EX84B_ARATH
ID EX84B_ARATH Reviewed; 752 AA.
AC Q9LTB0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Exocyst complex component EXO84B {ECO:0000303|PubMed:19895414};
DE Short=AtExo80b {ECO:0000303|PubMed:19895414};
GN Name=EXO84B {ECO:0000303|PubMed:19895414};
GN OrderedLocusNames=At5g49830 {ECO:0000312|Araport:AT5G49830};
GN ORFNames=K21G20.4 {ECO:0000312|EMBL:BAA98150.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
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 [5]
RP FUNCTION, COMPONENT OF THE EXOCYST COMPLEX, INTERACTION WITH SEC6; SEC10;
RP SEC15B AND EXO70A1, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20870962; DOI=10.1105/tpc.110.074351;
RA Fendrych M., Synek L., Pecenkova T., Toupalova H., Cole R., Drdova E.,
RA Nebesarova J., Sedinova M., Hala M., Fowler J.E., Zarsky V.;
RT "The Arabidopsis exocyst complex is involved in cytokinesis and cell plate
RT maturation.";
RL Plant Cell 22:3053-3065(2010).
RN [6]
RP FUNCTION, AND INTERACTION WITH EXO70B1.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27803190; DOI=10.1104/pp.16.01252;
RA Mao H., Nakamura M., Viotti C., Grebe M.;
RT "A framework for lateral membrane trafficking and polar tethering of the
RT PEN3 ATP-binding cassette transporter.";
RL Plant Physiol. 172:2245-2260(2016).
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. Involved in polarized cell growth and
CC organ morphogenesis. During cytokinesis, involved in cell plate
CC initiation, cell plate maturation and formation of new primary cell
CC wall. Probable component of an exocyst subcomplex specifically involved
CC in autophagy-related, Golgi-independent membrane traffic to the
CC vacuole. Regulates autophagosome formation and autophagy-related Golgi-
CC independent import into the vacuole. Mediates ABCG36/PEN3 outer-
CC membrane polarity at the periphery of lateral root cap and root
CC epidermal cells (PubMed:27803190). {ECO:0000269|PubMed:20870962,
CC ECO:0000269|PubMed:23944713, ECO:0000269|PubMed:27803190}.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, EXO70A1 and EXO84B. Interacts with SEC6, SEC10, SEC15B and
CC EXO70A1. Interacts with EXO70B1. {ECO:0000269|PubMed:20870962,
CC ECO:0000269|PubMed:23944713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:19895414}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:20870962}. Secreted,
CC cell wall {ECO:0000269|PubMed:20870962}. Cell membrane
CC {ECO:0000269|PubMed:27803190}. Note=Localized to globular structures in
CC the perinuclear region (PubMed:19895414). During cytokinesis, localizes
CC to the nascent cell plate and later to the cell plate insertion site
CC and along the post-cytokinetic wall (PubMed:20870962). Polarized
CC localization at the outermost side of root epidermal and cap cells, in
CC the outer lateral membrane domain facing the environment
CC (PubMed:27803190). {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:20870962, ECO:0000269|PubMed:27803190}.
CC -!- DISRUPTION PHENOTYPE: Sterile plants with extreme dwarf phenotype and
CC cytokinetic defects, and accumulation of vesicles in leaf epidermal
CC cells (PubMed:20870962). Impaired trafficking and endocytic recycling
CC of ABCG36/PEN3 between the trans-Golgi network and the plasma membrane
CC in root epidermal and cap cells leading to a strong intracellular
CC accumulation of ABCG36/PEN3 and lost ABCG36/PEN3 outer lateral plasma
CC membrane polarity (PubMed:27803190). {ECO:0000269|PubMed:20870962,
CC ECO:0000269|PubMed:27803190}.
CC -!- SIMILARITY: Belongs to the EXO84 family. {ECO:0000305}.
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DR EMBL; AB025612; BAA98150.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95860.1; -; Genomic_DNA.
DR EMBL; AY075643; AAL77652.1; -; mRNA.
DR EMBL; AY093996; AAM16257.1; -; mRNA.
DR RefSeq; NP_199794.1; NM_124361.5.
DR AlphaFoldDB; Q9LTB0; -.
DR SMR; Q9LTB0; -.
DR BioGRID; 20292; 4.
DR STRING; 3702.AT5G49830.2; -.
DR iPTMnet; Q9LTB0; -.
DR PaxDb; Q9LTB0; -.
DR PRIDE; Q9LTB0; -.
DR ProMEX; Q9LTB0; -.
DR ProteomicsDB; 221812; -.
DR EnsemblPlants; AT5G49830.1; AT5G49830.1; AT5G49830.
DR GeneID; 835046; -.
DR Gramene; AT5G49830.1; AT5G49830.1; AT5G49830.
DR KEGG; ath:AT5G49830; -.
DR Araport; AT5G49830; -.
DR eggNOG; KOG2215; Eukaryota.
DR HOGENOM; CLU_015217_2_0_1; -.
DR OMA; TMDDITK; -.
DR PhylomeDB; Q9LTB0; -.
DR PRO; PR:Q9LTB0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LTB0; baseline and differential.
DR Genevisible; Q9LTB0; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1210; -; 1.
DR Gene3D; 1.20.58.1220; -; 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 PANTHER; PTHR21426; PTHR21426; 1.
DR Pfam; PF16528; Exo84_C; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cytoplasm; Cytoskeleton; Exocytosis; Membrane;
KW Protein transport; Reference proteome; Secreted; Transport.
FT CHAIN 1..752
FT /note="Exocyst complex component EXO84B"
FT /id="PRO_0000424568"
FT REGION 511..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 82748 MW; E6F164E6BF082932 CRC64;
MAAKTARSKA TPTKENGVRV EEGLSLFKSD KFDADAYVQS KCSINEKDIK QLCSYLLDLK
RASAEEMRRS VYANYPAFIR TSKEISDLEG ELSSIRNLLS TQATLIHGLA DGVNIDDDKV
SDESLANGLL NFEDNGLSDL EKWATEFPDH LDALLAERRV DEALAAFDEG EILVSQANEK
HTLSSSVLSS LQFAIAERKQ KLADQLAKAA CQPSTRGGEL RSAIAALKRL GDGPRAHTVL
LDAHFQRYQY NMQSLRPSST SYGGAYTAAL SQLVFSAISQ ASSDSLGIFG KEPAYSSELV
TWATKQTEAF SLLVKRHALA SSAAAGGLRA AAECAQIALG HCSLLEARGL SLCPVLLKHF
KPIVEQALEA NLKRIEENTA AMAAADDWVL TSPPAGSRHA STAFQNKLTS SAHRFNLMVQ
DFFEDVGPLL SMQLGSKALE GLFRVFNSYV DVLVRALPGS IEEEDPNFES SCNKIVQMAE
TEANQLALLA NASLLADELL PRAAMKLSLD QTGQRTDDLR RPLDRQNRNP EQREWKRRLL
STVDKLKDAF CRQHALDLIF TEEGDSHLSA DMYVNIDENG EDVDFFPSLI FQELFAKLNR
MASLAADMFV GRERFAISLL MRLTETVILW LSGDQSFWDD IEEGPRPLGP LGLRQLYLDM
KFVICFASQG RYLSRNLHRG TNEIISKALA AFTATGIDPY SELPEDDWFN DICVDAMERL
SGKTKGNNGD VHSPTASVSA QSVSSARSHG SY
