ID A0A1U7S143_ALLSI Unreviewed; 921 AA.
AC A0A1U7S143;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 4 isoform X1 {ECO:0000313|RefSeq:XP_006022568.3};
GN Name=FGD4 {ECO:0000313|RefSeq:XP_006022568.3};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006022568.3};
RN [1] {ECO:0000313|RefSeq:XP_006022568.3}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR RefSeq; XP_006022568.3; XM_006022506.3.
DR AlphaFoldDB; A0A1U7S143; -.
DR STRING; 38654.A0A1U7S143; -.
DR KEGG; asn:102379917; -.
DR eggNOG; KOG4424; Eukaryota.
DR InParanoid; A0A1U7S143; -.
DR OrthoDB; 5385125at2759; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd15741; FYVE_FGD1_2_4; 1.
DR CDD; cd15791; PH1_FDG4; 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; IPR037742; FDG4_N_PH.
DR InterPro; IPR035941; FGD1-4_PH2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000315; Znf_B-box.
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:SF98; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 4; 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; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 320..507
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 536..635
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 674..734
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 675..725
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 758..855
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 75..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 287..316
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 620..647
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 96..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 103613 MW; E70458B89DC75713 CRC64;
MVCESVTILT LIPCECSSIQ MSLVSESMKT MSSDPGSSVC PKILITAKSC PASNTNRLVK
QNACSEAAQG INGSVPVKQS PCSASNPKPQ VPPKPKHLQN LSSSITYQTP RHKALPRSNP
RMEEVTSTSA SCVSKEKSSK VSDLISHFEG GSPSSHSDLK KESSVLNTAK SQGRYGSTPS
PQPKLLSQHP LQKQGRNNMI QTQVVQKHTA NGVVAQNQME CEDNKLPDHS TNTSAQISDP
LVNSSLLNGE RESTTIDSLP TTTACEGQIL NSCCRTPSSS ILLPSEKETV ETNIDVEEKQ
NDELDKQDQL VEAKETDEQK LHKIASELLH TERAYVSRLD LLDQGFYSKL LAEANRGSFP
AEVVNKIFSN ISSINAFHSK FLLPELEKRM QEWIITPRIG DILQKLAPFL KMYGEYVKNF
DNAMELVKTW TERSPLFKSI IQDIQKQKVC GSLTLQHHML EPVQRIPRYE MLLKDYLRKL
PQDSLDWKDA EKSLEIISTA ASHSNSAIRK MENLKKLLEI YEMLGEEEDI VNPSNELIKE
GQILKLAARN TSAQERYLFL FNNMLLYCVP KFSLVGSKFS VRTRVGIDGM KIIETHNEEY
PHTFQVSGKE RTLELQASSA QDKEEWIKAL QNTIEAFQQR NETFRNAIAK EYEDMPAEVS
NAELGKRAPR WIRDNEVTMC MKCKEPFNAL TRRRHHCRAC GHVVCWKCSD YKVHLEYDSN
KLNKVCKDCY HIITGCTDSE EKKKRGILEI ESAEVSGNSV ICSFLQYMEK SKPWQKAWCV
IPKHEALVLY MYGAPQDVKA LATIPLLGYT VDDTPRSADL PHSFKLTQSK SVHSFAADSE
ELKQKWLKVI NLAVKALRMK DYLLIPCAFQ MSLYCPMHRK GRVSKRQNII ICTNILLCNL
IDVTGTDFAL CGTSVKSCAN L
//
