SYP43_ARATH
ID SYP43_ARATH Reviewed; 331 AA.
AC Q9SUJ1; Q8L7J6; Q9M9X6;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Syntaxin-43 {ECO:0000303|Ref.1};
DE Short=AtSYP43 {ECO:0000303|Ref.1};
GN Name=SYP43 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At3g05710 {ECO:0000312|Araport:AT3G05710};
GN ORFNames=F18C1.2 {ECO:0000312|EMBL:AAF26126.1};
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Gansel X., Sticher L.;
RT "Vesicle traffic in Arabidopsis thaliana: characterization of AtSNAP33, a
RT novel plant t-SNARE that interacts with syntaxins.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15342965; DOI=10.1247/csf.29.49;
RA Uemura T., Ueda T., Ohniwa R.L., Nakano A., Takeyasu K., Sato M.H.;
RT "Systematic analysis of SNARE molecules in Arabidopsis: dissection of the
RT post-Golgi network in plant cells.";
RL Cell Struct. Funct. 29:49-65(2004).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=22307646; DOI=10.1073/pnas.1115146109;
RA Uemura T., Kim H., Saito C., Ebine K., Ueda T., Schulze-Lefert P.,
RA Nakano A.;
RT "Qa-SNAREs localized to the trans-Golgi network regulate multiple transport
RT pathways and extracellular disease resistance in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1784-1789(2012).
RN [8]
RP FUNCTION.
RX PubMed=24021022; DOI=10.1186/1471-2091-14-22;
RA Kim S.-J., Bassham D.C.;
RT "Functional redundancy between trans-Golgi network SNARE family members in
RT Arabidopsis thaliana.";
RL BMC Biochem. 14:22-22(2013).
CC -!- FUNCTION: Contributes to the regulation of secretory and vacuolar
CC transport pathways in the post-Golgi network, and to the maintenance of
CC the Golgi apparatus and trans-Golgi network (TGN) morphologies
CC (PubMed:22307646). Vesicle trafficking protein that functions in the
CC secretory pathway and mediates liposome fusion (PubMed:24021022).
CC Required for extracellular resistance responses to a fungal pathogen
CC (PubMed:22307646). Also involved in the protection of chloroplasts from
CC salicylic acid-dependent biotic stress (PubMed:22307646). Also involved
CC in the protection of chloroplasts from salicylic acid-dependent biotic
CC stress (PubMed:22307646). {ECO:0000269|PubMed:22307646,
CC ECO:0000269|PubMed:24021022}.
CC -!- SUBUNIT: Part of the t-SNARE complex. {ECO:0000250|UniProtKB:Q9SWH4}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:22307646}; Single-pass
CC type IV membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SUJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SUJ1-2; Sequence=VSP_009005;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, flowers
CC and leaves. {ECO:0000269|PubMed:15342965}.
CC -!- DISRUPTION PHENOTYPE: The double mutant syp42 syp43 exhibits severe
CC pleiotropic defects, including short roots, a large number of lateral
CC roots, semi dwarfism and early senescence (PubMed:22307646). Plants
CC lacking the three genes SYP41 SYP42 and SYP43 are seedling lethals
CC (PubMed:22307646). {ECO:0000269|PubMed:22307646}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AJ245408; CAB52175.1; -; mRNA.
DR EMBL; AC011620; AAF26126.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74282.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74283.1; -; Genomic_DNA.
DR EMBL; AY099723; AAM20574.1; -; mRNA.
DR EMBL; AY128886; AAM91286.1; -; mRNA.
DR EMBL; AY088000; AAM65546.1; -; mRNA.
DR RefSeq; NP_566256.1; NM_111445.5. [Q9SUJ1-2]
DR RefSeq; NP_850519.1; NM_180188.3. [Q9SUJ1-1]
DR AlphaFoldDB; Q9SUJ1; -.
DR SMR; Q9SUJ1; -.
DR BioGRID; 5075; 55.
DR IntAct; Q9SUJ1; 55.
DR STRING; 3702.AT3G05710.2; -.
DR SwissPalm; Q9SUJ1; -.
DR PaxDb; Q9SUJ1; -.
DR PRIDE; Q9SUJ1; -.
DR ProteomicsDB; 228469; -. [Q9SUJ1-1]
DR EnsemblPlants; AT3G05710.1; AT3G05710.1; AT3G05710. [Q9SUJ1-2]
DR EnsemblPlants; AT3G05710.2; AT3G05710.2; AT3G05710. [Q9SUJ1-1]
DR GeneID; 819740; -.
DR Gramene; AT3G05710.1; AT3G05710.1; AT3G05710. [Q9SUJ1-2]
DR Gramene; AT3G05710.2; AT3G05710.2; AT3G05710. [Q9SUJ1-1]
DR KEGG; ath:AT3G05710; -.
DR Araport; AT3G05710; -.
DR TAIR; locus:2078042; AT3G05710.
DR eggNOG; KOG0809; Eukaryota.
DR HOGENOM; CLU_038177_1_0_1; -.
DR InParanoid; Q9SUJ1; -.
DR OMA; QTMIIDQ; -.
DR OrthoDB; 1182451at2759; -.
DR PhylomeDB; Q9SUJ1; -.
DR PRO; PR:Q9SUJ1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SUJ1; baseline and differential.
DR Genevisible; Q9SUJ1; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0009658; P:chloroplast organization; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0006896; P:Golgi to vacuole transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IGI:TAIR.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IMP:UniProtKB.
DR GO; GO:0007034; P:vacuolar transport; IGI:TAIR.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IDA:UniProtKB.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Plant defense; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..331
FT /note="Syntaxin-43"
FT /id="PRO_0000210260"
FT TOPO_DOM 1..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..331
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 235..297
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 20..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..154
FT /evidence="ECO:0000255"
FT COMPBIAS 20..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.5"
FT /id="VSP_009005"
FT CONFLICT 207
FT /note="N -> T (in Ref. 4; AAM91286)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="N -> I (in Ref. 4; AAM91286)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="G -> K (in Ref. 4; AAM91286)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="V -> A (in Ref. 5; AAM65546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36981 MW; 12C14301C2FBB6F9 CRC64;
MATRNRTLLF RKYRNSLRSV RAPMGSSSSS TLTEHNSLTG AKSGLGPVIE MASTSLLNPN
RSYAPVSTED PGNSSRGTIT VGLPPDWVDV SEEISVYIQR ARTKMAELGK AHAKALMPSF
GDGKEDQHQI ETLTQEVTFL LKKSEKQLQR LSAAGPSEDS NVRKNVQRSL ATDLQNLSME
LRKKQSTYLK RLRLQKEDGA DLEMNLNGSR YKAEDDDFDD MVFSEHQMSK IKKSEEISIE
REKEIQQVVE SVSELAQIMK DLSALVIDQG TIVDRIDYNI QNVASTVDDG LKQLQKAERT
QRQGGMVMCA SVLVILCFIM LVLLILKEIL L
