END3_YEAS7
ID END3_YEAS7 Reviewed; 349 AA.
AC A6ZRZ6;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE AltName: Full=Endocytosis protein 3;
GN Name=END3; ORFNames=SCY_4707;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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. END3 regulates PAN1
CC function by preventing phosphorylation of PAN1 by PKR1 and is also
CC involved in the correct localization of SLA1 to the cell cortex, in the
CC bipolar budding of diploid cells and the correct distribution of chitin
CC at the cell surface (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex
CC composed of at least END3, PAN1, and SLA1. Interacts with SCD5, SLA2
CC and YAP1802. Interacts directly with PAN1. Note=The interaction with
CC PAN1 is prevented by PAN1 phosphorylation by PKR1 (By similarity).
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; AAFW02000067; EDN62728.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRZ6; -.
DR SMR; A6ZRZ6; -.
DR PRIDE; A6ZRZ6; -.
DR EnsemblFungi; EDN62728; EDN62728; SCY_4707.
DR HOGENOM; CLU_040829_0_0_1; -.
DR Proteomes; UP000007060; 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; 2.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
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 Phosphoprotein; Repeat.
FT CHAIN 1..349
FT /note="Actin cytoskeleton-regulatory complex protein END3"
FT /id="PRO_0000349461"
FT DOMAIN 8..98
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 40..75
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 130..222
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 146..164
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 276..295
FT /note="1"
FT REPEAT 315..334
FT /note="2"
FT REGION 96..105
FT /note="Polyphosphoinositide (PIP2)-binding"
FT /evidence="ECO:0000255"
FT REGION 226..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..334
FT /note="2 X 20 AA approximate repeats"
FT COILED 307..349
FT /evidence="ECO:0000255"
FT COMPBIAS 232..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..265
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"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39013"
SQ SEQUENCE 349 AA; 40323 MW; 1F9499BE51275842 CRC64;
MPKLEQFEIK KYWQIFSGLK PIENKVNHDQ VLPILYNSKL DSSVLNKIWF LADIDDDDNL
DFEEFVICMR LIFDMVNKNI SSVPDELPDW LIPGSKVNLI KERKKRKQIE NADLPPKKEI
KVDWYMSPDD LNQYEKIYNS CAKLTDGTIT FNELSTKLST KFFNISKTDL NKVWSLINPQ
NLPSIDRDPT FYFIHCLRQR NDLGAEIPAS LPNSLAEVCN KKQLSYDLRS SQPPTKRKEE
ANEVDNLRDN GQNSSSDNSG SNVLSNENSI KQKYASLTDD QVANMREQLE GLLNYKKSEK
TQGGSKLSKR INIRSITDDL DNIEQQVEVL ENYLNNKRHE LQALQAEIN
