ID S0DYN2_GIBF5 Unreviewed; 1258 AA.
AC S0DYN2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Related to EDE1 protein {ECO:0000313|EMBL:CCT67530.1};
GN ORFNames=FFUJ_13421 {ECO:0000313|EMBL:CCT67530.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT67530.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization.
CC {ECO:0000256|ARBA:ARBA00025194}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000256|ARBA:ARBA00011159}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004413};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm,
CC cytoskeleton, actin patch {ECO:0000256|ARBA:ARBA00004134}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004125}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004125}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004125}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; HF679026; CCT67530.1; -; Genomic_DNA.
DR AlphaFoldDB; S0DYN2; -.
DR STRING; 1279085.S0DYN2; -.
DR EnsemblFungi; CCT67530; CCT67530; FFUJ_13421.
DR VEuPathDB; FungiDB:FFUJ_13421; -.
DR HOGENOM; CLU_002006_0_0_1; -.
DR OrthoDB; 12127at2759; -.
DR Proteomes; UP000016800; Chromosome 4.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 3.
DR CDD; cd14270; UBA; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11216; EH DOMAIN; 1.
DR PANTHER; PTHR11216:SF161; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE CLONE 15, ISOFORM A; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 4.
DR SMART; SM00027; EH; 3.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF47473; EF-hand; 3.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 3.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 15..91
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 151..241
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 294..385
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT DOMAIN 327..362
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1217..1257
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 675..702
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 242..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..981
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 132122 MW; DCFA0412A575D39A CRC64;
MAADEAPNLN LSPEEKRTYG QLFRQADSDS VGVVVGEIAV RFFHKTGLDS RILGEIWQIA
DKENRGFLTP AGFGIALRLI GHAQAGREPT PEIALQQAPL PRFDGIVPQV TGAGGIPPPP
PVPVSSPPPP AALQAQSTGG PIRIPPLTPE KVAQYSGLFE RQPLQGGQLP GDQARTIFEK
SGLPNEALGR IWQLADTEQR GALVLTEFII AMHLLTSMKT GALRSLPSVL PAGLYEAASR
RGPASRQSST GPGISAIPRQ VSGTAQVRTS SPLGRPPMSP QQSGASDWAV TPADKARFDQ
IYADLDKGNK GYITGEEAVT FFSQSNLPED SLAQIWDLAD TKSQGQLSRD EFAVAMYLIR
QQRSGRSVPL PTTLPPNLVP PSMRTQIRPQ TATSAFDPPP PPVVQAPPPA PKSALDDLFG
LESGTSSPAP PPPAQAPMST GGSNANDPFA GGSALTPTSP VKPSLTGTGG SSFKPFVPSS
SFGRGLTQQP TGGSAGSGQK LPAPSASEDL LSDNDEASKN ISGETTELAN LSNQISSLSK
QTQDVQAKRN TTQNELNQAT SQKQNFEQRL AQLRTLYEKE AQDTRALEEQ LSNARKETAK
LQSECMALEG TYRDTRTQHQ QVLAALQADQ QENTNLRERI RVVNGEIAQL KPQIEKLKSD
ARQQKGLVAI NKKQLSTTEG ERDKLKGEAE ELTKSIEDLR LANTGSPASA SAQIASPAAS
TSSANNPFFR RTASTDIMGA FASPPPTKNV SDKSFDDLFG PSFPPSASAT PPPPPQTSFK
PQHTGASTAS AGSYSTPPAA SSPIMSRQAT LAAEPPAPPE SRQISSSFLP FPDHTESLSS
SRQVSPPASR ADDPLHGSAT PVPGDLKTSD SPAGVPGAFP GDELDKSNAK DVASASASDD
TTREAAKNEA PKATEPGDPF SGNDEAKAKA DFENAFAAFT TAKSHTKPSP EANKSSAFDS
EFPPISELER DDDEESDSSS DNGGFDDNFT PASPPAKPFG EKANAGESPE ATHAVPASTS
PQPVQGATPP SEPKAPSTEQ PSSPATVTEA TAQKSSVDDI FGAAATGTAP ASQQPAPSNP
PQTKGGFDDL DSDFEGLEDA KEGSADEDFA NISRSGLDDF NPVFDSSPPG SQTKTESTAF
GNESFDFISH SSTGAAQPAV GTNQQKAPEA HDWDAIFSGL DSPSATAAQP ASNEKPAGAE
SHPGQQALNR TLSTESEHDD PILKSLTSMG YKRPEALDAL EKYDYDLDKA ANFLASRS
//
