END3_EMENI
ID END3_EMENI Reviewed; 404 AA.
AC Q5BEK7; C8VU41; Q12076;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 105.
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=AN1023;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=FGSC 26;
RX PubMed=10102359; DOI=10.1007/s004380050964;
RA Jones G.W., Hooley P., Farrington S.M., Shawcross S.G., Iwanejko L.A.,
RA Strike P.;
RT "Cloning and characterisation of the sagA gene of Aspergillus nidulans: a
RT gene which affects sensitivity to DNA-damaging agents.";
RL Mol. Gen. Genet. 261:251-258(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:10102359}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28746.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAA65591.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U28804; AAC28746.1; ALT_FRAME; mRNA.
DR EMBL; AACD01000015; EAA65591.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF88316.1; -; Genomic_DNA.
DR RefSeq; XP_658627.1; XM_653535.1.
DR AlphaFoldDB; Q5BEK7; -.
DR STRING; 162425.CADANIAP00001624; -.
DR PRIDE; Q5BEK7; -.
DR EnsemblFungi; CBF88316; CBF88316; ANIA_01023.
DR EnsemblFungi; EAA65591; EAA65591; AN1023.2.
DR GeneID; 2876800; -.
DR KEGG; ani:AN1023.2; -.
DR VEuPathDB; FungiDB:AN1023; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_040829_0_0_1; -.
DR InParanoid; Q5BEK7; -.
DR OMA; SNKIDYQ; -.
DR OrthoDB; 597979at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
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:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:AspGD.
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 2: Evidence at transcript level;
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_0000349448"
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 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"
FT CONFLICT 39
FT /note="N -> S (in Ref. 1; AAC28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="E -> V (in Ref. 1; AAC28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> G (in Ref. 1; AAC28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="E -> Q (in Ref. 1; AAC28746)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="E -> D (in Ref. 1; AAC28746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 45995 MW; 409B8579900207D9 CRC64;
MSNKKIEQWE VERYWEIFSS LAGGQPHLNN SQAASVLRNS RLRDDQLEKV WDLADLDGDG
ELDFEEFCVA MRLVFDLVNG ELPQVPKSLP DWLVPESKAH LVQATRALSG GQEQFERIED
EDSTPGLKDG FDWYMSPEDK AKYEEIYSAN KNQRGEIAFG SLEPLYESLD VPDTDIRSAW
NLVNPSAAPE INKDATLAFL HILNYRHEGY RIPRTIPASL RASFENNKID YQLDSARPAQ
KWGTNGDTET STGRKAKFGD TYLSRLGVAG KTSYTPKGTD FSDTIQDEEW EKVRLRRELA
ELDAKLQAAN KAVEGRKAGN RNDGRPNWVL IKKEALQLLE YKERELRELR EGSGRAKAGG
DVERLREDVR TVGEQVDGLK NHLIQRKGVL EDLRREIEDE RASR
