FGD3_PONAB
ID FGD3_PONAB Reviewed; 737 AA.
AC Q5R5T1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 3;
GN Name=FGD3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Promotes the formation of filopodia. May activate CDC42, a
CC member of the Ras-like family of Rho- and Rac proteins, by exchanging
CC bound GDP for free GTP. Plays a role in regulating the actin
CC cytoskeleton and cell shape (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC {ECO:0000305}.
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DR EMBL; CR860772; CAH92885.1; -; mRNA.
DR RefSeq; NP_001126690.1; NM_001133218.1.
DR AlphaFoldDB; Q5R5T1; -.
DR BMRB; Q5R5T1; -.
DR SMR; Q5R5T1; -.
DR STRING; 9601.ENSPPYP00000021725; -.
DR GeneID; 100173690; -.
DR KEGG; pon:100173690; -.
DR CTD; 89846; -.
DR eggNOG; KOG4424; Eukaryota.
DR InParanoid; Q5R5T1; -.
DR OrthoDB; 652460at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035941; FGD1-4_PH2.
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; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Guanine-nucleotide releasing factor;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..737
FT /note="FYVE, RhoGEF and PH domain-containing protein 3"
FT /id="PRO_0000080946"
FT DOMAIN 157..341
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 370..469
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 616..715
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 532..588
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 538
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 558
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 583
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5JSP0"
SQ SEQUENCE 737 AA; 80555 MW; 28C77937884E1923 CRC64;
MESGGGSSTP PGPIAALGMP DSGPGSSSLG KLQALPVGPR AHCGDPGSLA AAGDGSLDTG
STGELSGSLK IPNRDSGIDS PSSSVAGENF PCEEGLEAGP SPTVLGAHPE MALDSQVPKV
TPREEADSDV GEEPDSENTP QKADKDAGLA QHSGPQKLLH IAQELLHTEE TYVKRLHLLD
QVFCTRLTDA GIPPEVIMGI FSNISSIHRF HGQFLLPELK TRITEEWDTN PRLGDILQKL
APFLKMYGEY VKNFDRAVGL VSTWTQRSPL FKDVVHSIQK QEVCGNLTLQ HHMLEPVQRV
PRYELLLKDY LKRLPQDAPD QKDAERSLEL ISTAANHSNA AIRKVEKMHK LLEVYEQLGG
EEDIANPANE LIKEGQIQKL SAKNGTPQDR HLFLFNSMIL YCVPKLRLMG QKFSVREKMD
ISGLQVQDIV KPNTAHTFII TGRKRSLELQ TRTEEEKKEW IQIIQATIEK HKQNSETFKA
FGGAFSQDED PSLSPDMPIT STSPVEPVVT TEGGSGAAGL EPRKLSSKTR RDKEKQSCKS
CGETFNSITK RRHHCKLCGV VICGKCSEFK AENSRQSRVC RECFLTQPVA PESPSPEAPA
KPRRSTEKTP TADPQPSLLC GPLRLSESGE TWSEVWAAIP MSDPQVLHLQ GGSQDGWLPR
TIPLPSCKLS VPDPEERLDS GHVWKLQWAK QSWYLSASSA ELQQRWLETL STAARGDTAQ
DSPGALQPQV PTGAAAP
