EXO84_YEAST
ID EXO84_YEAST Reviewed; 753 AA.
AC P38261; D6VQA1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Exocyst complex component EXO84;
DE AltName: Full=Exocyst complex protein of 84 kDa;
DE AltName: Full=U1 SNP1-associating protein 3;
GN Name=EXO84; Synonyms=USA3; OrderedLocusNames=YBR102C; ORFNames=YBR0831;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP FUNCTION, INTERACTION WITH SEC5; SEC8 AND SEC10, AND SUBCELLULAR LOCATION.
RX PubMed=10438536; DOI=10.1074/jbc.274.33.23558;
RA Guo W., Grant A., Novick P.;
RT "Exo84p is an exocyst protein essential for secretion.";
RL J. Biol. Chem. 274:23558-23564(1999).
RN [5]
RP FUNCTION, AND INTERACTION WITH SNP1.
RX PubMed=11425851; DOI=10.1074/jbc.m100022200;
RA Awasthi S., Palmer R., Castro M., Mobarak C.D., Ruby S.W.;
RT "New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing.";
RL J. Biol. Chem. 276:31004-31015(2001).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15583031; DOI=10.1083/jcb.200408124;
RA Boyd C., Hughes T., Pypaert M., Novick P.;
RT "Vesicles carry most exocyst subunits to exocytic sites marked by the
RT remaining two subunits, Sec3p and Exo70p.";
RL J. Cell Biol. 167:889-901(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15788396; DOI=10.1074/jbc.m500511200;
RA Zhang X., Zajac A., Zhang J., Wang P., Li M., Murray J., TerBush D.R.,
RA Guo W.;
RT "The critical role of EXO84P in the organization and polarized localization
RT of the exocyst complex.";
RL J. Biol. Chem. 280:20356-20364(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 523-753.
RX PubMed=16249794; DOI=10.1038/nsmb1017;
RA Dong G., Hutagalung A.H., Fu C., Novick P., Reinisch K.M.;
RT "The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains
RT reveal a common motif.";
RL Nat. Struct. Mol. Biol. 12:1094-1100(2005).
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 exocytosis
CC and to the budding site. Also involved in assembly of the spliceosome.
CC {ECO:0000269|PubMed:10438536, ECO:0000269|PubMed:11425851,
CC ECO:0000269|PubMed:15788396}.
CC -!- SUBUNIT: Component of the exocyst complex composed of SEC3, SEC5, SEC6,
CC SEC8, SEC10, SEC15, EXO70 and EXO84. Interacts also with SNP1.
CC {ECO:0000269|PubMed:10438536, ECO:0000269|PubMed:11425851}.
CC -!- INTERACTION:
CC P38261; P19658: EXO70; NbExp=2; IntAct=EBI-21567, EBI-6717;
CC P38261; Q06245: SEC10; NbExp=5; IntAct=EBI-21567, EBI-16504;
CC P38261; P22224: SEC15; NbExp=3; IntAct=EBI-21567, EBI-16543;
CC P38261; P89102: SEC5; NbExp=5; IntAct=EBI-21567, EBI-16865;
CC P38261; P32855: SEC8; NbExp=4; IntAct=EBI-21567, EBI-16896;
CC P38261; Q00916: SNP1; NbExp=2; IntAct=EBI-21567, EBI-724;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle. Bud. Bud
CC neck. Note=Cell periphery, bud and bud neck. The polarization of EXO84
CC requires actin cables.
CC -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
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DR EMBL; X78993; CAA55605.1; -; Genomic_DNA.
DR EMBL; Z35971; CAA85057.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07221.1; -; Genomic_DNA.
DR PIR; S48267; S48267.
DR RefSeq; NP_009660.1; NM_001178450.1.
DR PDB; 2D2S; X-ray; 2.85 A; A=523-753.
DR PDB; 5YFP; EM; 4.40 A; H=1-753.
DR PDB; 6VKL; EM; 4.40 A; H=1-753.
DR PDBsum; 2D2S; -.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P38261; -.
DR SMR; P38261; -.
DR BioGRID; 32806; 321.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-2732N; -.
DR IntAct; P38261; 19.
DR MINT; P38261; -.
DR STRING; 4932.YBR102C; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P38261; -.
DR MaxQB; P38261; -.
DR PaxDb; P38261; -.
DR PRIDE; P38261; -.
DR EnsemblFungi; YBR102C_mRNA; YBR102C; YBR102C.
DR GeneID; 852398; -.
DR KEGG; sce:YBR102C; -.
DR SGD; S000000306; EXO84.
DR VEuPathDB; FungiDB:YBR102C; -.
DR eggNOG; KOG2215; Eukaryota.
DR GeneTree; ENSGT00390000015936; -.
DR HOGENOM; CLU_014732_0_0_1; -.
DR InParanoid; P38261; -.
DR OMA; SACVKWA; -.
DR BioCyc; YEAST:G3O-29064-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR EvolutionaryTrace; P38261; -.
DR PRO; PR:P38261; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38261; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000145; C:exocyst; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0001927; P:exocyst assembly; IMP:SGD.
DR GO; GO:0051601; P:exocyst localization; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
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; IMP:SGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IC:ComplexPortal.
DR GO; GO:0090522; P:vesicle tethering involved in exocytosis; IC:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasmic vesicle; Exocytosis;
KW Isopeptide bond; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..753
FT /note="Exocyst complex component EXO84"
FT /id="PRO_0000118987"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 227..279
FT /evidence="ECO:0000255"
FT COILED 531..585
FT /evidence="ECO:0000255"
FT COMPBIAS 16..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT HELIX 528..548
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 552..568
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 579..604
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 609..621
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 625..645
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 653..678
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 684..708
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 717..728
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 729..733
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:2D2S"
FT HELIX 747..751
FT /evidence="ECO:0007829|PDB:2D2S"
SQ SEQUENCE 753 AA; 85538 MW; 1BCDE834466C3536 CRC64;
MVEFSLKKAR NNWKHVKKSA SSPAKQKTPP SPAKPKQKTK KNPYSDLKDP ATSYTLPTIN
ARERSRVATS MQRRLSIHNT NYAPPTLDYS MPLPDMPNMI VPNDNVDSSH NNSSFTTENE
SVSSKGPSNS LNLSTADLSL NDSSYNKVPA RSAMRNTVNP SGSNDPFNNS TSLRKMLANP
HFNAKDFVHD KLGNASAITI DKFTSNLTDL SIQVQEEVKL NINKSYNEIM TVNNDLNVAM
LELKRVRANI NDLNEVLDQC TKIAEKRLQL QDQIDQERQG NFNNVESHSN SPALLPPLKA
GQNGNLMRRD RSSVLILEKF WDTELDQLFK NVEGAQKFIN STKGRHILMN SANWMELNTT
TGKPLQMVQI FILNDLVLIA DKSRDKQNDF IVSQCYPLKD VTVTQEEFST KRLLFKFSNS
NSSLYECRDA DECSRLLDVI RKAKDDLCDI FHVEEENSKR IRESFRYLQS TQQTPGRENN
RSPNKNKRRS MGGSITPGRN VTGAMDQYLL QNLTLSMHSR PRSRDMSSTA QRLKFLDEGV
EEIDIELARL RFESAVETLL DIESQLEDLS ERISDEELML LNLISLKIEQ RREAISSKLS
QSILSSNEIV HLKSGTENMI KLGLPEQALD LFLQNRSNFI QDLILQIGSV DNPTNYLTQL
AVIRFQTIKK TVEDFQDIFK ELGAKISSIL VDWCSDEVDN HFKLIDKQLL NDEMLSPGSI
KSSRKQIDGL KAVGLDFVYK LDEFIKKNSD KIR
