SY132_ARATH
ID SY132_ARATH Reviewed; 304 AA.
AC Q8VZU2; Q9LEZ8;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Syntaxin-132 {ECO:0000305};
DE Short=AtSYP132 {ECO:0000305};
GN Name=SYP132 {ECO:0000303|PubMed:19098073};
GN OrderedLocusNames=At5g08080 {ECO:0000312|Araport:AT5G08080};
GN ORFNames=T22D6.20 {ECO:0000312|EMBL:CAB93709.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=19098073; DOI=10.1093/pcp/pcn197;
RA Enami K., Ichikawa M., Uemura T., Kutsuna N., Hasezawa S., Nakagawa T.,
RA Nakano A., Sato M.H.;
RT "Differential expression control and polarized distribution of plasma
RT membrane-resident SYP1 SNAREs in Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:280-289(2009).
RN [6]
RP FUNCTION.
RX PubMed=24642714; DOI=10.1093/pcp/pcu048;
RA Ichikawa M., Hirano T., Enami K., Fuselier T., Kato N., Kwon C., Voigt B.,
RA Schulze-Lefert P., Baluska F., Sato M.H.;
RT "Syntaxin of plant proteins SYP123 and SYP132 mediate root hair tip growth
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 55:790-800(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=29396117; DOI=10.1016/j.devcel.2017.12.027;
RA Park M., Krause C., Karnahl M., Reichardt I., El Kasmi F., Mayer U.,
RA Stierhof Y.D., Hiller U., Strompen G., Bayer M., Kientz M., Sato M.H.,
RA Nishimura M.T., Dangl J.L., Sanderfoot A.A., Juergens G.;
RT "Concerted action of evolutionarily ancient and novel SNARE complexes in
RT flowering-plant cytokinesis.";
RL Dev. Cell 44:500-511.e4(2018).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=30926657; DOI=10.1104/pp.19.00266;
RA Xia L., Mar Marques-Bueno M., Bruce C.G., Karnik R.;
RT "Unusual roles of secretory SNARE SYP132 in plasma membrane H+-ATPase
RT traffic and vegetative plant growth.";
RL Plant Physiol. 180:837-858(2019).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC pathway (Probable). Acts in coordination with SYP123 to mediate tip-
CC focused membrane trafficking for root hair tip growth
CC (PubMed:24642714). Functions in root hair elongation by forming SNARE
CC complexes with VAMP721,VAMP722 or VAMP724 (PubMed:24642714). Involved
CC in cytokinesis (PubMed:29396117). Acts as a cell plate-specific
CC syntaxin, required for the fusion of vesicles at the plane of cell
CC division (PubMed:29396117). Required for secretory trafficking to the
CC plasma membrane during interphase (PubMed:29396117). Involved in the
CC regulation of density of the H(+) ATPase proteins at the plasma
CC membrane of root and shoot in epidermal cells (PubMed:30926657).
CC Modulation of SYP132 expression by auxin affects clathrin-sensitive
CC H(+) ATPase traffic from the plasma membrane, and influences apoplastic
CC acidification and plant growth (PubMed:30926657).
CC {ECO:0000269|PubMed:24642714, ECO:0000269|PubMed:29396117,
CC ECO:0000269|PubMed:30926657, ECO:0000305|PubMed:24642714}.
CC -!- SUBUNIT: Part of the t-SNARE complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29396117,
CC ECO:0000269|PubMed:30926657}; Single-pass type IV membrane protein
CC {ECO:0000255}.
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=Q8VZU2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed in all tissues throughout plant
CC development. {ECO:0000269|PubMed:19098073}.
CC -!- INDUCTION: Induced by auxin in roots (PubMed:30926657). Down-regulated
CC by auxin in shoots (PubMed:30926657). {ECO:0000269|PubMed:30926657}.
CC -!- DISRUPTION PHENOTYPE: Defect in cytokinesis in embryos and defect in
CC seedling growth. {ECO:0000269|PubMed:29396117}.
CC -!- MISCELLANEOUS: Plants silencing SYP132 exhibit reduced root hair
CC length. {ECO:0000269|PubMed:24642714}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB93709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL357612; CAB93709.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91242.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70609.1; -; Genomic_DNA.
DR EMBL; AY063836; AAL36192.1; -; mRNA.
DR EMBL; AY117244; AAM51319.1; -; mRNA.
DR PIR; T50493; T50493.
DR RefSeq; NP_001332203.1; NM_001342979.1. [Q8VZU2-1]
DR RefSeq; NP_568187.1; NM_120890.3. [Q8VZU2-1]
DR AlphaFoldDB; Q8VZU2; -.
DR SMR; Q8VZU2; -.
DR BioGRID; 15980; 54.
DR IntAct; Q8VZU2; 53.
DR STRING; 3702.AT5G08080.3; -.
DR iPTMnet; Q8VZU2; -.
DR SwissPalm; Q8VZU2; -.
DR ProteomicsDB; 226775; -. [Q8VZU2-1]
DR EnsemblPlants; AT5G08080.1; AT5G08080.1; AT5G08080. [Q8VZU2-1]
DR EnsemblPlants; AT5G08080.4; AT5G08080.4; AT5G08080. [Q8VZU2-1]
DR GeneID; 830702; -.
DR Gramene; AT5G08080.1; AT5G08080.1; AT5G08080. [Q8VZU2-1]
DR Gramene; AT5G08080.4; AT5G08080.4; AT5G08080. [Q8VZU2-1]
DR KEGG; ath:AT5G08080; -.
DR Araport; AT5G08080; -.
DR eggNOG; KOG0810; Eukaryota.
DR InParanoid; Q8VZU2; -.
DR OMA; RWICFIL; -.
DR PhylomeDB; Q8VZU2; -.
DR PRO; PR:Q8VZU2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZU2; baseline and differential.
DR Genevisible; Q8VZU2; 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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
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 splicing; Cell cycle; Cell division;
KW Cell membrane; Coiled coil; Growth regulation; Membrane; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..304
FT /note="Syntaxin-132"
FT /id="PRO_0000210252"
FT TOPO_DOM 1..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..304
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 204..266
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 34..67
FT /evidence="ECO:0000255"
FT COILED 129..162
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9ZSD4"
SQ SEQUENCE 304 AA; 34225 MW; 8A6B7A962C43ACF2 CRC64;
MNDLLKGSFE LPRGQSSREG DVELGEQQGG DQGLEDFFKK VQVIDKQYDK LDKLLKKLQA
SHEESKSVTK APAMKAIKKT MEKDVDEVGS IARFIKGKLE ELDRENLANR QKPGCAKGSG
VDRSRTATTL SLKKKLKDKM AEFQVLRENI QQEYRDVVDR RVYTVTGERA DEDTIDELIE
TGNSEQIFQK AIQEQGRGQV MDTLAEIQER HDAVRDLEKK LLDLQQIFLD MAVLVDAQGE
MLDNIESQVS SAVDHVQSGN TALQRAKSLQ KNSRKWMCIA IIILLIVVAV IVVGVLKPWK
NKSA
