SYP42_ARATH
ID SYP42_ARATH Reviewed; 323 AA.
AC Q9SWH4; O04258; Q9SBD4;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Syntaxin-42 {ECO:0000303|PubMed:11739776};
DE Short=AtSYP42 {ECO:0000303|PubMed:11739776};
DE Short=AtTLG2b {ECO:0000303|PubMed:10888666};
GN Name=SYP42 {ECO:0000303|PubMed:11739776};
GN Synonyms=TLG2b {ECO:0000303|PubMed:10888666};
GN OrderedLocusNames=At4g02195 {ECO:0000312|Araport:AT4G02195};
GN ORFNames=T10M13.19 {ECO:0000312|EMBL:AAC78709.1},
GN T2H3.1 {ECO:0000312|EMBL:AAC28171.1};
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, AND INTERACTION WITH VPS45.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [7]
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).
CC {ECO:0000269|PubMed:22307646, ECO:0000269|PubMed:24021022}.
CC -!- SUBUNIT: Interacts with VTI12 and SYP61 to form a t-SNARE complex and
CC with VPS45. {ECO:0000269|PubMed:10888666, ECO:0000269|PubMed:11739776}.
CC -!- INTERACTION:
CC Q9SWH4; O49048: VPS45; NbExp=4; IntAct=EBI-1750405, EBI-1750377;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:22307646}; Single-pass type IV membrane protein
CC {ECO:0000255}. Note=SYP42 is found in a different region of the TGN
CC than SYP41. {ECO:0000269|PubMed:11739776}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, flowers
CC and leaves. {ECO:0000269|PubMed:15342965}.
CC -!- DISRUPTION PHENOTYPE: Gametophytic lethal in homozygote plants
CC (PubMed:22307646). Slightly shorter roots (PubMed:22307646). The double
CC mutant syp41 syp42 have short roots (PubMed:22307646). The double
CC mutant syp42 syp43 exhibits severe pleiotropic defects, including short
CC roots, a large number of lateral roots, semi dwarfism and early
CC senescence; these phenotypes are associated with defective secretory
CC and vacuolar transport pathways (PubMed:22307646). Double mutant plants
CC syp42 syp43 have an increased sensitivity to the powdery fungus
CC Golovinomyces orontii with leaf chlorosis in a pathogen-inducible
CC salicylic acid (SA) biosynthesis-dependent manner, thus revealing a
CC biotic stress-induced and SA-dependent chloroplast dysfunction
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=AAC28171.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC78709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF154574; AAD38983.1; -; mRNA.
DR EMBL; AF001308; AAC78709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF075597; AAC28171.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82136.1; -; Genomic_DNA.
DR PIR; T01521; T01521.
DR RefSeq; NP_567223.1; NM_116452.4.
DR AlphaFoldDB; Q9SWH4; -.
DR SMR; Q9SWH4; -.
DR BioGRID; 12798; 25.
DR IntAct; Q9SWH4; 22.
DR STRING; 3702.AT4G02195.1; -.
DR PaxDb; Q9SWH4; -.
DR PRIDE; Q9SWH4; -.
DR ProteomicsDB; 233051; -.
DR EnsemblPlants; AT4G02195.1; AT4G02195.1; AT4G02195.
DR GeneID; 827505; -.
DR Gramene; AT4G02195.1; AT4G02195.1; AT4G02195.
DR KEGG; ath:AT4G02195; -.
DR Araport; AT4G02195; -.
DR TAIR; locus:505006427; AT4G02195.
DR eggNOG; KOG0809; Eukaryota.
DR HOGENOM; CLU_038177_1_0_1; -.
DR InParanoid; Q9SWH4; -.
DR OMA; VEWNVME; -.
DR OrthoDB; 1182451at2759; -.
DR PhylomeDB; Q9SWH4; -.
DR PRO; PR:Q9SWH4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SWH4; baseline and differential.
DR Genevisible; Q9SWH4; 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; 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:1900150; P:regulation of defense response to fungus; 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 1: Evidence at protein level;
KW Golgi apparatus; Membrane; Plant defense; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..323
FT /note="Syntaxin-42"
FT /id="PRO_0000210259"
FT TOPO_DOM 1..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 227..289
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
SQ SEQUENCE 323 AA; 36432 MW; ACE3B9EAAA1719BD CRC64;
MATRNRTTVY RKHRDACKSA RAPLSLSASD SFGGPVIEMV SGSFSRSNHS SYAPLNSYDP
GPSSSDAFTI GMPPAWVDDS EEITFNIQKV RDKMNELAKA HSKALMPTFG DNKGIHREVE
MLTHEITDLL RKSEKRLQML STRGPSEESN LRKNVQRSLA TDLQNLSMEL RRKQSTYLKR
LQQQKEGQDE VDLEFNVNGK MSRLDEEDEL GGMGFDEHQT IKLKEGQHVS AEREREIQQV
LGSVNDLAQI MKDLSALVID QGTIVDRIDY NVQNVSTSVE EGYKQLQKAE RTQREGAMVK
CATILLVLCL IMIVLLILKN ILF
