SNP33_ARATH
ID SNP33_ARATH Reviewed; 300 AA.
AC Q9S7P9;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=SNAP25 homologous protein SNAP33 {ECO:0000303|PubMed:12746539};
DE Short=AtSNAP33 {ECO:0000303|PubMed:12746539};
DE AltName: Full=Snap25a {ECO:0000303|PubMed:11718726};
DE AltName: Full=Synaptosomal-associated protein SNAP25-like 1 {ECO:0000303|PubMed:11718726};
DE Short=SNAP-25-like protein 1 {ECO:0000303|PubMed:11718726};
GN Name=SNAP33 {ECO:0000303|PubMed:12746539};
GN Synonyms=SNAP33B {ECO:0000303|PubMed:11591731};
GN OrderedLocusNames=At5g61210 {ECO:0000312|Araport:AT5G61210};
GN ORFNames=MAF19.21 {ECO:0000312|EMBL:BAB10383.1};
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], NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND
RP CHARACTERIZATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=11591731; DOI=10.1083/jcb.200107126;
RA Heese M., Gansel X., Sticher L., Wick P., Grebe M., Granier F.,
RA Juergens G.;
RT "Functional characterization of the KNOLLE-interacting t-SNARE AtSNAP33 and
RT its role in plant cytokinesis.";
RL J. Cell Biol. 155:239-249(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 CHARACTERIZATION, AND INTERACTION WITH KNOLLE AND SYP121.
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 INDUCTION.
RX PubMed=12746539; DOI=10.1104/pp.102.012633;
RA Wick P., Gansel X., Oulevey C., Page V., Studer I., Durst M., Sticher L.;
RT "The expression of the t-SNARE AtSNAP33 is induced by pathogens and
RT mechanical stimulation.";
RL Plant Physiol. 132:343-351(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP 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 INTERACTION WITH EXO70B2.
RC STRAIN=cv. Columbia;
RX PubMed=21199889; DOI=10.1093/jxb/erq402;
RA Pecenkova T., Hala M., Kulich I., Kocourkova D., Drdova E., Fendrych M.,
RA Toupalova H., Zarsky V.;
RT "The role for the exocyst complex subunits Exo70B2 and Exo70H1 in the
RT plant-pathogen interaction.";
RL J. Exp. Bot. 62:2107-2116(2011).
CC -!- FUNCTION: t-SNARE involved in diverse vesicle trafficking and membrane
CC fusion processes, including cell plate formation. May function in the
CC secretory pathway.
CC -!- SUBUNIT: Interacts with the cytokinesis-specific syntaxin KNOLLE and
CC with SYP121 (PubMed:11718726). Binds to EXO70B2 (PubMed:21199889).
CC {ECO:0000269|PubMed:11718726, ECO:0000269|PubMed:21199889}.
CC -!- INTERACTION:
CC Q9S7P9; Q9C5X3: KEU; NbExp=5; IntAct=EBI-603017, EBI-603005;
CC Q9S7P9; Q9ZSD4: SYP121; NbExp=4; IntAct=EBI-603017, EBI-4476863;
CC -!- SUBCELLULAR LOCATION: Membrane. Note=Plasma membrane, some endomembrane
CC compartment and cell plate in dividing cells.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with a strong expression in root tips,
CC ovules, very young leaves, vascular tissue, hydathodes, stipules and
CC the abscission and dehiscence zones of the siliques.
CC -!- INDUCTION: Localy and systemically induced by pathogen infection and
CC localy only by mechanical stresses. {ECO:0000269|PubMed:12746539}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; X92420; CAB52583.1; -; mRNA.
DR EMBL; X92419; CAB52582.1; -; mRNA.
DR EMBL; Y13198; CAC79615.1; -; Genomic_DNA.
DR EMBL; AB006696; BAB10383.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97436.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70496.1; -; Genomic_DNA.
DR EMBL; AY057627; AAL15258.1; -; mRNA.
DR EMBL; AY141994; AAM98258.1; -; mRNA.
DR EMBL; AY085322; AAM62553.1; -; mRNA.
DR RefSeq; NP_001332102.1; NM_001345457.1.
DR RefSeq; NP_200929.1; NM_125514.5.
DR AlphaFoldDB; Q9S7P9; -.
DR SMR; Q9S7P9; -.
DR BioGRID; 21486; 6.
DR DIP; DIP-33365N; -.
DR IntAct; Q9S7P9; 4.
DR STRING; 3702.AT5G61210.1; -.
DR iPTMnet; Q9S7P9; -.
DR PaxDb; Q9S7P9; -.
DR PRIDE; Q9S7P9; -.
DR ProteomicsDB; 245323; -.
DR EnsemblPlants; AT5G61210.1; AT5G61210.1; AT5G61210.
DR EnsemblPlants; AT5G61210.2; AT5G61210.2; AT5G61210.
DR GeneID; 836242; -.
DR Gramene; AT5G61210.1; AT5G61210.1; AT5G61210.
DR Gramene; AT5G61210.2; AT5G61210.2; AT5G61210.
DR KEGG; ath:AT5G61210; -.
DR Araport; AT5G61210; -.
DR TAIR; locus:2159426; AT5G61210.
DR eggNOG; KOG3065; Eukaryota.
DR HOGENOM; CLU_061058_0_0_1; -.
DR InParanoid; Q9S7P9; -.
DR OMA; NYAVHKA; -.
DR OrthoDB; 1197028at2759; -.
DR PhylomeDB; Q9S7P9; -.
DR PRO; PR:Q9S7P9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9S7P9; baseline and differential.
DR Genevisible; Q9S7P9; AT.
DR GO; GO:0009504; C:cell plate; IDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IEA:InterPro.
DR GO; GO:0005484; F:SNAP receptor activity; ISS:TAIR.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0061025; P:membrane fusion; TAS:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR GO; GO:0051707; P:response to other organism; IEP:TAIR.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:TAIR.
DR CDD; cd15861; SNARE_SNAP25N_23N_29N_SEC9N; 1.
DR InterPro; IPR044766; NPSN/SNAP25-like_N_SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..300
FT /note="SNAP25 homologous protein SNAP33"
FT /id="PRO_0000213604"
FT DOMAIN 235..297
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 300 AA; 33644 MW; 685A0484608C6DE7 CRC64;
MFGLRKSPAN LPKHNSVDLK SSKPNPFDSD DESDNKHTLN PSKRTTSEPS LADMTNPFGG
ERVQKGDSSS SKQSLFSNSK YQYKNNFRDS GGIENQSVQE LEGYAVYKAE ETTKSVQGCL
KVAEDIRSDA TRTLVMLHDQ GEQITRTHHK AVEIDHDLSR GEKLLGSLGG MFSKTWKPKK
TRPINGPVVT RDDSPTRRVN HLEKREKLGL NSAPRGQSRT REPLPESADA YQRVEMEKAK
QDDGLSDLSD ILGELKNMAV DMGSEIEKQN KGLDHLHDDV DELNFRVQQS NQRGRRLLGK
