EXO84_KLULA
ID EXO84_KLULA Reviewed; 720 AA.
AC Q6CNM8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Exocyst complex component EXO84;
GN Name=EXO84; OrderedLocusNames=KLLA0E11319g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99548.1; -; Genomic_DNA.
DR RefSeq; XP_454461.1; XM_454461.1.
DR AlphaFoldDB; Q6CNM8; -.
DR SMR; Q6CNM8; -.
DR STRING; 28985.XP_454461.1; -.
DR PRIDE; Q6CNM8; -.
DR EnsemblFungi; CAG99548; CAG99548; KLLA0_E11353g.
DR GeneID; 2894545; -.
DR KEGG; kla:KLLA0_E11353g; -.
DR eggNOG; KOG2215; Eukaryota.
DR HOGENOM; CLU_014732_0_0_1; -.
DR InParanoid; Q6CNM8; -.
DR OMA; SACVKWA; -.
DR Proteomes; UP000000598; Chromosome E.
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; 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..720
FT /note="Exocyst complex component EXO84"
FT /id="PRO_0000118983"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 168..252
FT /evidence="ECO:0000255"
FT COMPBIAS 17..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 188
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 720 AA; 81770 MW; 14EE0E3C9B9365C3 CRC64;
MVDFSLKKHG VSSWGRGSLS RKESSAGDSS STFKSSRYQD MKVSDPELPK VSAKERSKAG
TMMKRRLSVH QSNNFGAVKM DFDNMPALPS SAADYSFASN VGNATQTSLI TEDQLPDRNT
SLASLNTNTR RPDQELYSSK SLRQILSNPD FKAKKFITEK LGDATAVDID QFTSNLNDLS
LEIQDEIKFN IDKSFKEILI VNKGLETATT ELKVLRTKVQ EMKDIMNQFV TIAEKKLQAE
QAANETADLN RTSSSASLSN HSLLPPLKPT PSATRKDRTS VYILERMWNE ELMTLFKNVD
GAHKYITSTP GRHILLESDN WIEINPATLK PLQKVRLFIL NDVVLIAAPK PSKQTELTVS
RFSPLRDVTV EVQSEHELSF NFSNKQHTLY RHRDPQVFSK VIDIIRQAKD ALREISQAEE
DTTRKIRNSY TLLQQERTPN RDATTSPVKV HGRQRSYGGT GTPSRHRSDA QNDALLTNIT
RSIHVRMGSE ETTEVTKRLK RLDDALEDLD LEIGRQNFDL AITKLNHIQS SLKSLYSSAT
FDESVMVELL SLKCSQRKTI LYTKLTNLLA CETSDMTKLK SYMLNLVALN EPVDALEVFL
QNRSNFINDL TLQIGIIDNV TSFITQVAII RFQTLKKVTQ QYLEVSKNLK RDYTSLLVCW
CSEEVDKHFQ LMERELSNSS TLSVQAIKIT RKQIDELKPV GMDYVYKLDD FIRRNNNRIL
