END3_ASPCL
ID END3_ASPCL Reviewed; 404 AA.
AC A1CPG1;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein end3;
DE AltName: Full=Cytoskeletal adapter protein sagA;
DE AltName: Full=Endocytosis protein 3;
GN Name=end3; Synonyms=sagA; ORFNames=ACLA_022460;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027059; EAW07532.1; -; Genomic_DNA.
DR RefSeq; XP_001268958.1; XM_001268957.1.
DR AlphaFoldDB; A1CPG1; -.
DR STRING; 5057.CADACLAP00002717; -.
DR PRIDE; A1CPG1; -.
DR EnsemblFungi; EAW07532; EAW07532; ACLA_022460.
DR GeneID; 4701465; -.
DR KEGG; act:ACLA_022460; -.
DR VEuPathDB; FungiDB:ACLA_022460; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_040829_0_0_1; -.
DR OMA; SNKIDYQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000006701; 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 3: Inferred from homology;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..404
FT /note="Actin cytoskeleton-regulatory complex protein end3"
FT /id="PRO_0000349436"
FT DOMAIN 10..100
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 42..77
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 139..227
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 280..399
FT /evidence="ECO:0000255"
FT BINDING 55
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 404 AA; 46385 MW; 8C1FD52BF3A17545 CRC64;
MSTKKIEQWE IERYWEIFAS LSNGQPHLNS SQAASVLRNS RLRDEQLEKV WDLADVDGDG
ELDFEEFCVA MRLVFDLVNG ELQEVPRVLP DWLVPESKAH LVQAGRALSG RPEQFERIED
EDDTPGLKDG FDWYMNPADK SKYEEIYSAN RNHRGEVTFE SLQGLYDSLD VPDTDVRSAW
NLVNPSASPA INKDATLAFL HILNYRHEGF RIPRTIPASL RASFENNKID YQVDNARPAQ
KWGADGSTET LTGRKTKFGD TYLSRLGVGG KGSYTPKGTD FSDTIQDEEW EKVRLRRELA
EMEAKLDAAN KASEGRRDRP RNDGRPNWVL IKKEALQLLE YKERELRELR EGTGRAKEGQ
DLERLRDDIK TVGDQVEGLK AHLAERKDVL ADVRRQIEEE RLHR
