SYP32_ARATH
ID SYP32_ARATH Reviewed; 347 AA.
AC Q9LK09;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Syntaxin-32;
DE Short=AtSYP32;
GN Name=SYP32; OrderedLocusNames=At3g24350; ORFNames=K7M2.13;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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).
CC -!- FUNCTION: Vesicle trafficking protein that functions in the secretory
CC pathway. {ECO:0000250}.
CC -!- SUBUNIT: Part of the t-SNARE complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
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=Q9LK09-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AP000382; BAB02935.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76892.1; -; Genomic_DNA.
DR EMBL; BT004300; AAO42298.1; -; mRNA.
DR EMBL; BT008604; AAP40429.1; -; mRNA.
DR RefSeq; NP_189078.2; NM_113342.4. [Q9LK09-1]
DR AlphaFoldDB; Q9LK09; -.
DR BioGRID; 7356; 76.
DR IntAct; Q9LK09; 76.
DR STRING; 3702.AT3G24350.2; -.
DR iPTMnet; Q9LK09; -.
DR PaxDb; Q9LK09; -.
DR ProteomicsDB; 228468; -. [Q9LK09-1]
DR EnsemblPlants; AT3G24350.1; AT3G24350.1; AT3G24350. [Q9LK09-1]
DR GeneID; 822024; -.
DR Gramene; AT3G24350.1; AT3G24350.1; AT3G24350. [Q9LK09-1]
DR KEGG; ath:AT3G24350; -.
DR Araport; AT3G24350; -.
DR eggNOG; KOG0812; Eukaryota.
DR HOGENOM; CLU_044998_0_0_1; -.
DR InParanoid; Q9LK09; -.
DR OMA; RGITGTM; -.
DR PhylomeDB; Q9LK09; -.
DR PRO; PR:Q9LK09; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK09; baseline and differential.
DR Genevisible; Q9LK09; AT.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; 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:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..347
FT /note="Syntaxin-32"
FT /id="PRO_0000210257"
FT TOPO_DOM 1..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 255..317
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 172..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39119 MW; 1DF52CC9ED9CD6C0 CRC64;
MSARHGQSSY RDRSDEFFKI VETLRRSIAP APAANNVPYG NNRNDGARRE DLINKSEFNK
RASHIGLAIN QTSQKLSKLA KLAKRTSVFD DPTQEIQELT VVIKQEISAL NSALVDLQLF
RSSQNDEGNN SRDRDKSTHS ATVVDDLKYR LMDTTKEFKD VLTMRTENMK VHESRRQLFS
SNASKESTNP FVRQRPLAAK AAASESVPLP WANGSSSSSS QLVPWKPGEG ESSPLLQQSQ
QQQQQQQQQM VPLQDTYMQG RAEALHTVES TIHELSSIFT QLATMVSQQG EIAIRIDQNM
EDTLANVEGA QSQLARYLNS ISSNRWLMMK IFFVLIAFLM IFLFFVA
