ID M7B8M7_CHEMY Unreviewed; 824 AA.
AC M7B8M7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 4 {ECO:0000313|EMBL:EMP28528.1};
GN ORFNames=UY3_14359 {ECO:0000313|EMBL:EMP28528.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP28528.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KB562899; EMP28528.1; -; Genomic_DNA.
DR AlphaFoldDB; M7B8M7; -.
DR STRING; 8469.M7B8M7; -.
DR eggNOG; KOG4424; Eukaryota.
DR Proteomes; UP000031443; 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; cd15741; FYVE_FGD1_2_4; 1.
DR CDD; cd15791; PH1_FDG4; 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; IPR037742; FDG4_N_PH.
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; 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; 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:UP000031443};
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 263..450
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 479..578
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 617..677
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 701..798
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 63..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 93647 MW; 518EB70572E790CF CRC64;
MRGENGKEKT VLHSSKQADG TNIFNFFGKH LIVQNAVPPK PVHLQNSFLS ITHQTPMRKA
LPTAQPRMEE VTPTSASCVS KEKPHKVSDL ISRFEGGSPS SPSDLKKETS VVKVAKSQGR
YGSASPQPKL LSQHPLQKQG NNTDQTQVVQ KHRANGVVAQ GQMECKDNKL LEHSTNTSTP
ASEIAVNSNL VNGEQESTTT DSLQATTVCT GQTLDCCRTP SRDTLFLSEN ETVETNTNVE
EKQNEDLNKE EEHVEAKETD EEKRHKIADE LLHTERAYVS RLDLLDKVFY GRLLEEANRG
SFPAEVVNKI FSNISSINAF HSKFLLPELE KRMQEWTGTP RIGDILQKLA PFLKMYGEYV
KNFDNAMELV KMWTERSPLF KSIIQDIQTQ KVCGSLTLQH HMLEPVQRIP RYEMLLKDYL
RKLPQDSLDW KDAEKSLEII STAASHSNSA IRKMENLKKL LEVYEMLGEE EDIVNPSNEL
IKEGQILKLA ARNTSAQERY LFLFNNMLLY CVPKFSLVGS KYSVRTRVGI DGMKIVETHN
EEYPCTFQVS GKERTLELQA SSEQDKEEWI KALQNTIEAF HQRNETFRNA IAKEYEDMPI
EVSKAELGKR APRWIRDNEV TMCMKCKEPF NALTRRRHHC RACGHVVCWK CSDYKAQLEY
DGNKLNKVCK DCYQIIMGCT DSEEKKKKGI LEIESAEVSG NSVICSFLQY MEKSKPWQKA
WCVIPKHEAL VLYMYGAPQD VKALATIPLL GYAVDDTPRS ADLPHSFKLT QSKSVHSFAA
DSEELKQKWL KVIHLAVKGE TPECQNELQM SLEEQPESSK KSEC
//
