E70H1_ARATH
ID E70H1_ARATH Reviewed; 636 AA.
AC Q8VY27; Q9M3D4;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Exocyst complex component EXO70H1 {ECO:0000303|PubMed:16942608};
DE Short=AtExo70h1 {ECO:0000303|PubMed:16942608};
DE AltName: Full=Exocyst subunit Exo70 family protein H1 {ECO:0000303|PubMed:16942608};
GN Name=EXO70H1 {ECO:0000303|PubMed:16942608};
GN OrderedLocusNames=At3g55150 {ECO:0000312|Araport:AT3G55150};
GN ORFNames=T26I12.30 {ECO:0000312|EMBL:CAB75749.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 DISRUPTION PHENOTYPE, 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 [5]
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 [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY B.GRAMINIS AND P.SYRINGAE,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SEC3A; SEC5A; SEC15B AND
RP EXO70B2.
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).
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). Involved in
CC defense responses to pathogenic bacteria (e.g. P.syringae pv.
CC maculicola) (PubMed:21199889). {ECO:0000250|UniProtKB:Q9FGH9,
CC ECO:0000269|PubMed:21199889}.
CC -!- SUBUNIT: Interacts with the exocyst subunits EXO70B2, SEC3A, SEC5A and
CC SEC15B (PubMed:21199889). Subunit of the exocyst complex that mediates
CC vesicle tethering during exocytosis (Probable).
CC {ECO:0000269|PubMed:21199889, ECO:0000305}.
CC -!- INTERACTION:
CC Q8VY27; O23160: MYB73; NbExp=3; IntAct=EBI-4470389, EBI-25506855;
CC Q8VY27; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-4470389, EBI-4426557;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome
CC {ECO:0000250|UniProtKB:Q9FGH9}. Cytoplasm
CC {ECO:0000269|PubMed:19895414}. Nucleus {ECO:0000269|PubMed:19895414}.
CC Endomembrane system {ECO:0000269|PubMed:21199889}. Note=Localized in
CC the vesicle-like structures in a peri-nuclear and nuclear pattern.
CC {ECO:0000269|PubMed:21199889}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and, to a lower extent,
CC in leaves, flower buds and siliques. {ECO:0000269|PubMed:20943851}.
CC -!- DEVELOPMENTAL STAGE: In roots, localized in elongation and root hair
CC zones. In flowers, observed in carpels. {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 -!- DISRUPTION PHENOTYPE: No discernible phenotype in normal conditions
CC (PubMed:21199889). Enhanced susceptibility to the bacterial pathogen
CC P.syringae pv. maculicola (PubMed:21199889).
CC {ECO:0000269|PubMed:21199889}.
CC -!- SIMILARITY: Belongs to the EXO70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB75749.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL132954; CAB75749.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79346.1; -; Genomic_DNA.
DR EMBL; AY074262; AAL66959.1; -; mRNA.
DR EMBL; AY096453; AAM20093.1; -; mRNA.
DR PIR; T47654; T47654.
DR RefSeq; NP_191075.2; NM_115373.4.
DR AlphaFoldDB; Q8VY27; -.
DR SMR; Q8VY27; -.
DR IntAct; Q8VY27; 14.
DR STRING; 3702.AT3G55150.1; -.
DR PaxDb; Q8VY27; -.
DR PRIDE; Q8VY27; -.
DR EnsemblPlants; AT3G55150.1; AT3G55150.1; AT3G55150.
DR GeneID; 824681; -.
DR Gramene; AT3G55150.1; AT3G55150.1; AT3G55150.
DR KEGG; ath:AT3G55150; -.
DR Araport; AT3G55150; -.
DR TAIR; locus:2100656; AT3G55150.
DR eggNOG; KOG2344; Eukaryota.
DR HOGENOM; CLU_010236_2_2_1; -.
DR InParanoid; Q8VY27; -.
DR OMA; SVIRKWD; -.
DR OrthoDB; 410847at2759; -.
DR PhylomeDB; Q8VY27; -.
DR PRO; PR:Q8VY27; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VY27; 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; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
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: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; IEP: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; Membrane; Nucleus; Plant defense;
KW Reference proteome; Transport.
FT CHAIN 1..636
FT /note="Exocyst complex component EXO70H1"
FT /id="PRO_0000440704"
FT REGION 132..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 71962 MW; B39BC1DF92961A8A CRC64;
MAKMAKFSFF SSSSPKYHPS SPSSFTSFPA SPLNQNFTQA MMEETVETAD SVIRKWDPNT
PSFTKIVSLF NHSRKEAKEF IRCVRDLRRA MHFLVSQDSQ SPKLALAQTL MQIAMARLEK
EFFQILSSNR DKLDPESVSG QSSISSNSEF EDVMGSDDDD ESDNEMRKAG ESITQVEKAS
AMVMSDLKAI AESMISCGYG KECVKIYKRV RKSIVDEGLS LLGIEIYKGS RFHRTDWVTL
EHMIKNWIKA AKIGIATLFR GEKLLCDHVF SASNSTRESC FYEIANEAAT NLFKFPEFVA
KEKKSHERIF PLMDLQAAIS DLWQDIEMIF HFDAVAGVKS QALTSLQKLK VSIHSALTDF
ESIIQKDTTK ALTPGGGIHK LTRSTMNFIS SLSKYSGVLS EILADHPLPR NTRLLESYVR
APISEDEQHN HALSVHFAWL ILVLLCKLDT KAEHYKDVSL SYLFLANNLQ IIIETVGSTP
LRNLLGDDWL NKHEDKLCAY AGNYEIAAWS NVFMSLPEEP TDLSPEEAKI YFRRFHTAFE
EAYMKQSSRV VPNAKLRDEL KVSIAKKLVP EYREFYRKYL PMLGQERNIE ILVRFKPDNL
ENYISDLFHG TPIHASSSFS SSSSSSSWKS LGCVSG
