END3_YEAST
ID END3_YEAST Reviewed; 349 AA.
AC P39013; D6W195; Q8TFC4; Q8TFD0; Q8TG51;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE AltName: Full=Endocytosis protein 3;
GN Name=END3; OrderedLocusNames=YNL084C; ORFNames=N2307;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7841519; DOI=10.1091/mbc.5.9.1023;
RA Benedetti H., Raths S., Crausaz F., Riezman H.;
RT "The END3 gene encodes a protein that is required for the internalization
RT step of endocytosis and for actin cytoskeleton organization in yeast.";
RL Mol. Biol. Cell 5:1023-1037(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-245; ASN-258 AND
RP ASN-268.
RC STRAIN=ATCC 200060 / W303, S96, SK1, YJM 1129, YJM 269, YJM 270, YJM 280,
RC YJM 320, YJM 326, YJM 339, YJM 421, YJM 627, and YJM 789;
RX PubMed=11907579; DOI=10.1038/416326a;
RA Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J.,
RA McCusker J.H., Davis R.W.;
RT "Dissecting the architecture of a quantitative trait locus in yeast.";
RL Nature 416:326-330(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-268.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740422;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<485::aid-yea928>3.0.co;2-u;
RA Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.;
RT "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome
RT XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading
RT frames.";
RL Yeast 12:485-491(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP FUNCTION.
RX PubMed=8380177; DOI=10.1083/jcb.120.1.55;
RA Raths S., Rohrer J., Crausaz F., Riezman H.;
RT "END3 and END4: two mutants defective in receptor-mediated and fluid-phase
RT endocytosis in Saccharomyces cerevisiae.";
RL J. Cell Biol. 120:55-65(1993).
RN [8]
RP FUNCTION.
RX PubMed=8144575; DOI=10.1016/s0021-9258(17)36959-4;
RA Volland C., Urban-Grimal D., Geraud G., Haguenauer-Tsapis R.;
RT "Endocytosis and degradation of the yeast uracil permease under adverse
RT conditions.";
RL J. Biol. Chem. 269:9833-9841(1994).
RN [9]
RP FUNCTION.
RX PubMed=7865884; DOI=10.1091/mbc.5.11.1185;
RA Berkower C., Loayza D., Michaelis S.;
RT "Metabolic instability and constitutive endocytosis of STE6, the a-factor
RT transporter of Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 5:1185-1198(1994).
RN [10]
RP FUNCTION.
RX PubMed=7852314; DOI=10.1074/jbc.270.6.2525;
RA Lai K., Bolognese C.P., Swift S., McGraw P.;
RT "Regulation of inositol transport in Saccharomyces cerevisiae involves
RT inositol-induced changes in permease stability and endocytic degradation in
RT the vacuole.";
RL J. Biol. Chem. 270:2525-2534(1995).
RN [11]
RP FUNCTION.
RX PubMed=8991091; DOI=10.1083/jcb.135.6.1789;
RA Tan P.K., Howard J.P., Payne G.S.;
RT "The sequence NPFXD defines a new class of endocytosis signal in
RT Saccharomyces cerevisiae.";
RL J. Cell Biol. 135:1789-1800(1996).
RN [12]
RP FUNCTION.
RX PubMed=8741841; DOI=10.1091/mbc.7.1.81;
RA Robinson K.S., Lai K., Cannon T.A., McGraw P.;
RT "Inositol transport in Saccharomyces cerevisiae is regulated by
RT transcriptional and degradative endocytic mechanisms during the growth
RT cycle that are distinct from inositol-induced regulation.";
RL Mol. Biol. Cell 7:81-89(1996).
RN [13]
RP FUNCTION.
RX PubMed=9128251; DOI=10.1083/jcb.137.2.399;
RA Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P., Drubin D.G.;
RT "High rates of actin filament turnover in budding yeast and roles for actin
RT in establishment and maintenance of cell polarity revealed using the actin
RT inhibitor latrunculin-A.";
RL J. Cell Biol. 137:399-416(1997).
RN [14]
RP FUNCTION.
RX PubMed=9243513; DOI=10.1091/mbc.8.7.1361;
RA Moreau V., Galan J.-M., Devilliers G., Haguenauer-Tsapis R., Winsor B.;
RT "The yeast actin-related protein Arp2p is required for the internalization
RT step of endocytosis.";
RL Mol. Biol. Cell 8:1361-1375(1997).
RN [15]
RP FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
RX PubMed=9234686; DOI=10.1128/mcb.17.8.4294;
RA Tang H.-Y., Munn A., Cai M.;
RT "EH domain proteins Pan1p and End3p are components of a complex that plays
RT a dual role in organization of the cortical actin cytoskeleton and
RT endocytosis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:4294-4304(1997).
RN [16]
RP DOMAINS.
RX PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
RA Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
RA Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
RT "Recognition specificity of individual EH domains of mammals and yeast.";
RL EMBO J. 17:6541-6550(1998).
RN [17]
RP FUNCTION.
RX PubMed=9436999; DOI=10.1091/mbc.9.1.173;
RA Prescianotto-Baschong C., Riezman H.;
RT "Morphology of the yeast endocytic pathway.";
RL Mol. Biol. Cell 9:173-189(1998).
RN [18]
RP FUNCTION.
RX PubMed=9885245; DOI=10.1083/jcb.144.1.71;
RA Zeng G., Cai M.;
RT "Regulation of the actin cytoskeleton organization in yeast by a novel
RT serine/threonine kinase Prk1p.";
RL J. Cell Biol. 144:71-82(1999).
RN [19]
RP FUNCTION.
RX PubMed=10954428; DOI=10.1242/jcs.113.18.3309;
RA Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H.,
RA Haguenauer-Tsapis R.;
RT "A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in
RT endocytosis.";
RL J. Cell Sci. 113:3309-3319(2000).
RN [20]
RP FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
RX PubMed=10594004; DOI=10.1128/mcb.20.1.12-25.2000;
RA Tang H.-Y., Xu J., Cai M.;
RT "Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical
RT actin cytoskeleton organization, associate with each other and play
RT essential roles in cell wall morphogenesis.";
RL Mol. Cell. Biol. 20:12-25(2000).
RN [21]
RP FUNCTION.
RX PubMed=10972812; DOI=10.1046/j.1365-2958.2000.02063.x;
RA Eisfeld K., Riffer F., Mentges J., Schmitt M.J.;
RT "Endocytotic uptake and retrograde transport of a virally encoded killer
RT toxin in yeast.";
RL Mol. Microbiol. 37:926-940(2000).
RN [22]
RP INTERACTION WITH PAN1, AND IDENTIFICATION IN THE PAN1 COMPLEX.
RX PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
RA Zeng G., Yu X., Cai M.;
RT "Regulation of yeast actin cytoskeleton-regulatory complex
RT Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
RL Mol. Biol. Cell 12:3759-3772(2001).
RN [23]
RP INTERACTION WITH YAP1802.
RX PubMed=11940605; DOI=10.1083/jcb.200110027;
RA Howard J.P., Hutton J.L., Olson J.M., Payne G.S.;
RT "Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-
RT mediated endocytosis.";
RL J. Cell Biol. 157:315-326(2002).
RN [24]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [25]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [26]
RP FUNCTION.
RX PubMed=15248838; DOI=10.1042/bj20040392;
RA Aouida M., Leduc A., Wang H., Ramotar D.;
RT "Characterization of a transport and detoxification pathway for the
RT antitumour drug bleomycin in Saccharomyces cerevisiae.";
RL Biochem. J. 384:47-58(2004).
RN [27]
RP FUNCTION.
RX PubMed=15944351; DOI=10.1534/genetics.105.041459;
RA Morishita M., Engebrecht J.;
RT "End3p-mediated endocytosis is required for spore wall formation in
RT Saccharomyces cerevisiae.";
RL Genetics 170:1561-1574(2005).
RN [28]
RP FUNCTION.
RX PubMed=16914733; DOI=10.1128/mcb.00117-06;
RA Gourlay C.W., Ayscough K.R.;
RT "Actin-induced hyperactivation of the Ras signaling pathway leads to
RT apoptosis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:6487-6501(2006).
RN [29]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [30]
RP INTERACTION WITH SLA2.
RX PubMed=17151356; DOI=10.1091/mbc.e06-09-0788;
RA Toshima J., Toshima J.Y., Duncan M.C., Cope M.J.T.V., Sun Y., Martin A.C.,
RA Anderson S., Yates J.R. III, Mizuno K., Drubin D.G.;
RT "Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p,
RT by the Hip1R-related protein, Sla2p, during endocytosis.";
RL Mol. Biol. Cell 18:658-668(2007).
RN [31]
RP INTERACTION WITH SCD5.
RX PubMed=17898076; DOI=10.1091/mbc.e07-06-0607;
RA Zeng G., Huang B., Neo S.P., Wang J., Cai M.;
RT "Scd5p mediates phosphoregulation of actin and endocytosis by the type 1
RT phosphatase Glc7p in yeast.";
RL Mol. Biol. Cell 18:4885-4898(2007).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [33]
RP SUBCELLULAR LOCATION.
RX PubMed=18298676; DOI=10.1111/j.1600-0854.2008.00726.x;
RA Toret C.P., Lee L., Sekiya-Kawasaki M., Drubin D.G.;
RT "Multiple pathways regulate endocytic coat disassembly in Saccharomyces
RT cerevisiae for optimal downstream trafficking.";
RL Traffic 9:848-859(2008).
RN [34]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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. {ECO:0000269|PubMed:10594004,
CC ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:10972812,
CC ECO:0000269|PubMed:15248838, ECO:0000269|PubMed:15944351,
CC ECO:0000269|PubMed:16914733, ECO:0000269|PubMed:7841519,
CC ECO:0000269|PubMed:7852314, ECO:0000269|PubMed:7865884,
CC ECO:0000269|PubMed:8144575, ECO:0000269|PubMed:8380177,
CC ECO:0000269|PubMed:8741841, ECO:0000269|PubMed:8991091,
CC ECO:0000269|PubMed:9128251, ECO:0000269|PubMed:9234686,
CC ECO:0000269|PubMed:9243513, ECO:0000269|PubMed:9436999,
CC ECO:0000269|PubMed:9885245}.
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; the interaction with PAN1 is
CC prevented by PAN1 phosphorylation by PKR1.
CC {ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:11940605, ECO:0000269|PubMed:17151356,
CC ECO:0000269|PubMed:17898076, ECO:0000269|PubMed:9234686}.
CC -!- INTERACTION:
CC P39013; P32521: PAN1; NbExp=9; IntAct=EBI-6460, EBI-12875;
CC P39013; P32790: SLA1; NbExp=4; IntAct=EBI-6460, EBI-17313;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Endosome membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch.
CC Note=Cytoplasmic and cortical actin patches.
CC -!- MISCELLANEOUS: Present with 2610 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the END3 family. {ECO:0000305}.
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DR EMBL; X79473; CAA55981.1; -; Genomic_DNA.
DR EMBL; AF458969; AAM00520.1; -; Genomic_DNA.
DR EMBL; AF458970; AAM00526.1; -; Genomic_DNA.
DR EMBL; AF458971; AAM00532.1; -; Genomic_DNA.
DR EMBL; AF458972; AAM00538.1; -; Genomic_DNA.
DR EMBL; AF458973; AAM00544.1; -; Genomic_DNA.
DR EMBL; AF458974; AAM00550.1; -; Genomic_DNA.
DR EMBL; AF458975; AAM00556.1; -; Genomic_DNA.
DR EMBL; AF458976; AAM00562.1; -; Genomic_DNA.
DR EMBL; AF458977; AAM00568.1; -; Genomic_DNA.
DR EMBL; AF458978; AAM00574.1; -; Genomic_DNA.
DR EMBL; AF458979; AAM00580.1; -; Genomic_DNA.
DR EMBL; AF458980; AAM00586.1; -; Genomic_DNA.
DR EMBL; AF458981; AAM00592.1; -; Genomic_DNA.
DR EMBL; DQ115393; AAZ22524.1; -; Genomic_DNA.
DR EMBL; X89016; CAA61426.1; -; Genomic_DNA.
DR EMBL; Z71360; CAA95959.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10461.1; -; Genomic_DNA.
DR PIR; S57538; S57538.
DR RefSeq; NP_014315.1; NM_001182922.1.
DR AlphaFoldDB; P39013; -.
DR BioGRID; 35739; 343.
DR ComplexPortal; CPX-426; PAN1 actin cytoskeleton-regulatory complex.
DR DIP; DIP-2220N; -.
DR IntAct; P39013; 18.
DR MINT; P39013; -.
DR STRING; 4932.YNL084C; -.
DR iPTMnet; P39013; -.
DR MaxQB; P39013; -.
DR PaxDb; P39013; -.
DR PRIDE; P39013; -.
DR EnsemblFungi; YNL084C_mRNA; YNL084C; YNL084C.
DR GeneID; 855640; -.
DR KEGG; sce:YNL084C; -.
DR SGD; S000005028; END3.
DR VEuPathDB; FungiDB:YNL084C; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_040829_0_0_1; -.
DR InParanoid; P39013; -.
DR OMA; HCLRQRN; -.
DR BioCyc; YEAST:G3O-33113-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR PRO; PR:P39013; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P39013; protein.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
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; IPI:SGD.
DR GO; GO:0000147; P:actin cortical patch assembly; TAS:SGD.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; TAS:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; TAS:SGD.
DR GO; GO:0071555; P:cell wall organization; IMP:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
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; 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 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endocytosis; Endosome; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..349
FT /note="Actin cytoskeleton-regulatory complex protein END3"
FT /id="PRO_0000073648"
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:0007744|PubMed:18407956"
FT VARIANT 245
FT /note="D -> E (in strain: YJM 421)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 258
FT /note="S -> N (in strain: YJM 280, YJM 320, YJM 326, YJM
FT 627, YJM 789 and YJM 1129)"
FT /evidence="ECO:0000269|PubMed:11907579"
FT VARIANT 268
FT /note="D -> N (in strain: SK1, YJM 269, YJM 270, YJM 280,
FT YJM 320, YJM 326, YJM 339, YJM 421, YJM 627, YJM 789 and
FT YJM 1129)"
FT /evidence="ECO:0000269|PubMed:11907579,
FT ECO:0000269|PubMed:16273108"
SQ SEQUENCE 349 AA; 40297 MW; 0F6709AFF15B84EF 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 GQNSSSDSSG SNVLSNEDSI KQKYASLTDD QVANMREQLE GLLNYKKSEK
TQGGSKLSKR INIRSITDDL DNIEQQVEVL ENYLNNKRHE LQALQAEIN
