ID   EXO84_ASHGO             Reviewed;         697 AA.
AC   Q75B91;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Exocyst complex component EXO84;
GN   Name=EXO84; OrderedLocusNames=ADL321W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 259; 262 AND 408.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR   EMBL; AE016817; AAS51599.2; -; Genomic_DNA.
DR   RefSeq; NP_983775.2; NM_209128.2.
DR   AlphaFoldDB; Q75B91; -.
DR   SMR; Q75B91; -.
DR   STRING; 33169.AAS51599; -.
DR   EnsemblFungi; AAS51599; AAS51599; AGOS_ADL321W.
DR   GeneID; 4619910; -.
DR   KEGG; ago:AGOS_ADL321W; -.
DR   eggNOG; KOG2215; Eukaryota.
DR   HOGENOM; CLU_014732_0_0_1; -.
DR   InParanoid; Q75B91; -.
DR   OMA; SACVKWA; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR   GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR   GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0001927; P:exocyst assembly; IEA:EnsemblFungi.
DR   GO; GO:0051601; P:exocyst localization; IEA:EnsemblFungi.
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   GO; GO:0000245; P:spliceosomal complex assembly; IEA:EnsemblFungi.
DR   Gene3D; 1.20.58.1210; -; 1.
DR   Gene3D; 1.20.58.1220; -; 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; IPR042560; Exo84_C_2.
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; Isopeptide bond;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation.
FT   CHAIN           1..697
FT                   /note="Exocyst complex component EXO84"
FT                   /id="PRO_0000118976"
FT   REGION          13..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          149..212
FT                   /evidence="ECO:0000255"
FT   COILED          377..407
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        169
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   697 AA;  78864 MW;  E4F3E08DCA1FCA88 CRC64;
     MVDFSLRKAR NNWSKLSSPG KTRQQGSPTK LKSNAYEDFV SPRDTLQLPE IGMKDRRKVG
     TSMQRRLSVH NAKYIPPPID YASAPALPTA VELPVRDNSL LSSELMKPNH RRPPVDIYGG
     RSLREILSNP QFQAKRFVHE KLGDATALEI DHFASNLNHL SQEIEQEIKS NINKSYNELM
     QVNKELAVAS TELKDLRSKV QQLQVVMGQF TAMAEKRLLL EKEHFRQSNT SVMTTKSGST
     GSGLLPPVKS GAAKKDRSSV IILEKIWTNE LSSLFRSVEG AQKYIAPAPG RRILLESNDW
     MEINIATLKP LHATRIFLLN DMILVAVCRS DKKGELVANQ CCSLRELTVA EESNYTLSFH
     FGNKHHSLYR SRTPTGYTAL LNEIKSAKDE LRDIYQAEED NARKLRDSFT YLQSTQQSPS
     RDISSPARGH SRQRSLGTLQ NTPSRASTYQ ENLLQNISMS MHTRSRSGGV NQTAVKLNLV
     YEELEELSVP VTRMNFGLAI KKLHSIENIL KGITAEAEGE VMLLNLLRMK CNQTRTLITQ
     KLTHVINTEY SDANKLESST KSLILLGMPA EALQLFLHNR SNFIQDLVLQ VGVHDNSNSY
     ITQVAVIRCQ TIKKVAIQFQ KLFEGTTAKY SSVLVSWCND EVDKHFFLMK KQLINDDQLT
     PQAIKISRKQ IDELKSVGMD FVYKLDDFLK IHSNKIY