ID   EXO84_EMENI             Reviewed;         666 AA.
AC   Q5BFX0; C8VSK6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Exocyst complex component exo84;
GN   Name=exo84; ORFNames=AN0560;
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 [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   [2]
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: Involved in the secretory pathway as part of the exocyst
CC       complex which tethers secretory vesicles to the sites of exocytosis.
CC       Plays a role in both the assembly of the exocyst and the polarization
CC       of this complex to specific sites of the plasma membrane for
CC       exocytosis. Also involved in assembly of the spliceosome (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the exocyst complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC       {ECO:0000250}. Note=Cell periphery. The polarization of EXO84 requires
CC       actin cables (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AACD01000007; EAA66659.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89232.1; -; Genomic_DNA.
DR   RefSeq; XP_658164.1; XM_653072.1.
DR   AlphaFoldDB; Q5BFX0; -.
DR   SMR; Q5BFX0; -.
DR   STRING; 162425.CADANIAP00002118; -.
DR   PRIDE; Q5BFX0; -.
DR   EnsemblFungi; CBF89232; CBF89232; ANIA_00560.
DR   EnsemblFungi; EAA66659; EAA66659; AN0560.2.
DR   GeneID; 2876338; -.
DR   KEGG; ani:AN0560.2; -.
DR   eggNOG; KOG2215; Eukaryota.
DR   HOGENOM; CLU_012488_2_0_1; -.
DR   InParanoid; Q5BFX0; -.
DR   OMA; SACVKWA; -.
DR   OrthoDB; 1357584at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR   GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1210; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR   InterPro; IPR033961; Exo84.
DR   InterPro; IPR032403; Exo84_C.
DR   InterPro; IPR042561; Exo84_C_1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR21426; PTHR21426; 1.
DR   Pfam; PF16528; Exo84_C; 1.
DR   SUPFAM; SSF74788; SSF74788; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytoplasmic vesicle; Exocytosis; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..666
FT                   /note="Exocyst complex component exo84"
FT                   /id="PRO_0000118981"
FT   REGION          1..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          133..200
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        25..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  73935 MW;  318AD5D61D723D37 CRC64;
     MDGRGLTLRS KNRRPRPQIS APKPISGPLP QNHQPAASGS GTASSGSGSR DYASSNHATS
     DLVKRRYSTR FNQVPDFDGA PPVPSVPQVP SAYAGLGPPQ PSRKQSAESS GPPEVDLTAL
     RDPSLPVDRY VTNLLANASE DDIREYQQAL RKVKNRTSTD LQQNVYQNRT QFIRISQEAD
     KLKGEMKTLR SLMAELTTAL GQTAIGDSPN PMSPTLDERA SKRSNRSSVA NLESMWNVQL
     QTLWKTVEGS QKFLPMVPGR HIVLETGNWA ELDSATWKPR RPVHLVLLND HLLVAAKKRK
     RVDQSNPNHR GPVPTKLIAE ECWPLQDIDM IDLGANLTGS AREEAEDRGI TNAVCVRVGS
     KPFTYRHDKR NSTAKSELLA TFRKTVEDLR RTLRSETEAA GKNGESLGFM SAINSRNSLL
     CSPKLDLSEN TDNPRDRPEV RIDVDGKQQN LRWVDSQVDE LDIDIALQRF EEAVSNIDRL
     RKLARGLKGN AVAQDVINTK VDERAAKLAG ILSRSLVDTH GFPVATKTNV VWLTRLGFED
     QARESYLKAR SDVISKRIRT YQQCFPSVMT SACIKWAKHH LDAFNALLTR QLSSVQRGAT
     VWQNCINIVH EQAGILAEVG VDFTDLVAKE LELTEEEKAA RPEMTRSESL IMGLADAASF
     FNMYGH