ID W5MZ93_LEPOC Unreviewed; 1446 AA.
AC W5MZ93;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=FYVE, RhoGEF and PH domain containing 5 {ECO:0000313|Ensembl:ENSLOCP00000013702.1};
GN Name=FGD5 {ECO:0000313|Ensembl:ENSLOCP00000013702.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013702.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013702.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; AHAT01031655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSLOCT00000013731.1; ENSLOCP00000013702.1; ENSLOCG00000011142.1.
DR GeneTree; ENSGT00940000157922; -.
DR HOGENOM; CLU_004088_1_0_1; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000011142; Expressed in heart and 10 other cell types or tissues.
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; cd15742; FYVE_FGD5; 1.
DR CDD; cd13237; PH2_FGD5_FGD6; 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; 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:SF13; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 5; 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:UP000018468};
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 879..1068
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1097..1191
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1226..1285
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1347..1445
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 94..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..869
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1446 AA; 162253 MW; BB1215F3AA91B01B CRC64;
SARGPKPPIA PKPKLLQDSD EKCCLYTNNS LNRCSNGTLL CSEEDFNQEN ESDSFQITGD
GYILLSDNEQ LTDDGEECDN EEGHLLELCS DAVALGSSDN GEELEEDEEG GEGNLMDPVD
TEGTDRMECA EISNAEYADL TEPACCGSHE ALEADDELSE IAEACDNEEV NKSSEHQPHQ
ANEDYELVDT QQGAEVDEEL SQDAGNDAKR EAVEECLSDN TPAIDTRCGI AEEDDAPAAV
SQESMTFYEE TQDPKEKEDD LMNNNCEDLL ESEERQDNQC AVSFETSFSE KQENEISVDF
SSVGEQEILA DQINDSSVSE AAEDSIIGNE PIADVENNLE TEAKPEEEYY VNETFKVLSS
EEQETEDLEA VECIPSEDLI EVPEADNLME SDQDKTEVDA DCTEREGEGL SSQSTNQGLI
VPYLEETDTD RAEDTISDEH VYEEAGLDTE GENLNFISLD RKSIVTRTRS LSGKVPGYVP
ETVPEETGPE SDMLQSNEYC TVALDKSGNP LSDHEQLEIN RMIPSKPRRF ILYPRSYSVE
GRDMPMSVFR ENDSSTGEDG RMKRKDDNLS LPCFIGSSGS FSQRSHLPSS GMSTPTSVVD
IPPPFELAYI TKKPITKSSP SLLIESDSAD KQKKKKSSFK RFLTLKFKKK TENKVHVDVN
VSSSRSSSES SHHGPLRVLE LDRRSLGSSP QLKSRSGKPW ALDSPSTFLF YKDSKRKGTP
KTFSRSVSRV ESFEDRSRPP FMPLPLTKPR SISFPNADTS DYENIPAMNS DYENIQIPPR
RPTRTGTFTE FFEDPSRALS SANENDGYVD MSSFTGFESK PQTPDQESES AYTEPYNVCP
VSTVPVSGLA SEEDQGKSSG EEDSLVESSQ ERQIDGQSRA FYIAKDLMDS ENTHVKALKL
LHEDFRNAVM SAVTEAGDPV LEEDKLCEIL SELPQIYQFH QDILSDLESR IANWEEYQRI
ADVLLSRRLQ FNIFTPYITQ YDRNMALLEE CCQKSLAFSL VVKQFEQSPA CGNVSLQHQL
LKVIVRILQY RMLLTDYLNN LSPDSAEYED TQAALVIVSE VADRANDSMR KGENLLRLVH
IEYSVRGQKD LLQPGRVFVK EGTLMKVSRR NRQPRHLFLM NDVMLYTYPQ QDGKYRLKNT
LSLTEMKVSK PIIENVHNAL KIENNNCSIT LSASSCGERE DWYHALSRAI SDHSKGQGTF
SSSNSCEARE KLWMSLGEKA PTLVPVSHVM MCMNCASDFS LTLRRHHCHA CGKIVCRACS
RNKYPLKYLK DRVAKVCDRC YAELKKRGTV SPIQLDIHQH ENLNALNSNR LSGRPLSAVF
QNIHPPILWK NRKSSSALTQ VAASAEGSSM SGSLHRCKRS RRTWKKLFFL IKDKVLYTFS
ASEDKVASES LPLLGFTVKQ PEKAEGAEAT MMFQLYHKKT LYYTFKAEDS YTAQRWINAM
EEATVL
//
