SEC3A_ARATH
ID SEC3A_ARATH Reviewed; 887 AA.
AC Q9SX85;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Exocyst complex component SEC3A {ECO:0000303|PubMed:19895414};
DE Short=AtSec3a {ECO:0000303|PubMed:19895414};
GN Name=SEC3A {ECO:0000303|PubMed:19895414};
GN OrderedLocusNames=At1g47550 {ECO:0000312|Araport:AT1G47550};
GN ORFNames=F16N3.18 {ECO:0000312|EMBL:AAD46032.1};
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 INTERACTION WITH ICR1 AND ICR2.
RX PubMed=17493810; DOI=10.1016/j.cub.2007.04.038;
RA Lavy M., Bloch D., Hazak O., Gutman I., Poraty L., Sorek N., Sternberg H.,
RA Yalovsky S.;
RT "A Novel ROP/RAC effector links cell polarity, root-meristem maintenance,
RT and vesicle trafficking.";
RL Curr. Biol. 17:947-952(2007).
RN [4]
RP COMPONENT OF THE EXOCYST COMPLEX, AND INTERACTION WITH EXO70A1.
RX PubMed=18492870; DOI=10.1105/tpc.108.059105;
RA Hala M., Cole R., Synek L., Drdova E., Pecenkova T., Nordheim A.,
RA Lamkemeyer T., Madlung J., Hochholdinger F., Fowler J.E., Zarsky V.;
RT "An exocyst complex functions in plant cell growth in Arabidopsis and
RT tobacco.";
RL Plant Cell 20:1330-1345(2008).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
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 INTERACTION WITH EXO70H1.
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 [7]
RP FUNCTION, INTERACTION WITH EXO70A1 AND SEC5A, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23495664; DOI=10.1111/nph.12236;
RA Zhang Y., Immink R., Liu C.M., Emons A.M., Ketelaar T.;
RT "The Arabidopsis exocyst subunit SEC3A is essential for embryo development
RT and accumulates in transient puncta at the plasma membrane.";
RL New Phytol. 199:74-88(2013).
RN [8]
RP SUBCELLULAR LOCATION.
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: 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. During cytokinesis, involved in cell plate initiation, cell plate
CC maturation and formation of new primary cell wall.
CC {ECO:0000269|PubMed:23495664}.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, EXO70A1 and EXO84B. Interacts with EXO70A1, SEC5A and ICR1, but
CC not with ICR2. Binds to EXO70H1 (PubMed:21199889).
CC {ECO:0000269|PubMed:17493810, ECO:0000269|PubMed:18492870,
CC ECO:0000269|PubMed:21199889, ECO:0000269|PubMed:23495664}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23495664,
CC ECO:0000269|PubMed:24307681}. Cell membrane
CC {ECO:0000305|PubMed:23495664}; Peripheral membrane protein
CC {ECO:0000305|PubMed:23495664}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:23495664}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:24307681}. Note=In interphase, SEC3A localizes to
CC the cytoplasm and plasma membrane, where it forms immobile, punctate
CC structures. Localizes to the early cell plate and completed division
CC wall during cytokinesis (PubMed:23495664). Shuttles from the cytoplasm
CC to the exocyst-positive organelle (EXPO) in the presence of EXO70E2
CC (PubMed:24307681). {ECO:0000269|PubMed:23495664,
CC ECO:0000269|PubMed:24307681}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SX85-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. Preferentially expressed in
CC tissues containing dividing and expanding cells, such as the shoot
CC apical meristem, root tip, lateral root primordia and developing
CC embryos. {ECO:0000269|PubMed:23495664}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:23495664}.
CC -!- SIMILARITY: Belongs to the SEC3 family. {ECO:0000305}.
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DR EMBL; AC007519; AAD46032.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32184.1; -; Genomic_DNA.
DR PIR; H96515; H96515.
DR RefSeq; NP_175186.2; NM_103648.3. [Q9SX85-1]
DR AlphaFoldDB; Q9SX85; -.
DR SMR; Q9SX85; -.
DR BioGRID; 26389; 4.
DR IntAct; Q9SX85; 1.
DR STRING; 3702.AT1G47550.2; -.
DR TCDB; 1.F.2.1.3; the octameric exocyst (exocyst) family.
DR iPTMnet; Q9SX85; -.
DR MetOSite; Q9SX85; -.
DR PaxDb; Q9SX85; -.
DR PRIDE; Q9SX85; -.
DR ProteomicsDB; 232874; -. [Q9SX85-1]
DR EnsemblPlants; AT1G47550.1; AT1G47550.1; AT1G47550. [Q9SX85-1]
DR GeneID; 841164; -.
DR Gramene; AT1G47550.1; AT1G47550.1; AT1G47550. [Q9SX85-1]
DR KEGG; ath:AT1G47550; -.
DR Araport; AT1G47550; -.
DR eggNOG; KOG2148; Eukaryota.
DR InParanoid; Q9SX85; -.
DR OMA; KEAKKCY; -.
DR PhylomeDB; Q9SX85; -.
DR PRO; PR:Q9SX85; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SX85; baseline and differential.
DR Genevisible; Q9SX85; AT.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR InterPro; IPR028258; Sec3-PIP2_bind.
DR InterPro; IPR019160; Sec3_C.
DR Pfam; PF15277; Sec3-PIP2_bind; 1.
DR Pfam; PF09763; Sec3_C; 2.
DR SMART; SM01313; Sec3-PIP2_bind; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Exocytosis; Membrane; Reference proteome; Secreted; Transport.
FT CHAIN 1..887
FT /note="Exocyst complex component SEC3A"
FT /id="PRO_0000356305"
FT REGION 542..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 221..248
FT /evidence="ECO:0000255"
FT COILED 281..301
FT /evidence="ECO:0000255"
SQ SEQUENCE 887 AA; 100065 MW; 533510830A4A5099 CRC64;
MAKSSADDEE LRRACEAAIE GTKQSIVMSI RVAKSRGVWG KSGKLGRQMA KPRVLALSVK
SKGPRKKAFL RVMKYSSGGV LEPAKMYKLK HLSKVEVITN DPSGCTFTLG FDNLRSQSVA
PPQWTMRNTD DRNRLLVCIL NICKDVLGRL PKVVGIDIVE MALWAKDNTP VVTTQRSTED
GEPVAESVTE SDLKVTVEKE LVSQAEEEDM EALLGTYVMG IGEAEAFSER LKRELQALEA
ANVHAILESE PLVDEVLNGL EAATNIVDDM DEWLGIFNIK LRHMREDIES IETRNNKLEM
QSVNNKALIE ELDKVIERLR VPSEYAASLT GGSFDEADML QNIEACEWLA KALRGLEVPN
LDPIYANMRA VKEKRAELEK LKATFVRRAS EFLRNYFASL VDFMVSDKSY FSQRGQLKRP
DHADLRYKCR TYARLLQHLK GLDKNCLGPL RKAYCSSLNL LLRREAREFA NELRASTKVS
RNPTVWLEGS TGSSQNANTD TSAVSDAYAK MLTIFIPLLV DESSFFAHFM CFEVPALAPP
GGAGNDKKSQ SNNDDGNDDD DLGIMDIDET DKKPGKNSPD LTALNESLQD LLDGIQEDFY
AVVDWAYKID PLRCISMHGI TERYLSGQKA DAAGFVRLLL GDLESRVSMQ FSRFVDEACH
QIERNERNVR QMGVLPYIPR FAALATRMEQ YIQGQSRDLV DQAYTKFVSI MFVTLEKIAQ
QDPKYADILL LENYAAFQNS LYDLANVVPT LAKFYHQASE AYEQACTRHI SMIIYYQFER
LFQFAKKIED FMYTITPEEI PFQLGLSKVE LRKMLKSSLS GVDKSIAAMY KKLQKNLASE
ELLPSLWDKC KKEFLDKYES FVQLVAKVYP SENVPGVTEM RGLLASM
