EXO84_CANGA
ID EXO84_CANGA Reviewed; 764 AA.
AC Q6FM00;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Exocyst complex component EXO84;
GN Name=EXO84; OrderedLocusNames=CAGL0K12166g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380957; CAG61707.1; -; Genomic_DNA.
DR RefSeq; XP_448744.1; XM_448744.1.
DR AlphaFoldDB; Q6FM00; -.
DR SMR; Q6FM00; -.
DR STRING; 5478.XP_448744.1; -.
DR PRIDE; Q6FM00; -.
DR EnsemblFungi; CAG61707; CAG61707; CAGL0K12166g.
DR GeneID; 2889972; -.
DR KEGG; cgr:CAGL0K12166g; -.
DR CGD; CAL0134525; CAGL0K12166g.
DR VEuPathDB; FungiDB:CAGL0K12166g; -.
DR eggNOG; KOG2215; Eukaryota.
DR HOGENOM; CLU_014732_0_0_1; -.
DR InParanoid; Q6FM00; -.
DR OMA; SACVKWA; -.
DR Proteomes; UP000002428; Chromosome K.
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; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
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; 2.
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..764
FT /note="Exocyst complex component EXO84"
FT /id="PRO_0000118979"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 239..272
FT /evidence="ECO:0000255"
FT COMPBIAS 10..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 764 AA; 86315 MW; 756789BE5D90DF00 CRC64;
MVDFSLRKTR NYWKGSNSSS KQNSEVSLKN AEKKKPVTNP YANLTVPNAA NLPTLDAKER
NKAASSMQRR LSIHTANYTA PNLDYSMPLP SSNLIDQAMG DEQPTGKVPA INVDDEYGQR
NGHSRSATPT DNETSRRPET LRPPELNRKR LGGSGSSAPS GSSRMTMVAP LNPLSPYANL
FHPASLRKIL SDPQFSAKKF IHERLSEASA VDIDLFTSNL TELSTDVQEE VKRNIYKSYN
EIITVNNDLH EASAELKQLR SSISELTKVT DQFVTVAKSR IQMDEQQKML HTQRPSSPQK
TQSSSLLPPV SSDINGTNPK RDRTSVMILE KMWDTQLATL YKNVEGAQKH LGPASNRHLL
IESSDWTELN ISTQKPLQTV QLYILNDAVL VAGKTKNKQH ELIVSQCCPI RDVTISTDRE
YRTKLMFNFG NSNTCLYETR DINECMRVLD AFRKAKDDLR DITENEKENS KRIKESLVYL
QNTQQTPGRE GSKSPAKRRS MGLSPSSASR PLSASMDQFI LQNLSISVHS RSKSHDWSSL
SHKFKLVDNL IEEVDIDLAR LKFDSAVNTL LEAESQLATM KDPTKEEDAI ILNVLTLKLD
QRRDDILTKV TQRNLFINEI AHLREGVKTL IRLGLPEAGL DLLLQNKSNL IQELLLQVGS
SEHPSLYLTE LAIVRFQIIK RTVIVFRELF HRDHDKLSSI LVSWCSHEVE KHFNLVSKQL
LNGDKLSPDA IRYSRKQIDD LKTVGLDFVY KLDEFIKNNI NKLG
