EXO70_YEAST
ID EXO70_YEAST Reviewed; 623 AA.
AC P19658; D6VW98; E9P961;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Exocyst complex component EXO70;
DE AltName: Full=Exocyst complex protein of 70 kDa;
GN Name=EXO70; OrderedLocusNames=YJL085W; ORFNames=J0932;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 36-52, AND
RP IDENTIFICATION IN THE EXOCYST COMPLEX.
RX PubMed=8978675; DOI=10.1002/j.1460-2075.1996.tb01039.x;
RA TerBush D.R., Maurice T., Roth D., Novick P.;
RT "The Exocyst is a multiprotein complex required for exocytosis in
RT Saccharomyces cerevisiae.";
RL EMBO J. 15:6483-6494(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3317276; DOI=10.1093/nar/15.21.9079;
RA Komatsoulis G.A., Westaway S.K., Abelson J.;
RT "Nucleotide sequence of ORF2: an open reading frame upstream of the tRNA
RT ligase gene.";
RL Nucleic Acids Res. 15:9079-9079(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7483841; DOI=10.1002/yea.320110709;
RA Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT cerevisiae chromosome X, including putative proteins with leucine zippers,
RT a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT alpha 2 binding site.";
RL Yeast 11:681-689(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70.
RC STRAIN=EJ101;
RX PubMed=3277966; DOI=10.1016/s0021-9258(18)69050-7;
RA Westaway S.K., Phizicky E.M., Abelson J.;
RT "Structure and function of the yeast tRNA ligase gene.";
RL J. Biol. Chem. 263:3171-3176(1988).
RN [8]
RP INTERACTION WITH RHO3.
RX PubMed=10207081; DOI=10.1128/mcb.19.5.3580;
RA Robinson N.G.G., Guo L., Imai J., Toh-e A., Matsui Y., Tamanoi F.;
RT "Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton
RT and exocytosis, is a GTPase which interacts with Myo2 and Exo70.";
RL Mol. Cell. Biol. 19:3580-3587(1999).
RN [9]
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 [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION.
RX PubMed=15583030; DOI=10.1083/jcb.200408001;
RA Wiederkehr A., De Craene J.-O., Ferro-Novick S., Novick P.;
RT "Functional specialization within a vesicle tethering complex: bypass of a
RT subset of exocyst deletion mutants by Sec1p or Sec4p.";
RL J. Cell Biol. 167:875-887(2004).
RN [12]
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 [13]
RP 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 63-623, AND INTERACTION WITH RHO3.
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 the assembly of the exocyst.
CC {ECO:0000269|PubMed:15583030}.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, SEC15, EXO70 and EXO84. Interacts with RHO3.
CC {ECO:0000269|PubMed:10207081, ECO:0000269|PubMed:16249794,
CC ECO:0000269|PubMed:8978675}.
CC -!- INTERACTION:
CC P19658; P38261: EXO84; NbExp=2; IntAct=EBI-6717, EBI-21567;
CC P19658; Q00245: RHO3; NbExp=4; IntAct=EBI-6717, EBI-15138;
CC P19658; Q06245: SEC10; NbExp=2; IntAct=EBI-6717, EBI-16504;
CC P19658; P22224: SEC15; NbExp=2; IntAct=EBI-6717, EBI-16543;
CC P19658; P32844: SEC6; NbExp=3; IntAct=EBI-6717, EBI-16874;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000269|PubMed:15583031}. Bud {ECO:0000269|PubMed:15788396}. Bud
CC neck {ECO:0000305}. Note=Its polarization in the cell depends on EXO84.
CC {ECO:0000269|PubMed:15788396}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
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DR EMBL; Y08787; CAA70039.1; -; Genomic_DNA.
DR EMBL; Y00473; CAA68535.1; -; Genomic_DNA.
DR EMBL; X83502; CAA58485.1; -; Genomic_DNA.
DR EMBL; Z49362; CAA89380.1; -; Genomic_DNA.
DR EMBL; AY723833; AAU09750.1; -; Genomic_DNA.
DR EMBL; J03546; AAA66919.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08714.1; -; Genomic_DNA.
DR PIR; A27300; A27300.
DR RefSeq; NP_012450.1; NM_001181518.1.
DR PDB; 2B1E; X-ray; 2.00 A; A=63-623.
DR PDB; 2B7M; X-ray; 3.50 A; A/B/C/D=63-623.
DR PDB; 2PFV; X-ray; 2.10 A; A=63-623.
DR PDB; 5YFP; EM; 4.40 A; G=1-623.
DR PDB; 6VKL; EM; 4.40 A; G=1-623.
DR PDBsum; 2B1E; -.
DR PDBsum; 2B7M; -.
DR PDBsum; 2PFV; -.
DR PDBsum; 5YFP; -.
DR PDBsum; 6VKL; -.
DR AlphaFoldDB; P19658; -.
DR SMR; P19658; -.
DR BioGRID; 33671; 529.
DR ComplexPortal; CPX-1890; Exocyst.
DR DIP; DIP-2934N; -.
DR IntAct; P19658; 10.
DR MINT; P19658; -.
DR STRING; 4932.YJL085W; -.
DR TCDB; 1.F.2.1.1; the octameric exocyst (exocyst) family.
DR iPTMnet; P19658; -.
DR MaxQB; P19658; -.
DR PaxDb; P19658; -.
DR PRIDE; P19658; -.
DR EnsemblFungi; YJL085W_mRNA; YJL085W; YJL085W.
DR GeneID; 853359; -.
DR KEGG; sce:YJL085W; -.
DR SGD; S000003621; EXO70.
DR VEuPathDB; FungiDB:YJL085W; -.
DR eggNOG; KOG2344; Eukaryota.
DR GeneTree; ENSGT00390000003595; -.
DR HOGENOM; CLU_010236_4_1_1; -.
DR InParanoid; P19658; -.
DR OMA; GPIYGNT; -.
DR BioCyc; YEAST:G3O-31542-MON; -.
DR Reactome; R-SCE-264876; Insulin processing.
DR EvolutionaryTrace; P19658; -.
DR PRO; PR:P19658; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P19658; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA: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:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IDA:SGD.
DR GO; GO:0001927; P:exocyst assembly; IMP:SGD.
DR GO; GO:0051601; P:exocyst localization; IGI:SGD.
DR GO; GO:0006887; P:exocytosis; IMP:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA: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 InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542; PTHR12542; 1.
DR Pfam; PF03081; Exo70; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing; Exocytosis;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..623
FT /note="Exocyst complex component EXO70"
FT /id="PRO_0000118975"
FT CONFLICT 497
FT /note="A -> S (in Ref. 6; AAU09750)"
FT /evidence="ECO:0000305"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:2B1E"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2PFV"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2B7M"
FT HELIX 125..153
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 195..214
FT /evidence="ECO:0007829|PDB:2B1E"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:2PFV"
FT HELIX 239..260
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 268..292
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2PFV"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:2B1E"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 327..358
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:2B1E"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 423..450
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 469..488
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:2B1E"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 499..532
FT /evidence="ECO:0007829|PDB:2B1E"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 542..563
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 571..596
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:2B1E"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:2B1E"
FT HELIX 611..622
FT /evidence="ECO:0007829|PDB:2B1E"
SQ SEQUENCE 623 AA; 71294 MW; 277D89176FC2837D CRC64;
MPAEIDIDEA DVLVLSQELQ KTSKLTFEIN KSLKKIAATS NQSSQLFTPI LARNNVLTTL
QRNIESTLNS VASVKDLANE ASKYEIILQK GINQVGLKQY TQVVHKLDDM LEDIQSGQAN
REENSEFHGI LTHLEQLIKR SEAQLRVYFI SILNSIKPFD PQINITKKMP FPYYEDQQLG
ALSWILDYFH GNSEGSIIQD ILVGERSKLI LKCMAFLEPF AKEISTAKNA PYEKGSSGMN
SYTEALLGFI ANEKSLVDDL YSQYTESKPH VLSQILSPLI SAYAKLFGAN LKIVRSNLEN
FGFFSFELVE SINDVKKSLR GKELQNYNLL QDCTQEVRQV TQSLFRDAID RIIKKANSIS
TIPSNNGVTE ATVDTMSRLR KFSEYKNGCL GAMDNITREN WLPSNYKEKE YTLQNEALNW
EDHNVLLSCF ISDCIDTLAV NLERKAQIAL MPNQEPDVAN PNSSKNKHKQ RIGFFILMNL
TLVEQIVEKS ELNLMLAGEG HSRLERLKKR YISYMVSDWR DLTANLMDSV FIDSSGKKSK
DKEQIKEKFR KFNEGFEDLV SKTKQYKLSD PSLKVTLKSE IISLVMPMYE RFYSRYKDSF
KNPRKHIKYT PDELTTVLNQ LVR
