END3_ASHGO
ID END3_ASHGO Reviewed; 372 AA.
AC Q755V2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE AltName: Full=Endocytosis protein 3;
GN Name=END3; OrderedLocusNames=AER416C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 110.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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 (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; AE016818; AAS53095.2; -; Genomic_DNA.
DR RefSeq; NP_985271.2; NM_210625.2.
DR AlphaFoldDB; Q755V2; -.
DR STRING; 33169.AAS53095; -.
DR EnsemblFungi; AAS53095; AAS53095; AGOS_AER416C.
DR GeneID; 4621490; -.
DR KEGG; ago:AGOS_AER416C; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_040829_0_0_1; -.
DR InParanoid; Q755V2; -.
DR OMA; SNKIDYQ; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IEA:EnsemblFungi.
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:0030674; F:protein-macromolecule adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0030476; P:ascospore wall assembly; IEA:EnsemblFungi.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
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..372
FT /note="Actin cytoskeleton-regulatory complex protein END3"
FT /id="PRO_0000349435"
FT DOMAIN 8..98
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 40..75
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 133..225
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT REGION 242..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..355
FT /evidence="ECO:0000255"
FT COMPBIAS 246..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 372 AA; 41364 MW; 9D5FC77434FADED8 CRC64;
MPKLEQFEIK KYWQIFSGLS PSDNKVTHDQ VAPILHNSKL EAGVLGKIWF LSDIDGDGNL
DFEEFVICMR LIFDMVNQNI TAVPDELPDW LVPGSKVELV RQRASQGGVA AASAAPASAG
EAPEMEWYMS PEDRALYERL YQKCQTATDG SVGYQGVKPV VTEHFQKITQ PELEQVWALV
NPKGFAAIDR DPVMYLFHLL RQRSDVGAKI PAGVPASLGE TFAKERVTTD IANEGQGAIR
KSELHIASAS RSNSARPKNE NSDYSATAGT DWEVVQLQRE LAALDSQLSD LKQQQESAPP
TRAEVLREQF EGLLKFKQAQ LSTSTNSSPA MNVLSLTEDI DSLEEQVTVL QHYLSTRSET
LQQLQWEIQS LK
