ID A0A3Q1FE95_9TELE Unreviewed; 871 AA.
AC A0A3Q1FE95;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=FYVE, RhoGEF and PH domain containing 4 {ECO:0000313|Ensembl:ENSAPOP00000015378.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000015378.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000015378.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR AlphaFoldDB; A0A3Q1FE95; -.
DR STRING; 80966.ENSAPOP00000015378; -.
DR Ensembl; ENSAPOT00000024065.1; ENSAPOP00000015378.1; ENSAPOG00000018335.1.
DR GeneTree; ENSGT00940000155765; -.
DR InParanoid; A0A3Q1FE95; -.
DR OrthoDB; 5385125at2759; -.
DR Proteomes; UP000257200; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
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:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 314..501
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 530..629
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 663..723
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 746..843
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 61..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 97917 MW; A438E10A4BB2EE26 CRC64;
MREPSVYRRD MDGFSRVAFR RKQRSLDFPD SNETERKGKT ACCKTRSADE EACVAVKIEH
SRALGSSPAR NPSSAPSVQA CLNRANRGTT EASRGGLNGR GSRPQLQSKP QVPPKPLHLQ
SPVTELSSPL GRFQKPPLRA AMEEGGGKTG AVNRDRAKEK HSKVSDLISR FEENSNTENK
RDGSPLKHTS KSSNCSPAHR QHQKQTESGR TQENHSSLPA AKQDAHKPAA NGVLVQMEQG
KEKEEKEEKN HDGVRIETGE LVNGDMGSAE QSHHSPTAHT DRTGSESCSG NEDSGTKAES
EEGSADQKET NEQKLFKIAS ELLHTEKAYV ARLNLLDQVF CAKLMEEANK GTFPVDVVKN
IFSNISSIHA FHSQFLLPDL EKRMGEWAST PRIGDILQKL TPFLKMYGEY VKNFDKAMEL
LKQWIDRSPQ FKAIIQEIQS QEVCGCLTLQ HHMLEPVQRV PRYEMLLKDY LKKLPQEDSD
RRDAEKSLEI IATAATHSNS AIRKSENLKK LMEIYEMLGE EEDIVHPSNE FIKEGHILKL
AARNTSAMER YLFLFNNMLL YCVPKFSLGG TKYTVRTRIG IDGMKVLETT NEDYPHTFQV
SGKERTLELQ ASSEQDKADW IKAFRETIEI FQLKNESFKN AQKDVEEVSK AELGKRAPRW
IRDNEVTMCM KCKEPFNALT RRRHHCRACG YVVCWKCSDN KVKLEYDGNK VNKVCRDCYS
ILKGEGIAEG KKKGILEIEA GQFADSSIMC GFLQYSEKNK LWQKVWCVIP EKESLVLYLY
GAPQDVKAQC SIPLLGYSVD DSAGPTDHPA SFRLSQSKSV HSFAAETEDL KQRWLKVIRL
AVTGDLPERP HSNGSGSLDN NNSQEASTDS S
//
