ID   EXO84_CANAL             Reviewed;         791 AA.
AC   Q59XM1; A0A1D8PPK5; Q59WR9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 3.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Exocyst complex component EXO84;
GN   Name=EXO84; OrderedLocusNames=CAALFM_C601280WA;
GN   ORFNames=CaO19.135, CaO19.7779;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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}.
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; CP017628; AOW30069.1; -; Genomic_DNA.
DR   RefSeq; XP_714341.2; XM_709248.2.
DR   AlphaFoldDB; Q59XM1; -.
DR   BioGRID; 1227116; 3.
DR   STRING; 237561.Q59XM1; -.
DR   PRIDE; Q59XM1; -.
DR   GeneID; 3644022; -.
DR   KEGG; cal:CAALFM_C601280WA; -.
DR   CGD; CAL0000174176; EXO84.
DR   VEuPathDB; FungiDB:C6_01280W_A; -.
DR   HOGENOM; CLU_024067_0_0_1; -.
DR   InParanoid; Q59XM1; -.
DR   OMA; RWHEINV; -.
DR   OrthoDB; 1357584at2759; -.
DR   PRO; PR:Q59XM1; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0000145; C:exocyst; ISO:CGD.
DR   GO; GO:0001411; C:hyphal tip; IDA:CGD.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; ISO:CGD.
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; 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..791
FT                   /note="Exocyst complex component EXO84"
FT                   /id="PRO_0000118978"
FT   REGION          16..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          432..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          190..229
FT                   /evidence="ECO:0000255"
FT   COILED          521..577
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        21..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        193
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   791 AA;  88593 MW;  19842E278F76A738 CRC64;
     MDNLDPNSSL QVEKLRNRKS RAVWQNNNTT THNNPYANLS TGEKSRSRHN TGSSYVSPYG
     GGNGEENAYT GNNNKSNTSG NLLQVPGAGG GGDLNSNKKQ SRRMSIHVSA RQHGRSFSQT
     GPIDMANLPA LPKIGGVTTS GVGGAGGDVM TRTGGLTIEQ KIFKELSQGS AAEVDDYYKT
     LLKQKNLITR DIKDNINQNQ KNILQLTKDL KETQEELIEL RGTTKELYEV LGYFKESAQR
     RLELEFEPET QKELHSPQKS NQLGIPSNKK KDRSSIMVLK KMWDSQLQSL FKHVDGASKF
     VQPLPNRHIV AESGRWFEVN VGNWKPSYPT HLFIFNDLIL IAVKKSSSSS QEPTTGGSNG
     GSKSRLQAVQ CWPLTQVSLQ QIKSPKKDDD KMYFINLKSK SLSYVYSTDR YDHFVKVTEA
     FNKGRNEMIQ SERLLDSRLS SPSNNNGDSK EEKRQLRESL RNSGNYKEGV TDDAGGAATG
     GGRKSAGTPN RNSTDYVLHD ISARVHSRNR SQDLGNNFKL ANNGKSQFFN EIKTLEDRLD
     DVDVEISHNQ YAEAVELISI IESKLRNIEN ALTNQRNGGK NVNIADELLL LDVSKLKIKN
     RKENVSNGLI FDLQHNIAKL KQDDIDNILT LFDNLEQLDR GVQGYLDSMS AYLSTTVSKL
     IVGLQGSTKI DVVNYLSNLM VINVSIVKRT IQTYEQIIAP ILKRHGDVDS SGLINWCIDE
     FTKLCKQIKK HLYGTLLISS GINMETDEPI YKVKERKLYD NFLKIMQPQL EELKSVGLNV
     DYIFESILNL E