E70E2_ARATH
ID E70E2_ARATH Reviewed; 639 AA.
AC Q9FNR3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Exocyst complex component EXO70E2 {ECO:0000303|PubMed:16942608};
DE Short=AtExo70e2 {ECO:0000303|PubMed:16942608};
DE AltName: Full=Exocyst subunit Exo70 family protein E2 {ECO:0000303|PubMed:16942608};
GN Name=EXO70E2 {ECO:0000303|PubMed:16942608};
GN OrderedLocusNames=At5g61010 {ECO:0000312|Araport:AT5G61010};
GN ORFNames=MAF19.1 {ECO:0000312|EMBL:BAB10364.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower, and Silique;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16942608; DOI=10.1111/j.1365-313x.2006.02854.x;
RA Synek L., Schlager N., Elias M., Quentin M., Hauser M.-T., Zarsky V.;
RT "AtEXO70A1, a member of a family of putative exocyst subunits specifically
RT expanded in land plants, is important for polar growth and plant
RT development.";
RL Plant J. 48:54-72(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND GENE FAMILY.
RX PubMed=19895414; DOI=10.1111/j.1469-8137.2009.03070.x;
RA Chong Y.T., Gidda S.K., Sanford C., Parkinson J., Mullen R.T., Goring D.R.;
RT "Characterization of the Arabidopsis thaliana exocyst complex gene families
RT by phylogenetic, expression profiling, and subcellular localization
RT studies.";
RL New Phytol. 185:401-419(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21193573; DOI=10.1105/tpc.110.080697;
RA Wang J., Ding Y., Wang J., Hillmer S., Miao Y., Lo S.W., Wang X.,
RA Robinson D.G., Jiang L.;
RT "EXPO, an exocyst-positive organelle distinct from multivesicular endosomes
RT and autophagosomes, mediates cytosol to cell wall exocytosis in Arabidopsis
RT and tobacco cells.";
RL Plant Cell 22:4009-4030(2010).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=20943851; DOI=10.1104/pp.110.164178;
RA Li S., van Os G.M.A., Ren S., Yu D., Ketelaar T., Emons A.M.C., Liu C.-M.;
RT "Expression and functional analyses of EXO70 genes in Arabidopsis implicate
RT their roles in regulating cell type-specific exocytosis.";
RL Plant Physiol. 154:1819-1830(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH SEC6; SEC10A AND SEC10B.
RC STRAIN=cv. Columbia;
RX PubMed=24307681; DOI=10.1091/mbc.e13-10-0586;
RA Ding Y., Wang J., Chun Lai J.H., Ling Chan V.H., Wang X., Cai Y., Tan X.,
RA Bao Y., Xia J., Robinson D.G., Jiang L.;
RT "Exo70E2 is essential for exocyst subunit recruitment and EXPO formation in
RT both plants and animals.";
RL Mol. Biol. Cell 25:412-426(2014).
CC -!- FUNCTION: Influences the subcellular localization patterns of other
CC exocyst complex proteins (e.g. SEC5A, SEC15A, SEC15B and EXO84B)
CC leading to their recruitment to exocyst, well-defined large punctate
CC structures throughout the cytosol (PubMed:19895414, PubMed:24307681).
CC Essential component for the formation and the recruitment of exocyst
CC subunits to the exocyst-positive organelle (EXPO), a secreted double
CC membrane structure also called extracellular exosome, that acts as a
CC sequester for cytosolic proteins to release them into the apoplast
CC (PubMed:21193573, PubMed:24307681). {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:21193573, ECO:0000269|PubMed:24307681}.
CC -!- SUBUNIT: Component of the exocyst complex and of the exocyst-positive
CC organelle (EXPO). Interacts with SEC6, SEC10A and SEC10B.
CC {ECO:0000269|PubMed:24307681}.
CC -!- INTERACTION:
CC Q9FNR3; Q93WJ9: KAN1; NbExp=2; IntAct=EBI-4429105, EBI-4426504;
CC Q9FNR3; O23160: MYB73; NbExp=3; IntAct=EBI-4429105, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular exosome
CC {ECO:0000269|PubMed:21193573}. Secreted {ECO:0000269|PubMed:21193573}.
CC Cell membrane {ECO:0000269|PubMed:21193573}. Cytoplasm
CC {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21193573}.
CC Endomembrane system {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:21193573}. Note=Localized to well-defined large
CC punctate structures throughout the cytosol (PubMed:19895414). Component
CC of the secreted double membrane structure exocyst-positive organelle
CC (EXPO). Locates to the plasma membrane as discrete punctae and secreted
CC outside of the cells (PubMed:21193573). {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:21193573}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, in the root-hair zone, both in
CC root hair and nonhair cells. {ECO:0000269|PubMed:20943851}.
CC -!- DISRUPTION PHENOTYPE: Unability to recruit a number of exocyst subunits
CC to the exocyst-positive organelle (EXPO).
CC {ECO:0000269|PubMed:24307681}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
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DR EMBL; AB006696; BAB10364.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97410.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97411.1; -; Genomic_DNA.
DR EMBL; AY050411; AAK91427.1; -; mRNA.
DR EMBL; AY059656; AAL31149.1; -; mRNA.
DR EMBL; AK317325; BAH19999.1; -; mRNA.
DR RefSeq; NP_001032116.1; NM_001037039.2.
DR RefSeq; NP_200909.1; NM_125494.3.
DR AlphaFoldDB; Q9FNR3; -.
DR SMR; Q9FNR3; -.
DR IntAct; Q9FNR3; 53.
DR STRING; 3702.AT5G61010.1; -.
DR PaxDb; Q9FNR3; -.
DR PRIDE; Q9FNR3; -.
DR EnsemblPlants; AT5G61010.1; AT5G61010.1; AT5G61010.
DR EnsemblPlants; AT5G61010.2; AT5G61010.2; AT5G61010.
DR GeneID; 836222; -.
DR Gramene; AT5G61010.1; AT5G61010.1; AT5G61010.
DR Gramene; AT5G61010.2; AT5G61010.2; AT5G61010.
DR KEGG; ath:AT5G61010; -.
DR Araport; AT5G61010; -.
DR TAIR; locus:2159386; AT5G61010.
DR eggNOG; KOG2344; Eukaryota.
DR HOGENOM; CLU_010236_2_2_1; -.
DR InParanoid; Q9FNR3; -.
DR OMA; KFQQHAT; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; Q9FNR3; -.
DR PRO; PR:Q9FNR3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNR3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0052542; P:defense response by callose deposition; IMP:TAIR.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IMP:TAIR.
DR GO; GO:1903553; P:positive regulation of extracellular exosome assembly; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903533; P:regulation of protein targeting; IDA:UniProtKB.
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 Cell membrane; Cytoplasm; Exocytosis; Membrane; Protein transport;
KW Reference proteome; Secreted; Transport.
FT CHAIN 1..639
FT /note="Exocyst complex component EXO70E2"
FT /id="PRO_0000440983"
SQ SEQUENCE 639 AA; 73486 MW; BEE68751AC479B4F CRC64;
MAEFDSKVPV SGMNNHVFEA CHHVVKALRA SDNNLDANLR KLLSDLEMHL STFGIADTKV
EDAGFSEIKK RFKEAVKRIR SWETNQSTMF EAGLSEADQF FQALYDVQTV LVGFKALPMK
TNQMEKDVYN QATVALDIAM LRLEKELCDV LHQHKRHVQP DYLAVSSRRK DIVYDESFVS
LDDEVIVEAS SHEDDEQISD FYNSDLVDPI VLPHIKAIAN AMFACEYDQP FCEAFIGVQR
EALEEYMVTL EMERFSCVDV LRMDWEDLNG AMRKWTKVVK IITQVYLASE KQLCDQILGD
FESISTACFI EISKDAILSL LNFGEAVVLR SCKPEMLERF LSMYEVSAEI LVDVDNLFPD
ETGSSLRIAF HNLSKKLADH TTTTFLKFKD AIASDESTRP FHGGGIHHLT RYVMNYLKLL
PEYTDSLNSL LQNIHVDDSI PEKTGEDVLP STFSPMARHL RSIVTTLESS LERKAQLYAD
EALKSIFLMN NFRYMVQKVK GSELRRLFGD EWIRKHIASY QCNVTNYERS TWSSILALLR
DNNDSVRTLR ERCRLFSLAF DDVYKNQTRW SVPDSELRDD LHISTSVKVV QSYRGFLGRN
AVRIGEKHIR YTCEDIENML LDLFECLPSP RSLRSSRKR
