SY121_ARATH
ID SY121_ARATH Reviewed; 346 AA.
AC Q9ZSD4; F4J7G9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 173.
DE RecName: Full=Syntaxin-121 {ECO:0000303|PubMed:11718726};
DE Short=AtSYP121 {ECO:0000303|PubMed:11718726};
DE AltName: Full=Protein SYNTAXIN OF PLANTS 121 {ECO:0000303|PubMed:11718726};
DE AltName: Full=Syntaxin-related protein At-Syr1 {ECO:0000303|PubMed:9915701};
GN Name=SYP121 {ECO:0000303|PubMed:11718726};
GN Synonyms=SYR1 {ECO:0000303|PubMed:9915701};
GN OrderedLocusNames=At3g11820 {ECO:0000312|Araport:AT3G11820};
GN ORFNames=F26K24.11 {ECO:0000312|EMBL:AAF23198.1};
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 1).
RC STRAIN=cv. Columbia;
RX PubMed=9915701; DOI=10.1126/science.283.5401.537;
RA Leyman B., Geelen D., Quintero F.J., Blatt M.R.;
RT "A tobacco syntaxin with a role in hormonal control of guard cell ion
RT channels.";
RL Science 283:537-540(1999).
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 2).
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 INTERACTION WITH SNAP33.
RX PubMed=11718726; DOI=10.1016/s0014-5793(01)03089-7;
RA Kargul J., Gansel X., Tyrrell M., Sticher L., Blatt M.R.;
RT "Protein-binding partners of the tobacco syntaxin NtSyr1.";
RL FEBS Lett. 508:253-258(2001).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
RN [9]
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 [10]
RP 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS] (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH SYP61 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).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC pathway (By similarity). Together with SYP61, 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:0000250|UniProtKB:Q946Y7, ECO:0000269|PubMed:25082856}.
CC -!- SUBUNIT: Part of the t-SNARE complex (PubMed:11718726,
CC PubMed:21826108). Binds to SNAP33 (PubMed:11718726). Colocalizes with
CC SYP61 and PIP2-7 in trafficking vesicles and at the plasma membrane
CC (PubMed:25082856). Interacts with SYP61 and PIP2-7 (PubMed:25082856).
CC {ECO:0000269|PubMed:11718726, ECO:0000269|PubMed:21826108,
CC ECO:0000269|PubMed:25082856}.
CC -!- INTERACTION:
CC Q9ZSD4; Q9S7P9: SNAP33; NbExp=4; IntAct=EBI-4476863, EBI-603017;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130,
CC ECO:0000269|PubMed:15342965, ECO:0000269|PubMed:25082856}; Single-pass
CC type IV membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000269|PubMed:15342965,
CC ECO:0000269|PubMed:21826108, ECO:0000269|PubMed:25082856}; Single-pass
CC type IV membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZSD4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZSD4-2; Sequence=VSP_057947;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, stems, flowers
CC and leaves. {ECO:0000269|PubMed:15342965}.
CC -!- INDUCTION: Ninefold induction within 30-min exposure to abscisic acid
CC and after 48 hours drought stress.
CC -!- DISRUPTION PHENOTYPE: Abnormal PIP proteins (e.g. PIP1-4, PIP2-1 and
CC PIP2-7) trafficking and subcellular localization leading to a reduced
CC levels at the plasma membrane. {ECO:0000269|PubMed:25082856}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF112864; AAD11809.1; -; mRNA.
DR EMBL; AC016795; AAF23198.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75102.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75103.1; -; Genomic_DNA.
DR EMBL; AY093151; AAM13150.1; -; mRNA.
DR EMBL; BT003393; AAO30056.1; -; mRNA.
DR EMBL; AY087842; AAM65395.1; -; mRNA.
DR RefSeq; NP_187788.1; NM_112015.3. [Q9ZSD4-1]
DR RefSeq; NP_974288.1; NM_202559.3. [Q9ZSD4-2]
DR AlphaFoldDB; Q9ZSD4; -.
DR SMR; Q9ZSD4; -.
DR BioGRID; 5689; 68.
DR DIP; DIP-59829N; -.
DR IntAct; Q9ZSD4; 60.
DR STRING; 3702.AT3G11820.1; -.
DR TCDB; 8.A.91.1.7; the syntaxin (syntaxin) family.
DR iPTMnet; Q9ZSD4; -.
DR SwissPalm; Q9ZSD4; -.
DR PaxDb; Q9ZSD4; -.
DR PRIDE; Q9ZSD4; -.
DR ProteomicsDB; 226782; -. [Q9ZSD4-1]
DR EnsemblPlants; AT3G11820.1; AT3G11820.1; AT3G11820. [Q9ZSD4-1]
DR EnsemblPlants; AT3G11820.2; AT3G11820.2; AT3G11820. [Q9ZSD4-2]
DR GeneID; 820355; -.
DR Gramene; AT3G11820.1; AT3G11820.1; AT3G11820. [Q9ZSD4-1]
DR Gramene; AT3G11820.2; AT3G11820.2; AT3G11820. [Q9ZSD4-2]
DR KEGG; ath:AT3G11820; -.
DR Araport; AT3G11820; -.
DR TAIR; locus:2081476; AT3G11820.
DR eggNOG; KOG0810; Eukaryota.
DR InParanoid; Q9ZSD4; -.
DR PhylomeDB; Q9ZSD4; -.
DR PRO; PR:Q9ZSD4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9ZSD4; baseline and differential.
DR Genevisible; Q9ZSD4; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0043495; F:protein-membrane adaptor activity; IDA:TAIR.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IGI:TAIR.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0072660; P:maintenance of protein location in plasma membrane; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:TAIR.
DR GO; GO:0006612; P:protein targeting to membrane; IDA:TAIR.
DR GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009620; P:response to fungus; IMP:TAIR.
DR GO; GO:0032940; P:secretion by cell; IDA:TAIR.
DR GO; GO:0010148; P:transpiration; IMP:TAIR.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
DR CDD; cd00179; SynN; 1.
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 Pfam; PF00804; Syntaxin; 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 Acetylation; Alternative initiation; Cell membrane; Coiled coil;
KW Golgi apparatus; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..346
FT /note="Syntaxin-121"
FT /id="PRO_0000210246"
FT TOPO_DOM 1..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..346
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 214..276
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..76
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057947"
FT INIT_MET Q9ZSD4-2:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q9ZSD4-2:2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 346 AA; 37957 MW; 8A6E2390761A8446 CRC64;
MNDLFSSSFS RFRSGEPSPR RDVAGGGDGV QMANPAGSTG GVNLDKFFED VESVKEELKE
LDRLNETLSS CHEQSKTLHN AKAVKDLRSK MDGDVGVALK KAKMIKVKLE ALDRANAANR
SLPGCGPGSS SDRTRTSVLN GLRKKLMDSM DSFNRLRELI SSEYRETVQR RYFTVTGENP
DERTLDRLIS TGESERFLQK AIQEQGRGRV LDTINEIQER HDAVKDIEKN LRELHQVFLD
MAVLVEHQGA QLDDIESHVG RASSFIRGGT DQLQTARVYQ KNTRKWTCIA IIILIIIITV
VVLAVLKPWN NSSGGGGGGG GGGTTGGSQP NSGTPPNPPQ ARRLLR
