SYP61_ARATH
ID SYP61_ARATH Reviewed; 245 AA.
AC Q946Y7; Q8VYF3; Q9SGP7;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Syntaxin-61 {ECO:0000303|PubMed:11739776};
DE Short=AtSYP61 {ECO:0000303|PubMed:11739776};
DE AltName: Full=Osmotic stress-sensitive mutant 1 {ECO:0000303|PubMed:12468724};
DE AltName: Full=Protein SYNTAXIN OF PLANTS 61 {ECO:0000303|PubMed:11739776};
GN Name=SYP61 {ECO:0000303|PubMed:11739776};
GN Synonyms=OSM1 {ECO:0000303|PubMed:12468724};
GN OrderedLocusNames=At1g28490 {ECO:0000312|Araport:AT1G28490};
GN ORFNames=F3M18.7 {ECO:0000312|EMBL:AAF16768.1};
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], PROTEIN SEQUENCE OF 173-189, INTERACTION WITH
RP SYP41; SYP42; SYP51; VTI11 AND VTI12, 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 [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=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 CHARACTERIZATION, FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. C24;
RX PubMed=12468724; DOI=10.1105/tpc.006981;
RA Zhu J., Gong Z., Zhang C., Song C.-P., Damsz B., Inan G., Koiwa H.,
RA Zhu J.-K., Hasegawa P.M., Bressan R.A.;
RT "OSM1/SYP61: a syntaxin protein in Arabidopsis controls abscisic acid-
RT mediated and non-abscisic acid-mediated responses to abiotic stress.";
RL Plant Cell 14:3009-3028(2002).
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, SUBUNIT, INTERACTION WITH SYP41, AND TISSUE SPECIFICITY.
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 SUBCELLULAR LOCATION.
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, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21826108; DOI=10.1038/cr.2011.129;
RA Drakakaki G., van de Ven W., Pan S., Miao Y., Wang J., Keinath N.F.,
RA Weatherly B., Jiang L., Schumacher K., Hicks G., Raikhel N.;
RT "Isolation and proteomic analysis of the SYP61 compartment reveal its role
RT in exocytic trafficking in Arabidopsis.";
RL Cell Res. 22:413-424(2012).
RN [10]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23832588; DOI=10.1105/tpc.113.112482;
RA Gendre D., McFarlane H.E., Johnson E., Mouille G., Sjoedin A., Oh J.,
RA Levesque-Tremblay G., Watanabe Y., Samuels L., Bhalerao R.P.;
RT "Trans-Golgi network localized ECHIDNA/Ypt interacting protein complex is
RT required for the secretion of cell wall polysaccharides in Arabidopsis.";
RL Plant Cell 25:2633-2646(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SYP121 AND PIP2-7, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25082856; DOI=10.1105/tpc.114.127159;
RA Hachez C., Laloux T., Reinhardt H., Cavez D., Degand H., Grefen C.,
RA De Rycke R., Inze D., Blatt M.R., Russinova E., Chaumont F.;
RT "Arabidopsis SNAREs SYP61 and SYP121 coordinate the trafficking of plasma
RT membrane aquaporin PIP2;7 to modulate the cell membrane water
RT permeability.";
RL Plant Cell 26:3132-3147(2014).
RN [12]
RP FUNCTION.
RX PubMed=25535279; DOI=10.1104/pp.114.249003;
RA Worden N., Wilkop T.E., Esteve V.E., Jeannotte R., Lathe R., Vernhettes S.,
RA Weimer B., Hicks G., Alonso J., Labavitch J., Persson S., Ehrhardt D.,
RA Drakakaki G.;
RT "CESA TRAFFICKING INHIBITOR inhibits cellulose deposition and interferes
RT with the trafficking of cellulose synthase complexes and their associated
RT proteins KORRIGAN1 and POM2/CELLULOSE SYNTHASE INTERACTIVE PROTEIN1.";
RL Plant Physiol. 167:381-393(2015).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC pathway; the fusion of phospholipid vesicles containing SYP61 and VTI12
CC is triggered by YKT61 and YKT62 (PubMed:15919093, PubMed:21826108).
CC Together with VTI12, required for membrane fusion (PubMed:15919093).
CC Involved in osmotic stress tolerance and in abscisic acid (ABA)
CC regulation of stomatal responses (PubMed:12468724). Plays a role in the
CC exocytic trafficking of cellulose synthases (CESAs) and the transport
CC of cell wall components to the plasma membrane (PubMed:21826108,
CC PubMed:25535279). Together with SYP121, regulates the post-Golgi
CC trafficking of the aquaporin PIP2-7 to the plasma membrane, thus
CC modulating cell membrane water permeability (PubMed:25082856).
CC {ECO:0000269|PubMed:12468724, ECO:0000269|PubMed:15919093,
CC ECO:0000269|PubMed:21826108, ECO:0000269|PubMed:25082856,
CC ECO:0000269|PubMed:25535279}.
CC -!- SUBUNIT: Interacts with VTI12 and either SYP41, SYP42 or SYP51 in the
CC trans-Golgi network or with VTI11 and SYP51 in the prevacuolar
CC compartment to form t-SNARE complexes (PubMed:11739776,
CC PubMed:15919093, PubMed:21826108). Core constituent of the SNARE
CC complex required for membrane fusion at the trans-Golgi network
CC (PubMed:15919093, PubMed:21826108). Also observed in the SYP121-complex
CC and cellulose synthases (PubMed:21826108). Colocalizes with PIP2-7 and
CC SYP121 in trafficking vesicles and at the plasma membrane
CC (PubMed:25082856). Interacts with SYP121 and PIP2-7 (PubMed:25082856).
CC {ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15919093,
CC ECO:0000269|PubMed:21826108, ECO:0000269|PubMed:25082856}.
CC -!- INTERACTION:
CC Q946Y7; Q9SA23: SYP51; NbExp=2; IntAct=EBI-4438441, EBI-4436558;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:11739776, ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:21826108, ECO:0000269|PubMed:23832588,
CC ECO:0000269|PubMed:25082856}; Single-pass type IV membrane protein
CC {ECO:0000255}. Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:23832588, ECO:0000269|PubMed:25082856}; Single-pass
CC type IV membrane protein {ECO:0000255}. Note=And along the cell wall
CC inner surface (PubMed:23832588). Intracellular trafficking is modulated
CC by TNO1 (PubMed:21521696). {ECO:0000269|PubMed:21521696,
CC ECO:0000269|PubMed:23832588}.
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=Q946Y7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in root, leaf, stem, flower and silique,
CC but not in hypocotyl or young leaf (PubMed:12468724, PubMed:15919093,
CC PubMed:15342965). Strong expression in the vasculature and in guard
CC cells of the leaf epidermis (PubMed:12468724).
CC {ECO:0000269|PubMed:12468724, ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:15919093}.
CC -!- INDUCTION: Not induced by osmotic stress or ABA treatment.
CC -!- DISRUPTION PHENOTYPE: Abnormally branched root pattern
CC (PubMed:12468724). Hypersensitivity to inhibition by Na(+), K(+) and
CC Li(+) but not Cs(+) (PubMed:12468724). Abnormal PIP2-7 trafficking and
CC subcellular localization leading to a reduced levels at the plasma
CC membrane and abnormal accumulation in globular or lenticular structures
CC (PubMed:25082856). {ECO:0000269|PubMed:12468724,
CC ECO:0000269|PubMed:25082856}.
CC -!- MISCELLANEOUS: The exact location of the SYP51/SYP61 complex is
CC unclear, but is probably on the trans-Golgi network because of the
CC likelihood of containing chiefly VTI12.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF16768.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF355754; AAK40222.2; -; mRNA.
DR EMBL; AC010155; AAF16768.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30982.1; -; Genomic_DNA.
DR EMBL; AY150420; AAN12965.1; -; mRNA.
DR EMBL; AY072115; AAL59937.1; -; mRNA.
DR RefSeq; NP_564310.1; NM_102617.4. [Q946Y7-1]
DR AlphaFoldDB; Q946Y7; -.
DR SMR; Q946Y7; -.
DR BioGRID; 24984; 13.
DR IntAct; Q946Y7; 7.
DR STRING; 3702.AT1G28490.1; -.
DR iPTMnet; Q946Y7; -.
DR PaxDb; Q946Y7; -.
DR PRIDE; Q946Y7; -.
DR ProteomicsDB; 228486; -. [Q946Y7-1]
DR EnsemblPlants; AT1G28490.1; AT1G28490.1; AT1G28490. [Q946Y7-1]
DR GeneID; 839749; -.
DR Gramene; AT1G28490.1; AT1G28490.1; AT1G28490. [Q946Y7-1]
DR KEGG; ath:AT1G28490; -.
DR Araport; AT1G28490; -.
DR TAIR; locus:2032569; AT1G28490.
DR eggNOG; KOG3202; Eukaryota.
DR HOGENOM; CLU_061883_3_0_1; -.
DR InParanoid; Q946Y7; -.
DR OMA; EHDPYRF; -.
DR PhylomeDB; Q946Y7; -.
DR PRO; PR:Q946Y7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q946Y7; baseline and differential.
DR Genevisible; Q946Y7; 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:TAIR.
DR GO; GO:0032588; C:trans-Golgi network membrane; 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:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0052324; P:plant-type cell wall cellulose biosynthetic process; IDA: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; IPR015260; Syntaxin-6_N.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF09177; Syntaxin-6_N; 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 Abscisic acid signaling pathway; Alternative splicing;
KW Direct protein sequencing; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..245
FT /note="Syntaxin-61"
FT /id="PRO_0000210263"
FT TOPO_DOM 1..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 153..215
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT CONFLICT 240
FT /note="V -> I (in Ref. 4; AAL59937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27722 MW; 19E979D31525BCF2 CRC64;
MSSAQDPFYI VKEEIQDSID KLQSTFHKWE RISPDMGDQA HVAKELVATC GSIEWQVDEL
EKAITVAAKD PSWYGIDEAE LEKRRRWTSN ARTQVRNVKS GVLAGKVSSG AGHASEVRRE
LMRMPNSGEA SRYDQYGGRD DDGFVQSESD RQMLLIKQQD EELDELSKSV QRIGGVGLTI
HDELVAQERI IDELDTEMDS TKNRLEFVQK KVGMVMKKAG AKGQMMMICF LLVLFIILFV
LVFLT
