ID A0A3Q3BH80_KRYMA Unreviewed; 869 AA.
AC A0A3Q3BH80;
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:ENSKMAP00000029453.1};
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:ENSKMAP00000029453.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029453.1}
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_017274538.1; XM_017419049.1.
DR AlphaFoldDB; A0A3Q3BH80; -.
DR Ensembl; ENSKMAT00000029819.1; ENSKMAP00000029453.1; 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 311..498
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 527..626
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 660..720
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 743..840
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 78..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 618..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 78..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..309
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 869 AA; 98178 MW; DA0D01CB39849EB7 CRC64;
MMKRRRKYWI WSRKGKNSKM CLLCCYERRS KTPCCQTKSA DDETCVAVKI EQSRALGSSP
VYKVTTSTVQ DCLNRASAVT SNRPRGGVNG RGPSSRSRLS SKPEVPPKPE HLKSPVTPVL
SPFGVIQKSP LRTSMEGRGG KSVPVARDRM RDKPSKVSDL ISRFEENGGT ENKKDSSPAR
HINKASNYSA TQRVFQKTEA SRVQDNRVPV TAEAQDAKKP AANGVLVQME QGKPKEEDED
EKNHNSVRTD AAELLNGDMG SAEQSEDHSP AHSDRTAAEN LAKNEDRETK TESVQKSEEG
SSDHKETNEQ KLFNIASELL HTEKAYVARL HLLDQVFCTK LMEEANKGTF PVDVVKNIFS
NIASIHAFHS QFLLPDLEKR MGEWTSTPRI GDILQKLTPF LKMYAEYVKN FDKAMEVLKQ
WIDRSPPFKA IIQEIQSQEI CGSLTLQHHM LEPVQRIPRY EMLLKDYLKK LPQDDPDHRD
AEKSLEIIAT AATHSNSAIR KSENLKKLME IYEMLGEEED IVHPSNEFIK EGNILKLAAR
NASAMERYLF LFNNMLLYCV PKFSLGGTKY TVRTRIGIDG LKVQETTNED YPHTFQVSGK
ERALELQASS EQDKADWIKA LQETIEIFQQ KNESFKNALK EVEDVSEAEL GKRAPRWIRD
NEVTMCMKCK ESFNAITRRR HHCRACGYVV CWKCSEHKAP LEYDGNKVNK VCKDCFWILT
GKGVTEDKKK GILEIEAGQF ADSSIICGFL QYSEKGKIWQ KVWGVIPEKE GVVLYLYGAQ
QDVKALCTIP LLGYIVEDGP RPTDPPASFR LLQSKFIHNF AAETEEVKQR WLKVIREAAT
GAILTRPETN GSSANTDTTT TQEANPDST
//
