SYP41_ARATH
ID SYP41_ARATH Reviewed; 322 AA.
AC O65359; O04639;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tlg2p-like protein a {ECO:0000303|PubMed:10888666};
DE Short=AtTLG2a {ECO:0000303|PubMed:10888666};
DE AltName: Full=Syntaxin-41 {ECO:0000303|PubMed:11739776};
DE Short=AtSYP41 {ECO:0000303|PubMed:11739776};
GN Name=SYP41 {ECO:0000303|PubMed:11739776};
GN Synonyms=TLG2a {ECO:0000303|PubMed:10888666};
GN OrderedLocusNames=At5g26980 {ECO:0000312|Araport:AT5G26980};
GN ORFNames=F2P16.16 {ECO:0000312|EMBL:AAB61065.1};
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, INTERACTION WITH VPS45 AND VTI12, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=10888666; DOI=10.1091/mbc.11.7.2251;
RA Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT "AtVPS45 complex formation at the trans-Golgi network.";
RL Mol. Biol. Cell 11:2251-2265(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 INTERACTION WITH VTI12 AND SYP61, AND SUBCELLULAR LOCATION.
RX PubMed=11739776; DOI=10.1091/mbc.12.12.3733;
RA Sanderfoot A.A., Kovaleva V., Bassham D.C., Raikhel N.V.;
RT "Interactions between syntaxins identify at least five SNARE complexes
RT within the Golgi/prevacuolar system of the Arabidopsis cell.";
RL Mol. Biol. Cell 12:3733-3743(2001).
RN [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15743878; DOI=10.1242/dev.01716;
RA Koizumi K., Naramoto S., Sawa S., Yahara N., Ueda T., Nakano A.,
RA Sugiyama M., Fukuda H.;
RT "VAN3 ARF-GAP-mediated vesicle transport is involved in leaf vascular
RT network formation.";
RL Development 132:1699-1711(2005).
RN [7]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH SYP61; YKT61; YKT62 AND VTI12.
RX PubMed=15919093; DOI=10.1016/j.jmb.2005.04.061;
RA Chen Y., Shin Y.-K., Bassham D.C.;
RT "YKT6 is a core constituent of membrane fusion machineries at the
RT Arabidopsis trans-Golgi network.";
RL J. Mol. Biol. 350:92-101(2005).
RN [8]
RP INTERACTION WITH TNO1, AND TISSUE SPECIFICITY.
RC TISSUE=Silique;
RX PubMed=21521696; DOI=10.1104/pp.110.168963;
RA Kim S.-J., Bassham D.C.;
RT "TNO1 is involved in salt tolerance and vacuolar trafficking in
RT Arabidopsis.";
RL Plant Physiol. 156:514-526(2011).
RN [9]
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 [10]
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). Together with VTI12, required for membrane fusion
CC (PubMed:15919093). Vesicle trafficking protein that functions in the
CC secretory pathway and mediates liposome fusion; the fusion of
CC phospholipid vesicles containing SYP41 and VTI12 is triggered by YKT61
CC and YKT62 (PubMed:15919093, PubMed:24021022). Required for
CC 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).
CC {ECO:0000269|PubMed:15919093, ECO:0000269|PubMed:22307646,
CC ECO:0000269|PubMed:24021022}.
CC -!- SUBUNIT: Interacts with VTI12 and SYP61 to form a t-SNARE complex and
CC with VPS45 (PubMed:10888666, PubMed:11739776, PubMed:15919093).
CC Interacts with TNO1 (PubMed:21521696). Binds to YKT61 and YKT62
CC (PubMed:15919093). Core constituent of the SNARE complex required for
CC membrane fusion at the trans-Golgi network (PubMed:15919093).
CC {ECO:0000269|PubMed:10888666, ECO:0000269|PubMed:11739776,
CC ECO:0000269|PubMed:15919093, ECO:0000269|PubMed:21521696}.
CC -!- INTERACTION:
CC O65359; O49048: VPS45; NbExp=6; IntAct=EBI-1750331, EBI-1750377;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:10888666, ECO:0000269|PubMed:11739776,
CC ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:15743878,
CC ECO:0000269|PubMed:22307646}; Single-pass type IV membrane protein
CC {ECO:0000255}. Note=SYP41 is found in a different region of the TGN
CC than SYP42. {ECO:0000269|PubMed:11739776}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, to a lower extent in
CC leaves and roots, and, at low levels, in stems.
CC {ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:21521696}.
CC -!- DISRUPTION PHENOTYPE: Gametophytic lethal in homozygote plants
CC (PubMed:22307646). The double mutant syp41 syp42 have short roots
CC (PubMed:22307646). Plants lacking the three genes SYP41 SYP42 and SYP43
CC are seedling lethals (PubMed:22307646). {ECO:0000269|PubMed:22307646}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61065.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF067789; AAC27707.1; -; mRNA.
DR EMBL; AF007270; AAB61065.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93636.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93637.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70302.1; -; Genomic_DNA.
DR RefSeq; NP_001031950.1; NM_001036873.2.
DR RefSeq; NP_001331924.1; NM_001343989.1.
DR RefSeq; NP_198050.1; NM_122580.4.
DR AlphaFoldDB; O65359; -.
DR SMR; O65359; -.
DR BioGRID; 18031; 29.
DR IntAct; O65359; 25.
DR STRING; 3702.AT5G26980.1; -.
DR PaxDb; O65359; -.
DR PRIDE; O65359; -.
DR ProteomicsDB; 228485; -.
DR EnsemblPlants; AT5G26980.1; AT5G26980.1; AT5G26980.
DR EnsemblPlants; AT5G26980.2; AT5G26980.2; AT5G26980.
DR EnsemblPlants; AT5G26980.3; AT5G26980.3; AT5G26980.
DR GeneID; 832756; -.
DR Gramene; AT5G26980.1; AT5G26980.1; AT5G26980.
DR Gramene; AT5G26980.2; AT5G26980.2; AT5G26980.
DR Gramene; AT5G26980.3; AT5G26980.3; AT5G26980.
DR KEGG; ath:AT5G26980; -.
DR Araport; AT5G26980; -.
DR TAIR; locus:2148513; AT5G26980.
DR eggNOG; KOG0809; Eukaryota.
DR HOGENOM; CLU_038177_1_0_1; -.
DR InParanoid; O65359; -.
DR OMA; SIQEIHR; -.
DR OrthoDB; 1182451at2759; -.
DR PhylomeDB; O65359; -.
DR PRO; PR:O65359; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O65359; baseline and differential.
DR Genevisible; O65359; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
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:0009863; P:salicylic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0098629; P:trans-Golgi network membrane organization; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Membrane; Plant defense; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..322
FT /note="Tlg2p-like protein a"
FT /id="PRO_0000210258"
FT TOPO_DOM 1..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 226..288
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT COILED 116..146
FT /evidence="ECO:0000255"
SQ SEQUENCE 322 AA; 36134 MW; C7314E34BA0DD8E9 CRC64;
MATRNRTLLF RKYRNSLRSV RAPLSSSSLT GTRSGGVGPV IEMASTSLLN PNRSYAPIST
EDPGTSSKGA ITVGLPPAWV DVSEEISVNI QRARTKMAEL GKAHAKALMP SFGDGKEDQH
NIESLTQEIT FLLKKSEKQL QRLSASGPSE DSNVRKNVQR SLATDLQLLS MELRKKQSTY
LKRLRQQKED GMDLEMNLSR NRYRPEEDDF GDMLNEHQMS KIKKSEEVSV EREKEIQQVV
ESVNDLAQIM KDLSALVIDQ GTIVDRIDYN IENVATTVED GLKQLQKAER TQRHGGMVKC
ASVLVILCFI MLLLLILKEI FL
