACGHVVC GKCSEFRARL IYDNNRSNRV
     CTDCYVALHG APGSSPACSQ HTPQRRRSIL EKQASVAAEN SVICSFLHYM EKGGKGWHKA
     WFVVPENEPL VLYIYGAPQD VKAQRSLPLI GFEVGPPEAG ERPDRRHVFK ITQSHLSWYF
     SPETEELQRR WMAVLGRAGR GDTFCPGPTL SEDKEMEETP VAASGATAEP PEASQTRDKT
//