E70A3_ARATH
ID E70A3_ARATH Reviewed; 586 AA.
AC F4KG58; Q9FHC5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Exocyst complex component EXO70A3 {ECO:0000303|PubMed:16942608, ECO:0000303|PubMed:31299202};
DE Short=AtExo70a3 {ECO:0000303|PubMed:16942608, ECO:0000303|PubMed:31299202};
DE AltName: Full=Exocyst subunit Exo70 family protein A3 {ECO:0000303|PubMed:16942608};
GN Name=EXO70A3 {ECO:0000303|PubMed:16942608, ECO:0000303|PubMed:31299202};
GN OrderedLocusNames=At5g52350 {ECO:0000312|Araport:AT5G52350};
GN ORFNames=K24M7.8 {ECO:0000312|EMBL:BAB10532.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 [4]
RP TISSUE SPECIFICITY, AND GENE FAMILY.
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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBUNIT.
RC STRAIN=cv. C24, cv. Columbia, cv. Cvi-0, cv. Lac-5, cv. Ler-1, cv. Mib-60,
RC cv. Sha, cv. Ty-0, and cv. Wassilewskija-2;
RX PubMed=31299202; DOI=10.1016/j.cell.2019.06.021;
RA Ogura T., Goeschl C., Filiault D., Wolhrab B., Satbhai S.B., Busch W.;
RT "Root system depth in Arabidopsis is shaped by EXOCYST70A3 via the dynamic
RT modulation of auxin transport.";
RL Cell 178:P400.E16-P412.E16(2019).
CC -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC exocytic vesicles with fusion sites on the plasma membrane during
CC regulated or polarized secretion (PubMed:31299202). Involved in PIN4
CC exocytosis and gravitropic responses in columella cells
CC (PubMed:31299202). By monitoring PIN4 distribution in columella cells,
CC modulates auxin repartition and subsequently regulates the root system
CC architecture (RSA), thus being a component of the auxin-dependent root
CC directional growth (ARD) (PubMed:31299202).
CC {ECO:0000269|PubMed:31299202}.
CC -!- SUBUNIT: Subunit of the exocyst complex. {ECO:0000305|PubMed:31299202}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to the outer layer of the columella cells
CC in the root tips of young seedlings. {ECO:0000269|PubMed:20943851,
CC ECO:0000269|PubMed:31299202}.
CC -!- DISRUPTION PHENOTYPE: Alteration of root gravitropic responses (e.g.
CC delay, auxin-dependent root directional growth and larger variation of
CC root tip angles) resulting in deeper root system architecture (RSA) and
CC enhanced drought resistance (PubMed:31299202). Disturbed PIN4
CC distribution in columella cells associated with a perturbation of the
CC auxin distribution pattern and an asymmetric accumulation of DR5 in the
CC downward peripheral layer under gravistimulus (PubMed:31299202).
CC {ECO:0000269|PubMed:31299202}.
CC -!- MISCELLANEOUS: Associated with natural variation of agravitropic root
CC growth upon auxin transport perturbation with N-1-naphtylphthalamic
CC acid (NPA). {ECO:0000269|PubMed:31299202}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10532.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019226; BAB10532.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96204.1; -; Genomic_DNA.
DR RefSeq; NP_200048.2; NM_124614.2.
DR AlphaFoldDB; F4KG58; -.
DR SMR; F4KG58; -.
DR STRING; 3702.AT5G52350.1; -.
DR PaxDb; F4KG58; -.
DR PRIDE; F4KG58; -.
DR ProteomicsDB; 218279; -.
DR EnsemblPlants; AT5G52350.1; AT5G52350.1; AT5G52350.
DR GeneID; 835311; -.
DR Gramene; AT5G52350.1; AT5G52350.1; AT5G52350.
DR KEGG; ath:AT5G52350; -.
DR Araport; AT5G52350; -.
DR TAIR; locus:2156717; AT5G52350.
DR eggNOG; KOG2344; Eukaryota.
DR HOGENOM; CLU_010236_5_1_1; -.
DR InParanoid; F4KG58; -.
DR OMA; ILQCITV; -.
DR OrthoDB; 410847at2759; -.
DR PRO; PR:F4KG58; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KG58; differential.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0010252; P:auxin homeostasis; IDA:UniProtKB.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0009630; P:gravitropism; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010015; P:root morphogenesis; 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 Auxin signaling pathway; Developmental protein; Exocytosis; Glycoprotein;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..586
FT /note="Exocyst complex component EXO70A3"
FT /id="PRO_0000448067"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 119..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 487
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 586 AA; 67572 MW; A8F371E5194274A8 CRC64;
MSNVLDKTNL HELSIAPKIS THDEKLYECT KCGIFFHRDS VESATEINPH ENLGEVRAVE
DKPNNESIKV DERGTCNFHF IDEHHGKVDG INTEYDASKF KQILENYSKL TEPNQLFECL
PSNLRPPSDD EGSDGKSHDP QSNGLGKTDY TVPTIIPPTV LPVLHDLAQQ MVKAGHQQEL
FKTYRDIRRA VLAQSLEKLG VERHSKYDVE RMNQDVFEAK IMNWIHYIRI SVKLLFAAEK
EICHQILDGV EPFRDQSFAE ITTISFGMLL SFGYAIAISR RSPEKVFVIL DMYEIMIELQ
PEFELIFGSK PCTEMKEDAL NLTKLLAQTV KETIADFEVA IEMDATETVV MDGSVHALTS
YVARYVKFLF DYEPTLRQLF QEFNSNDPDT KLKSVMTGIM RALRNNLDGK SRQFEDAALT
QLFLMNNVYY IVRNFRREEA KNFLGDDLVQ THRRIVQQHA KQYQTISWNK ILQCITVQSS
KSGLIKNESI KKTLVKEKFK TFNSQFEELH QRQCQWSVSD VELRESLRLA IAEVLLPAYG
SFLKRFGPMI ESGKNSQKYI RFTPEDLERM LNDFFQGKNL DVSPKR
