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Database: UniProt
Entry: A0A2C9KV79_BIOGL
LinkDB: A0A2C9KV79_BIOGL
Original site: A0A2C9KV79_BIOGL 
ID   A0A2C9KV79_BIOGL        Unreviewed;      1458 AA.
AC   A0A2C9KV79;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=FYVE, RhoGEF and PH domain-containing protein 4 {ECO:0008006|Google:ProtNLM};
GN   Name=106053183 {ECO:0000313|EnsemblMetazoa:BGLB023855-PC};
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB023855-PC, ECO:0000313|Proteomes:UP000076420};
RN   [1] {ECO:0000313|EnsemblMetazoa:BGLB023855-PC}
RP   IDENTIFICATION.
RC   STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB023855-PC};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   RefSeq; XP_013064132.1; XM_013208678.1.
DR   STRING; 6526.A0A2C9KV79; -.
DR   EnsemblMetazoa; BGLB023855-RC; BGLB023855-PC; BGLB023855.
DR   GeneID; 106053183; -.
DR   KEGG; bgt:106053183; -.
DR   VEuPathDB; VectorBase:BGLB023855; -.
DR   OrthoDB; 5385125at2759; -.
DR   Proteomes; UP000076420; Unassembled WGS sequence.
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; 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; 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   PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR   PANTHER; PTHR12673:SF241; PROTEIN CBG10230; 1.
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; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
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   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          843..1031
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          1196..1254
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          1280..1377
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          261..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1382..1458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        328..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..552
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..710
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        721..768
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..836
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1383..1427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1458 AA;  162582 MW;  6120508E74E862D9 CRC64;
     MYKRSTFLFP PIPEVENDGF PFAATEEEIR QFDKAFFHGK PAKPKKSWAK SFSEGTPLAS
     LRRLQVPSRP KFIDKFLLGA SSLSRKSSGK LKKSPSVSSQ DSSKFYLDFQ EDQSDVGSTC
     DSVSQCSSSF EGHSDHTGYL DVNCQGDDYD DEAALDEVVE DSDGGESSHT SLEICSQLNV
     SSEDQSSELQ LKNHLHDYSV EEIIYDITDA EQQLITDAEQ QLITDAGQQF NSDHEHITKI
     SCNSVEISDS QSVGALDIPA VSDSPTEAQE STSDSPTEAQ ESTSDEPPEP SLVTKGFVKR
     QCQVFLQSLQ PSESARDSLD LSRKVKRSSS ELNPNSSLCG QYRRPLSPHS DNPDKWSKSL
     YDISRNNKFT EAVMAKGYVK ALSEQINQQG ALKLEVDDDD AKKDALEESD EDAVFLHQFK
     DQGLRQSFVK DLIQAAESQS SKENSSGNCK PPTVKKPGGY DQSPHSEHNS PSSVSCHNLS
     SQTGINGDSS LNKSTSSNIN PTPKLFIKKT PENALSHSRS LHLSQSSSTT KHSPSKASSV
     RSHSTTSPGD KPHVDYNSKP KKLSLTPELT QMLNVKADSP SESSLAHNES SVSKFSVTTN
     TVGSPSEIKH SETHVAKHSE THVAKHSEIH VAKHSEMSEA KHIEIHLTYP NETSHKHADI
     LVTKHNTTYV TTHSKTQTPK HTETQVSSPS SHPTSPISKS SNSSLPHPIS SPGTHIAALP
     SELRMTSSNE SNKSCAGTQR EDSESSTSSS NSHNLEVSMR VSSTRSSQQY RDSVFNTIYD
     NAPALNAAEL FDSSWSDSDS MDEFSDGEEK QEERKKVEEK KKKEEEKKEP SVSEQVDVPA
     EDKRFRIASE LLQTERDYVA RLHLLHQVFY FTLDKENRQQ QMFPPDTLRH MFSNTKSIFL
     FHNDFLLPQL EDRMKNWNAD PRIGDLMKKN APFLKMYTEY IRNFDRAMKL INQWMEKSVR
     FSEIIRDIQK KPECGSLSLQ HHMLGPIQRV PRYELLLKDY VKHLPENSPD KSDAKDALDL
     VTKAACHSNE AMKKIETFHK LLDIYQSLRG DVPVDFISPT REFVTQGPVT KISARSGEKQ
     PRQIILFNDM VLVCAYILGA YSVRSVLEVD SLEIKPGNNM HIPNTMMLRS KQKAVELLDE
     NPSGELMGWK VKFEDVIANY KQRKRFIKSI DVTDDSSETN MPESCLGKTA PVWIPDDAAT
     MCMLCQSTFN MVRRRHHCRS CGKLICKSCC KKAPLEYKKM KIDRVCVLCY DVIVNKRGAT
     ETSSVVDKKK GVLQVKASDP GLLCGYMHCS TDNGVSWSKL WVSARNDFAL YTFRAHEDVS
     AIGSLPLPGH EVECFGEYEN KQNVFGLKHK NKMVFFFQAD NDKKMKRWVS LLSKLVKAEL
     PEESSRLSSQ SNTSNTSSDN IATEGGNNRN STHSGSQADS GYPGDSNSSL AALAAEDIDH
     ESADGVSQYD NIDAVVSE
//
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