ID A0A3Q3BRT0_KRYMA Unreviewed; 845 AA.
AC A0A3Q3BRT0;
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:ENSKMAP00000029464.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029464.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029464.1}
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 RefSeq; XP_017274541.1; XM_017419052.1.
DR AlphaFoldDB; A0A3Q3BRT0; -.
DR Ensembl; ENSKMAT00000029830.1; ENSKMAP00000029464.1; ENSKMAG00000021811.1.
DR GeneTree; ENSGT00940000155765; -.
DR Proteomes; UP000264800; 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; 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; 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; IPR011011; Znf_FYVE_PHD.
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; SSF57903; FYVE/PHD zinc finger; 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 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:UP000264800};
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 287..474
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 503..602
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 636..696
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 719..816
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 51..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 594..621
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 51..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 845 AA; 95029 MW; 9684A3329E1E4865 CRC64;
MAERRSKTPC CQTKSADDET CVAVKIEQSR ALGSSPVYKV TTSTVQDCLN RASAVTSNRP
RGGVNGRGPS SRSRLSSKPE VPPKPEHLKS PVTPVLSPFG VIQKSPLRTS MEGRGGKSVP
VARDRMRDKP SKVSDLISRF EENGGTENKK DSSPARHINK ASNYSATQRV FQKTEASRVQ
DNRVPVTAEA QDAKKPAANG VLVQMEQGKP KEEDEDEKNH NSVRTDAAEL LNGDMGSAEQ
SEDHSPAHSD RTAAENLAKN EDRETKTESV QKSEEGSSDH KETNEQKLFN IASELLHTEK
AYVARLHLLD QVFCTKLMEE ANKGTFPVDV VKNIFSNIAS IHAFHSQFLL PDLEKRMGEW
TSTPRIGDIL QKLTPFLKMY AEYVKNFDKA MEVLKQWIDR SPPFKAIIQE IQSQEICGSL
TLQHHMLEPV QRIPRYEMLL KDYLKKLPQD DPDHRDAEKS LEIIATAATH SNSAIRKSEN
LKKLMEIYEM LGEEEDIVHP SNEFIKEGNI LKLAARNASA MERYLFLFNN MLLYCVPKFS
LGGTKYTVRT RIGIDGLKVQ ETTNEDYPHT FQVSGKERAL ELQASSEQDK ADWIKALQET
IEIFQQKNES FKNALKEVED VSEAELGKRA PRWIRDNEVT MCMKCKESFN AITRRRHHCR
ACGYVVCWKC SEHKAPLEYD GNKVNKVCKD CFWILTGKGV TEDKKKGILE IEAGQFADSS
IICGFLQYSE KGKIWQKVWG VIPEKEGVVL YLYGAQQDVK ALCTIPLLGY IVEDGPRPTD
PPASFRLLQS KFIHNFAAET EEVKQRWLKV IREAATGAIL TRPETNGSSA NTDTTTTQEA
NPDST
//
