E70B2_ARATH
ID E70B2_ARATH Reviewed; 599 AA.
AC Q9LMJ4; Q56YJ9;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Exocyst complex component EXO70B2 {ECO:0000303|PubMed:16942608};
DE Short=AtExo70b2 {ECO:0000303|PubMed:16942608};
DE AltName: Full=Exocyst subunit Exo70 family protein B2 {ECO:0000303|PubMed:16942608};
GN Name=EXO70B2 {ECO:0000303|PubMed:16942608};
GN OrderedLocusNames=At1g07000 {ECO:0000312|Araport:AT1G07000};
GN ORFNames=F10K1.28 {ECO:0000312|EMBL:AAF82219.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 403-599.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
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 SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
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 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.
RC STRAIN=cv. Columbia;
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, INDUCTION BY B.GRAMINIS AND P.SYRINGAE,
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH SEC5A; SEC15B; EXO70H1
RP AND SNAP33.
RC STRAIN=cv. Columbia;
RX PubMed=21199889; DOI=10.1093/jxb/erq402;
RA Pecenkova T., Hala M., Kulich I., Kocourkova D., Drdova E., Fendrych M.,
RA Toupalova H., Zarsky V.;
RT "The role for the exocyst complex subunits Exo70B2 and Exo70H1 in the
RT plant-pathogen interaction.";
RL J. Exp. Bot. 62:2107-2116(2011).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, REGULATION BY PUB22, AND INTERACTION WITH
RP PUB22.
RC STRAIN=cv. Columbia;
RX PubMed=23170036; DOI=10.1105/tpc.112.104463;
RA Stegmann M., Anderson R.G., Ichimura K., Pecenkova T., Reuter P.,
RA Zarsky V., McDowell J.M., Shirasu K., Trujillo M.;
RT "The ubiquitin ligase PUB22 targets a subunit of the exocyst complex
RT required for PAMP-triggered responses in Arabidopsis.";
RL Plant Cell 24:4703-4716(2012).
RN [11]
RP INTERACTION WITH EXO70B1.
RC STRAIN=cv. Columbia;
RX PubMed=23944713; DOI=10.1111/tra.12101;
RA Kulich I., Pecenkova T., Sekeres J., Smetana O., Fendrych M., Foissner I.,
RA Hoeftberger M., Zarsky V.;
RT "Arabidopsis exocyst subcomplex containing subunit EXO70B1 is involved in
RT the autophagy-related transport to the vacuole.";
RL Traffic 14:1155-1165(2013).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=27956469; DOI=10.1105/tpc.16.00347;
RA Seo D.H., Ahn M.Y., Park K.Y., Kim E.Y., Kim W.T.;
RT "The N-terminal UND motif of the Arabidopsis U-box E3 ligase PUB18 is
RT critical for the negative regulation of ABA-mediated stomatal movement and
RT determines its ubiquitination specificity for exocyst subunit Exo70B1.";
RL Plant Cell 28:2952-2973(2016).
CC -!- FUNCTION: Component of an exocyst subcomplex specifically involved in
CC autophagy-related, Golgi-independent membrane traffic to the vacuole.
CC Regulates autophagosome formation and autophagy-related Golgi-
CC independent import into the vacuole (By similarity). Positive regulator
CC of defense responses to pathogenic bacteria (e.g. P.syringae pv.
CC maculicola), to the biotrophic oomycete H.arabidopsidis and to fungi
CC (e.g. B.graminis hordei), especially in cell wall apposition formation
CC related to plant defense (PubMed:21199889, PubMed:23170036). Required
CC for both immediate and later responses triggered by pathogen-associated
CC molecular patterns (PAMPs) (PubMed:23170036). Positive regulator of
CC abscisic acid (ABA)-independent mannitol (drought)-promoted stomatal
CC closure (PubMed:27956469). {ECO:0000250|UniProtKB:Q9FGH9,
CC ECO:0000269|PubMed:21199889, ECO:0000269|PubMed:23170036,
CC ECO:0000269|PubMed:27956469}.
CC -!- SUBUNIT: Self interacts (PubMed:21199889). Interacts with EXO70B1
CC (PubMed:23944713). Interacts with the exocyst subunits EXO70H1, SEC5A
CC and SEC15B. Binds to SNAP33 (PubMed:21199889). Subunit of the exocyst
CC complex that mediates vesicle tethering during exocytosis (Probable).
CC Binds to PUB22 (PubMed:23170036). {ECO:0000269|PubMed:21199889,
CC ECO:0000269|PubMed:23170036, ECO:0000269|PubMed:23944713, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9FGH9}. Cytoplasm {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:21193573, ECO:0000269|PubMed:21199889}. Nucleus
CC {ECO:0000269|PubMed:19895414, ECO:0000269|PubMed:21199889}. Note=In the
CC cytoplasm, localized in a peri-nuclear pattern.
CC {ECO:0000269|PubMed:21199889}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and, to a lower extent,
CC in roots, cotyledons, internodes, flower buds, siliques and anthers.
CC {ECO:0000269|PubMed:20943851}.
CC -!- INDUCTION: Induced by elicitor peptides elf18 and flg22, by the fungus
CC B.graminis hordei and by the bacterium P.syringae.
CC {ECO:0000269|PubMed:21199889}.
CC -!- PTM: Target of the E3 ubiquitin-protein ligase PUB22 that mediates its
CC ubiquitination and degradation via the 26S proteasome to attenuate
CC pathogen-associated molecular patterns (PAMP)-induced signaling,
CC especially is response to the bacterial elicitor flg22.
CC {ECO:0000269|PubMed:23170036}.
CC -!- DISRUPTION PHENOTYPE: No discernible phenotype in normal conditions
CC (PubMed:16942608, PubMed:21199889, PubMed:27956469). Altered mannitol
CC (drought)-promoted stomatal closure (PubMed:27956469). Enhanced
CC susceptibility to the bacterial pathogen P.syringae pv. maculicola and
CC abnormal papilla formation, with an unusual wide halo made of vesicle-
CC like structures upon inoculation by the fungal pathogen B.graminis
CC hordei (PubMed:21199889). Reduced sensitivity to pathogen-associated
CC molecular patterns (PAMPs) (e.g. bacterial elicitor flg22, bacterial
CC transcription factor elf18, Pep1 and fungal chitin) leading to a
CC reduced production of reactive oxygen species (ROS) and impaired
CC induction of several plant defense genes. Increased disease
CC susceptibility to the biotrophic oomycete H.arabidopsidis
CC (PubMed:23170036). {ECO:0000269|PubMed:16942608,
CC ECO:0000269|PubMed:21199889, ECO:0000269|PubMed:23170036,
CC ECO:0000269|PubMed:27956469}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
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DR EMBL; AC067971; AAF82219.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28064.1; -; Genomic_DNA.
DR EMBL; AY075660; AAL77667.1; -; mRNA.
DR EMBL; AY101526; AAM26647.1; -; mRNA.
DR EMBL; AK221323; BAD94116.1; -; mRNA.
DR PIR; G86204; G86204.
DR RefSeq; NP_172181.1; NM_100573.4.
DR AlphaFoldDB; Q9LMJ4; -.
DR SMR; Q9LMJ4; -.
DR IntAct; Q9LMJ4; 5.
DR STRING; 3702.AT1G07000.1; -.
DR iPTMnet; Q9LMJ4; -.
DR PaxDb; Q9LMJ4; -.
DR PRIDE; Q9LMJ4; -.
DR ProteomicsDB; 222037; -.
DR EnsemblPlants; AT1G07000.1; AT1G07000.1; AT1G07000.
DR GeneID; 837210; -.
DR Gramene; AT1G07000.1; AT1G07000.1; AT1G07000.
DR KEGG; ath:AT1G07000; -.
DR Araport; AT1G07000; -.
DR TAIR; locus:2007347; AT1G07000.
DR eggNOG; KOG2344; Eukaryota.
DR HOGENOM; CLU_010236_2_1_1; -.
DR InParanoid; Q9LMJ4; -.
DR OMA; SWNQVVG; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; Q9LMJ4; -.
DR PRO; PR:Q9LMJ4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMJ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0042545; P:cell wall modification; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; TAS:UniProtKB.
DR GO; GO:0009620; P:response to fungus; TAS:UniProtKB.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IMP:UniProtKB.
DR GO; GO:0002238; P:response to molecule of fungal origin; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP: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 Cytoplasm; Cytoplasmic vesicle; Nucleus; Plant defense; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..599
FT /note="Exocyst complex component EXO70B2"
FT /id="PRO_0000440703"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 417
FT /note="D -> G (in Ref. 4; BAD94116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 67715 MW; D0D32919FFA702BE CRC64;
MAEAGDENLY AAARDIARAL GKDPSAAGDI LQILSGYGAS GNRGGDPRPT PSRGGSNVNF
DRALTSLERQ ISSYIVEDRP IWSDPVDSRT FLDSVDELLA IAGDLRSMAG DKSVAVCQSR
ADELIQQVMF RLQEEFGFVM DRAPDSFDSD DEFPGEEDND TSDGVIVARP ITDYKIVIEA
LQSSVIGDLN AIAVRMVAGG FAKECSRVYS SRRREFLEES LSRLHLRGLS MEEVQESPWQ
DLEDEIDRWI KAVTLIFHVF FPSERLLCDR VFSDLPVSSV TDLSFMEVCR GTTTQLLNFA
DAIALGSRLP ERLFKVVDLY EAMQDLIPKM ETLFSDRYCS PLRHEALAIH KRLGEAIRGI
FMELENLIRR DPPKTAFPGG GIHPITRYVM NYLRAACKSR QSLEQILDQT GNETGSDTRP
LSVQIIWVLE LLESNLEGKK RTYRDPSLCF LFMMNNDKYI LDKAKDNELG LVLGEDWIVK
HAAKLRQYHS NYRRSSWNQV VGLLRTDGPY PKLVENLRLF KSQFDEVCKV QSQWVVSDGQ
LREELRSSVA GIVSPAYSNF IRRLKESPEI NGRRGEPFIP YTVEDVEFII KRLFKESSS
