SEC5A_ARATH
ID SEC5A_ARATH Reviewed; 1090 AA.
AC Q8S3U9; Q0WL36; Q541W6; Q9C6K6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Exocyst complex component SEC5A {ECO:0000303|PubMed:19895414};
DE Short=AtSec5a {ECO:0000303|PubMed:19895414};
DE AltName: Full=Exocyst complex component 2;
GN Name=SEC5A {ECO:0000303|PubMed:19895414};
GN OrderedLocusNames=At1g76850 {ECO:0000312|Araport:AT1G76850};
GN ORFNames=F7O12.2 {ECO:0000312|EMBL:AAG51148.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Elias M., Cvrckova F., Zarsky V.;
RT "Molecular characterization of the exocyst complex in Arabidopsis
RT thaliana.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-1090.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [8]
RP COMPONENT OF THE EXOCYST COMPLEX, AND DISRUPTION PHENOTYPE.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [11]
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 [12]
RP INTERACTION WITH EXO70H1 AND 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).
RN [13]
RP INTERACTION WITH SEC3A.
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 [14]
RP FUNCTION, AND 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 [15]
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. 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. {ECO:0000269|PubMed:23944713}.
CC -!- SUBUNIT: The exocyst complex is composed of SEC3, SEC5, SEC6, SEC8,
CC SEC10, EXO70A1 and EXO84B. Interacts with SEC3A and EXO70B1. Binds to
CC EXO70H1 AND EXO70B2 (PubMed:21199889). {ECO:0000269|PubMed:21199889,
CC ECO:0000269|PubMed:23495664, ECO:0000269|PubMed:23944713}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:24307681}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:24307681}. Note=Localized to globular structures in
CC the perinuclear region (PubMed:19895414). Shuttles from the cytoplasm
CC to the exocyst-positive organelle (EXPO) in the presence of EXO70E2
CC (PubMed:24307681). {ECO:0000269|PubMed:19895414,
CC ECO:0000269|PubMed:24307681}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but the double mutant sec5a-1 and sec5b-1 is male
CC gametophytic lethal due to defect in pollen germination and pollen tube
CC growth. {ECO:0000269|PubMed:18492870}.
CC -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000305}.
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DR EMBL; AF479278; AAL87121.1; -; mRNA.
DR EMBL; AC079283; AAG51148.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35895.1; -; Genomic_DNA.
DR EMBL; AK118540; BAC43143.1; -; mRNA.
DR EMBL; BT005978; AAO64913.1; -; mRNA.
DR EMBL; AK230372; BAF02171.1; -; mRNA.
DR PIR; C96797; C96797.
DR RefSeq; NP_177811.2; NM_106336.4.
DR AlphaFoldDB; Q8S3U9; -.
DR SMR; Q8S3U9; -.
DR BioGRID; 29239; 4.
DR IntAct; Q8S3U9; 4.
DR STRING; 3702.AT1G76850.1; -.
DR TCDB; 1.F.2.1.3; the octameric exocyst (exocyst) family.
DR iPTMnet; Q8S3U9; -.
DR PaxDb; Q8S3U9; -.
DR PRIDE; Q8S3U9; -.
DR ProteomicsDB; 232950; -.
DR EnsemblPlants; AT1G76850.1; AT1G76850.1; AT1G76850.
DR GeneID; 844020; -.
DR Gramene; AT1G76850.1; AT1G76850.1; AT1G76850.
DR KEGG; ath:AT1G76850; -.
DR Araport; AT1G76850; -.
DR TAIR; locus:2030056; AT1G76850.
DR eggNOG; KOG2347; Eukaryota.
DR HOGENOM; CLU_003742_0_0_1; -.
DR InParanoid; Q8S3U9; -.
DR OMA; LFPDACG; -.
DR OrthoDB; 97000at2759; -.
DR PhylomeDB; Q8S3U9; -.
DR PRO; PR:Q8S3U9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8S3U9; baseline and differential.
DR Genevisible; Q8S3U9; AT.
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:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0060321; P:acceptance of pollen; IMP:TAIR.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR PANTHER; PTHR13043; PTHR13043; 1.
DR Pfam; PF15469; Sec5; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Exocytosis; Phosphoprotein; Reference proteome; Secreted;
KW Transport.
FT CHAIN 1..1090
FT /note="Exocyst complex component SEC5A"
FT /id="PRO_0000118923"
FT REGION 18..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT CONFLICT 384..388
FT /note="Missing (in Ref. 2; AAG51148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1090 AA; 121902 MW; 9E0C29580CBE3AD8 CRC64;
MSSDSNDLDE DELLQMALKE QAKRDLTYQK PPSSSARKPV ANLVQQPRQQ KPVAAAAAPP
KKSAAAVRKP SMDEDEESEV ELLSISSGDD DLEREREIGG SSGGAGRGRG SDVREKGRAR
KEDDGAWDGG EPDCWKRVNE AELARRVRDM RESRTAPVVQ KVEGKAPAPG KKVALTSLQS
LPRGMECIDP LKLGIIDNKT LRLITESSGS PSKAEKVDNT LREKLVYFSD HFDPKLFLSR
IHQDTTAADL EAGALGLKSD LKGRNLQRKQ LVKDNFDCFV SCKTTIDDIE SKLKRIEEDP
EGSGTTHLFN CMKSVTSRAN LAFEPLFERQ AQAEKIRSVQ GMLQRFRTLF NLPSIIRSSI
SKGEYDLAVR EYKKAKSIAL PSHVNILKRV LEEVEKVMLE FKGTLYKSME DPKIDFTSLE
NTVRLLLELE PESDPVWHYL NVQNHRIHGL LEKCTYDHEA RVEILRNDTH EKAISDAKWQ
QIQQNGVSYS DTASSNENNA VQVDLQSVEF PSEEIDILKG RYIKRLTAVL VHHIPVFWKT
AISIFSGKFA KSSQVTDTSA NKAEEKVTEA RYSTHSLEEV AGMIRKTISV YEAKVNSTFC
DFDESCILRP FMSDAINEVS KACQAFEAKE STPHSAVVAL RKIQAEITKI YIQRLCSWMR
ASTEGISKEE TWIPVSILER NRSPYAISYL PLAFRSVIVS GMEQVNLMIL SVKSEAAKSE
DMFAQIEEII ISVRLAFLNC FLDFAAHLEQ IGADLSQSTS RQDNWKNGYS DEHQEEPSAN
TYGSVIDPHR RLLMVLSNIG YCKDELASEL YNKFKYTWLQ SRDKNEDSSD LQDLIMSFSG
LGEKVLEHYT FAKANLIRTA ATNYLLDSGI QWGSAPQVKG IRDAAVELLH TLVAVHAEVF
AGAKPLLDKI LGVLIEGLID TFLSVVEENR SSDLRSIDAN GFCQLMFELE YFETVLYSYF
TSAATESLKS LQGTVLEIAI ESISEAVETP GHNRRPTRGS EDTVSDDKQS VSADDLLALT
KQCSNELLQQ ELERTRVNTA CFAESAPLES TPPLPKATYS SFRGSMDSPS RNYRGSQSSG
SPINARPRRR
