ID W5MZ81_LEPOC Unreviewed; 1587 AA.
AC W5MZ81;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=FYVE, RhoGEF and PH domain containing 5 {ECO:0000313|Ensembl:ENSLOCP00000013690.1};
GN Name=FGD5 {ECO:0000313|Ensembl:ENSLOCP00000013690.1};
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:ENSLOCP00000013690.1, 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:ENSLOCP00000013690.1}
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 EMBL; AHAT01031655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01031657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015202862.1; XM_015347376.1.
DR STRING; 7918.ENSLOCP00000013690; -.
DR Ensembl; ENSLOCT00000013719.1; ENSLOCP00000013690.1; ENSLOCG00000011142.1.
DR GeneID; 102683174; -.
DR KEGG; loc:102683174; -.
DR CTD; 152273; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000157922; -.
DR InParanoid; W5MZ81; -.
DR OrthoDB; 5385125at2759; -.
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; IBA:GO_Central.
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 1026..1215
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1244..1338
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1373..1432
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 1488..1586
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 23..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1587 AA; 177337 MW; 62A8A1C679EB295F CRC64;
MNTDYKKPPL APKPKILSHL TSKLPSSLMS KPCSSARGPK PPIAPKPKLL QDSDEKCCLY
TNNSLNRCSN GTLLCSEEDF NQENESDSFQ ITGDGYILLS DNEQLTDDGE ECDNEEGHLL
ELCSDAVALG SSDNGEELEE DEEGGEGNLM DPVDTEGTDR MECAEISNAE YADLTEPACC
GSHEALEADD ELSEIAEACD NEEVNKSSEH QPHQANEDYE LVDTQQGAEV DEELSQDAGN
DAKREAVEEC LSDNTPAIDT RCGIAEEDDA PAAVSQESMT FYEETQDPKE KEDDLMNNNC
EDLLESEERQ DNQCAVSFET SFSEKQENEI SVDFSSVGEQ EILADQINDS SVSEAAEDSI
IGNEPIADVE NNLETEAKPE EEYYVNETFK VLSSEEQGPM NTTDNVSLEA IADVEEIQAN
MVGDTTEETI DSLQFSSEIQ SAMIELMPEI EVSEPVEDAS ELDGSVSQET EDLEAVECIP
SEDLIEVPEA DNLMESDQDK TEVDADCTER EGEGLSSQST NQAQNEPCAM TVPGDIDVIR
IDELINRQVL TDTSDIFGDD IDFEGLIVPY LEETDTDRAE DTISDEHVYE EAGLDTEGEN
LNFISLDRKS IVTRTRSLSG KVPGYVPETV PEETGPESDM LQSNEYCTVA LDKSGNPLSD
HEQLEINRMI PSKPRRFILY PRSYSVEGRD MPMSVFREND SSTGEDGRMK RKDDNLSLPC
FIGSSGSFSQ RSHLPSSGMS TPTSVVDIPP PFELAYITKK PITKSSPSLL IESDSADKQK
KKKSSFKRFL TLKFKKKTEN KVHVDVNVSS SRSSSESSHH GPLRVLELDR RSLGSSPQLK
SRSGKPWALD SPSTFLFYKD SKRKGTPKTF SRSVSRVESF EDRSRPPFMP LPLTKPRSIS
FPNADTSDYE NIPAMNSDYE NIQIPPRRPT RTGTFTEFFE DPSRALSSAN ENDGYVDMSS
FTGFESKPQT PDQESESAYT EPYNVCPVST VPVSGLASEE DQGKSSGEED SLVESSQERQ
IDGQSRAFYI AKDLMDSENT HVKALKLLHE DFRNAVMSAV TEAGDPVLEE DKLCEILSEL
PQIYQFHQDI LSDLESRIAN WEEYQRIADV LLSRRLQFNI FTPYITQYDR NMALLEECCQ
KSLAFSLVVK QFEQSPACGN VSLQHQLLKV IVRILQYRML LTDYLNNLSP DSAEYEDTQA
ALVIVSEVAD RANDSMRKGE NLLRLVHIEY SVRGQKDLLQ PGRVFVKEGT LMKVSRRNRQ
PRHLFLMNDV MLYTYPQQDG KYRLKNTLSL TEMKVSKPII ENVHNALKIE NNNCSITLSA
SSCGEREDWY HALSRAISDH SKGQGTFSSS NSCEAREKLW MSLGEKAPTL VPVSHVMMCM
NCASDFSLTL RRHHCHACGK IVCRACSRNK YPLKYLKDRV AKVCDRCYAE LKKRGGVCPG
AGENSSHQSN RLSGRPLSAV FQNIHPPILW KNRKSSSALT QVAASAEGSS MSGSLHRCKR
SRRTWKKLFF LIKDKVLYTF SASEDKVASE SLPLLGFTVK QPEKAEGAEA TMMFQLYHKK
TLYYTFKAED SYTAQRWINA MEEATVL
//
