GENTAUR Molecular Products.

 SY132_ARATH             Reviewed;         304 AA.
 Q8VZU2; Q9LEZ8;
 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
 01-MAR-2002, sequence version 1.
 07-NOV-2018, entry version 126.
 RecName: Full=Syntaxin-132;
          Short=AtSYP132;
 Name=SYP132; OrderedLocusNames=At5g08080; ORFNames=T22D6.20;
 Arabidopsis thaliana (Mouse-ear cress).
 Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
 Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
 Arabidopsis.
 NCBI_TaxID=3702;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=cv. Columbia;
 PubMed=11130714; DOI=10.1038/35048507;
 Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
 Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
 Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
 Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
 Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
 Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
 Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
 Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
 Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
 Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
 Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
 Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
 Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
 Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
 Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
 Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
 Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
 Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
 Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
 van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
 Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
 Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
 Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
 Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
 "Sequence and analysis of chromosome 5 of the plant Arabidopsis
 thaliana.";
 Nature 408:823-826(2000).
 [2]
 GENOME REANNOTATION.
 STRAIN=cv. Columbia;
 PubMed=27862469; DOI=10.1111/tpj.13415;
 Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
 Town C.D.;
 "Araport11: a complete reannotation of the Arabidopsis thaliana
 reference genome.";
 Plant J. 89:789-804(2017).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=14593172; DOI=10.1126/science.1088305;
 Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
 Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
 Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
 Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
 Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
 Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
 Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
 Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
 Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
 Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
 Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
 Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
 "Empirical analysis of transcriptional activity in the Arabidopsis
 genome.";
 Science 302:842-846(2003).
 [4]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19376835; DOI=10.1104/pp.109.138677;
 Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
 Grossmann J., Gruissem W., Baginsky S.;
 "Large-scale Arabidopsis phosphoproteome profiling reveals novel
 chloroplast kinase substrates and phosphorylation networks.";
 Plant Physiol. 150:889-903(2009).
 -!- FUNCTION: Vesicle trafficking protein that functions in the
     secretory pathway. {ECO:0000250}.
 -!- SUBUNIT: Part of the t-SNARE complex. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV
     membrane protein {ECO:0000250}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=1;
       Comment=A number of isoforms are produced. According to EST
       sequences.;
     Name=1;
       IsoId=Q8VZU2-1; Sequence=Displayed;
 -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=CAB93709.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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 EMBL; AL357612; CAB93709.1; ALT_SEQ; Genomic_DNA.
 EMBL; CP002688; AED91242.1; -; Genomic_DNA.
 EMBL; CP002688; ANM70609.1; -; Genomic_DNA.
 EMBL; AY063836; AAL36192.1; -; mRNA.
 EMBL; AY117244; AAM51319.1; -; mRNA.
 PIR; T50493; T50493.
 RefSeq; NP_001332203.1; NM_001342979.1. [Q8VZU2-1]
 RefSeq; NP_568187.1; NM_120890.3. [Q8VZU2-1]
 UniGene; At.27182; -.
 ProteinModelPortal; Q8VZU2; -.
 SMR; Q8VZU2; -.
 BioGrid; 15980; 53.
 IntAct; Q8VZU2; 53.
 iPTMnet; Q8VZU2; -.
 SwissPalm; Q8VZU2; -.
 PRIDE; Q8VZU2; -.
 EnsemblPlants; AT5G08080.1; AT5G08080.1; AT5G08080. [Q8VZU2-1]
 EnsemblPlants; AT5G08080.4; AT5G08080.4; AT5G08080. [Q8VZU2-1]
 GeneID; 830702; -.
 Gramene; AT5G08080.1; AT5G08080.1; AT5G08080. [Q8VZU2-1]
 Gramene; AT5G08080.4; AT5G08080.4; AT5G08080. [Q8VZU2-1]
 KEGG; ath:AT5G08080; -.
 Araport; AT5G08080; -.
 HOGENOM; HOG000238904; -.
 InParanoid; Q8VZU2; -.
 KO; K08486; -.
 OMA; FEEIDHI; -.
 PhylomeDB; Q8VZU2; -.
 Reactome; R-ATH-449836; Other interleukin signaling.
 PRO; PR:Q8VZU2; -.
 Proteomes; UP000006548; Chromosome 5.
 ExpressionAtlas; Q8VZU2; baseline and differential.
 Genevisible; Q8VZU2; AT.
 GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
 GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
 GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
 GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
 GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
 GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
 GO; GO:0006887; P:exocytosis; IBA:GO_Central.
 GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
 GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
 GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
 CDD; cd00179; SynN; 1.
 InterPro; IPR010989; SNARE.
 InterPro; IPR006012; Syntaxin/epimorphin_CS.
 InterPro; IPR006011; Syntaxin_N.
 InterPro; IPR000727; T_SNARE_dom.
 Pfam; PF05739; SNARE; 1.
 Pfam; PF00804; Syntaxin; 1.
 SMART; SM00503; SynN; 1.
 SMART; SM00397; t_SNARE; 1.
 SUPFAM; SSF47661; SSF47661; 1.
 PROSITE; PS00914; SYNTAXIN; 1.
 PROSITE; PS50192; T_SNARE; 1.
 1: Evidence at protein level;
 Acetylation; Alternative splicing; Coiled coil; Complete proteome;
 Membrane; Protein transport; Reference proteome; Transmembrane;
 Transmembrane helix; Transport.
 CHAIN         1    304       Syntaxin-132.
                              /FTId=PRO_0000210252.
 TOPO_DOM      1    275       Cytoplasmic. {ECO:0000255}.
 TRANSMEM    276    296       Helical; Anchor for type IV membrane
                              protein. {ECO:0000255}.
 TOPO_DOM    297    304       Vesicular. {ECO:0000255}.
 DOMAIN      204    266       t-SNARE coiled-coil homology.
                              {ECO:0000255|PROSITE-ProRule:PRU00202}.
 COILED       34     67       {ECO:0000255}.
 COILED      129    162       {ECO:0000255}.
 MOD_RES       1      1       N-acetylmethionine.
                              {ECO:0000250|UniProtKB:Q9ZSD4}.
 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

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