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Database: UniProt
Entry: Q5BEK7
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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   16-APR-2014, entry version 68.
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
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
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
RT   nidulans: a 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.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   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.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory
CC       complex required for the internalization of endosomes during
CC       actin-coupled endocytosis. The complex links the site of
CC       endocytosis to the cell membrane-associated actin cytoskeleton.
CC       Mediates uptake of external molecules and vacuolar degradation of
CC       plasma membrane proteins. Plays a role in the proper organization
CC       of the cell membrane-associated actin cytoskeleton and promotes
CC       its destabilization (By similarity).
CC   -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Endosome membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Cytoplasm,
CC       cytoskeleton, actin patch (By similarity). Note=Cytoplasmic and
CC       cortical actin patches (By similarity).
CC   -!- SIMILARITY: Belongs to the END3 family.
CC   -!- SIMILARITY: Contains 2 EH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC28746.1; Type=Frameshift; Positions=364, 396, 401;
CC       Sequence=EAA65591.1; Type=Erroneous gene model prediction;
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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   EnsemblFungi; CADANIAT00001624; CADANIAP00001624; CADANIAG00001624.
DR   GeneID; 2876800; -.
DR   KEGG; ani:AN1023.2; -.
DR   eggNOG; NOG331512; -.
DR   HOGENOM; HOG000076607; -.
DR   OMA; YDSLDVP; -.
DR   OrthoDB; EOG7RZ623; -.
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:0005509; F:calcium ion binding; IEA:InterPro.
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; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.238.10; -; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR025604; End3.
DR   InterPro; IPR000261; EPS15_homology.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF12761; End3; 1.
DR   SMART; SM00027; EH; 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; Cell membrane; Coiled coil; Complete proteome;
KW   Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Membrane;
KW   Reference proteome; Repeat.
FT   CHAIN         1    404       Actin cytoskeleton-regulatory complex
FT                                protein end3.
FT                                /FTId=PRO_0000349448.
FT   DOMAIN       10    100       EH 1.
FT   DOMAIN      139    227       EH 2.
FT   COILED      280    399       Potential.
FT   CONFLICT     39     39       N -> S (in Ref. 1; AAC28746).
FT   CONFLICT     81     81       E -> V (in Ref. 1; AAC28746).
FT   CONFLICT    188    188       A -> G (in Ref. 1; AAC28746).
FT   CONFLICT    396    396       E -> Q (in Ref. 1; AAC28746).
FT   CONFLICT    398    398       E -> D (in Ref. 1; AAC28746).
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
//
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