END3_MAGOY
ID END3_MAGOY Reviewed; 396 AA.
AC L7IIY8; G4N017; Q5EN00;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE AltName: Full=Endocytosis protein 3;
GN Name=END3; ORFNames=OOU_Y34scaffold00192g42;
OS Magnaporthe oryzae (strain Y34) (Rice blast fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=1143189;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Y34; TISSUE=Conidium;
RA Dong H.T., Peng Y.L., Chen B.S., Li Y.Z., Li D.B.;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y34;
RX PubMed=22876203; DOI=10.1371/journal.pgen.1002869;
RA Xue M., Yang J., Li Z., Hu S., Yao N., Dean R.A., Zhao W., Shen M.,
RA Zhang H., Li C., Liu L., Cao L., Xu X., Xing Y., Hsiang T., Zhang Z.,
RA Xu J.-R., Peng Y.-L.;
RT "Comparative analysis of the genomes of two field isolates of the rice
RT blast fungus Magnaporthe oryzae.";
RL PLoS Genet. 8:E1002869-E1002869(2012).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the END3 family. {ECO:0000305}.
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DR EMBL; AY849632; AAX07653.1; -; mRNA.
DR EMBL; JH793663; ELQ42856.1; -; Genomic_DNA.
DR AlphaFoldDB; L7IIY8; -.
DR Proteomes; UP000011086; Unassembled WGS sequence.
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:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00052; EH; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR025604; End3.
DR Pfam; PF12763; EF-hand_4; 1.
DR Pfam; PF12761; End3; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50031; EH; 2.
PE 2: Evidence at transcript level;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding; Repeat.
FT CHAIN 1..396
FT /note="Actin cytoskeleton-regulatory complex protein END3"
FT /id="PRO_0000423542"
FT DOMAIN 9..99
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 41..76
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 138..226
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 341..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 282..395
FT /evidence="ECO:0000255"
FT COMPBIAS 360..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 396 AA; 44920 MW; B8E6709E19D92B29 CRC64;
MAPRIEAQEI ETYWNIFSAR TNGSKFLTGE QAAPVLKNSG LRDDQLERVW DLADVDNDGN
LDFEEFCVAM RVIFDILNGE HADVPSTLPD WLVPESKAHL VQANRALTGK QVQFERVDDD
PDSPGLKDGF DWYMSPADKS KYESIYQENR DMRGEVSFGA LEDLYESLDV PDTDIRSAWN
LINPSAGPTI NKDACLAFLH ILNYRHEGYR IPRTVPASLR ASFERNKIDY QVDKQAASRW
ATKADDETST GRKAKFGDQY LTRLGRGSFK TSGTDFSSAQ TDSEWEEVRL KKQLAELDAK
MASVEADAER RKGGKRDSKP ALVKRELEQL LDYKRKQLRE IEEGKTKGQG GGSLKGIQDD
LQTVREQTDG LASHLRSRQQ HLEELRRQIE DEKAGR
