ID   END3_CHAGB              Reviewed;         402 AA.
AC   Q2H2V8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein END3;
DE   AltName: Full=Endocytosis protein 3;
GN   Name=END3; ORFNames=CHGG_03888;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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; CH408032; EAQ87269.1; -; Genomic_DNA.
DR   RefSeq; XP_001223102.1; XM_001223101.1.
DR   AlphaFoldDB; Q2H2V8; -.
DR   STRING; 38033.XP_001223102.1; -.
DR   EnsemblFungi; EAQ87269; EAQ87269; CHGG_03888.
DR   GeneID; 4391596; -.
DR   eggNOG; KOG0998; Eukaryota.
DR   HOGENOM; CLU_040829_0_0_1; -.
DR   InParanoid; Q2H2V8; -.
DR   OMA; SNKIDYQ; -.
DR   OrthoDB; 597979at2759; -.
DR   Proteomes; UP000001056; 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..402
FT                   /note="Actin cytoskeleton-regulatory complex protein END3"
FT                   /id="PRO_0000349445"
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   COILED          285..401
FT                   /evidence="ECO:0000255"
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   402 AA;  45363 MW;  3C66E4F61DE926D3 CRC64;
     MAPRIEAQEI ETYWNIFSTR TNGGKFLNGE QAAPVLKNSG LRDDQLERVW DLADVDNDGN
     LDFEEFCVAM RVIFDLLNGE YADVPTTLPD WLVPESKAHL VQANRALTGK AVQFEQVEDE
     DDSPGLKDGF DWYMSPADKA KYEQIYQENR DMRGEVAFSA LQDLYESLEV PDTDIRSAWN
     LINPSAGSSI NKDACLAFLH ILNNRHEGFR IPRTVPASLR ASFERNQIDY QIDSARNNAA
     AQSRWATRAD DETSTGRKAK FGDQYLTRLG RSGFKSAGTD FSSGAKTDAE WEEVRLKKQL
     AELDEKMAKV EAGVERRKGG QRDSKPALVK RELDQLLDYK RKQLRELEEG GGAAKAGGNL
     KSVGEDLQTV REQVEGLEGH LRSRQEVLEQ LRREIEDERA GR