SYP22_ARATH
ID SYP22_ARATH Reviewed; 268 AA.
AC P93654;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 161.
DE RecName: Full=Syntaxin-22;
DE Short=AtSYP22;
DE Short=AtVAM3;
DE AltName: Full=Protein SHOOT GRAVITROPISM 3;
GN Name=SYP22; Synonyms=SGR3, VAM3; OrderedLocusNames=At5g46860;
GN ORFNames=MSD23.9;
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].
RC STRAIN=cv. Columbia;
RX PubMed=9305917; DOI=10.1074/jbc.272.39.24530;
RA Sato M.H., Nakamura N., Ohsumi Y., Kouchi H., Kondo M., Hara-Nishimura I.,
RA Nishimura M., Wada Y.;
RT "The AtVAM3 encodes a syntaxin-related molecule implicated in the vacuolar
RT assembly in Arabidopsis thaliana.";
RL J. Biol. Chem. 272:24530-24535(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8819871; DOI=10.1104/pp.110.3.945;
RA Fukaki H., Fujisawa H., Tasaka M.;
RT "SGR1, SGR2, SGR3: novel genetic loci involved in shoot gravitropism in
RT Arabidopsis thaliana.";
RL Plant Physiol. 110:945-955(1996).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10557242; DOI=10.1104/pp.121.3.929;
RA Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT "The t-SNARE AtVAM3p resides on the prevacuolar compartment in Arabidopsis
RT root cells.";
RL Plant Physiol. 121:929-938(1999).
RN [8]
RP LACK OF INTERACTION WITH VPS45.
RX PubMed=10888666; DOI=10.1091/mbc.11.7.2251;
RA Bassham D.C., Sanderfoot A.A., Kovaleva V., Zheng H., Raikhel N.V.;
RT "AtVPS45 complex formation at the trans-Golgi network.";
RL Mol. Biol. Cell 11:2251-2265(2000).
RN [9]
RP INTERACTION WITH VTI11 AND SYP51.
RX PubMed=11739776; DOI=10.1091/mbc.12.12.3733;
RA Sanderfoot A.A., Kovaleva V., Bassham D.C., Raikhel N.V.;
RT "Interactions between syntaxins identify at least five SNARE complexes
RT within the Golgi/prevacuolar system of the Arabidopsis cell.";
RL Mol. Biol. Cell 12:3733-3743(2001).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=21645145; DOI=10.1111/j.1365-313x.2011.04665.x;
RA Saito C., Uemura T., Awai C., Tominaga M., Ebine K., Ito J., Ueda T.,
RA Abe H., Morita M.T., Tasaka M., Nakano A.;
RT "The occurrence of 'bulbs', a complex configuration of the vacuolar
RT membrane, is affected by mutations of vacuolar SNARE and phospholipase in
RT Arabidopsis.";
RL Plant J. 68:64-73(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE 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).
CC -!- FUNCTION: May provide the t-SNARE function in the vacuolar assembly.
CC Promotes the formation of vacuolar membrane 'bulbs'. Required for
CC inflorescence stem gravitropism. {ECO:0000269|PubMed:21645145,
CC ECO:0000269|PubMed:8819871}.
CC -!- SUBUNIT: Interacts with VTI11 and SYP51 to form a t-SNARE complex, but
CC not with VPS45. {ECO:0000269|PubMed:11739776}.
CC -!- INTERACTION:
CC P93654; Q9SEL6: VTI11; NbExp=3; IntAct=EBI-2352632, EBI-1162795;
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane
CC {ECO:0000269|PubMed:10557242}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:10557242}. Vacuole membrane
CC {ECO:0000269|PubMed:10557242}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:10557242}. Note=Prevacuolar compartment (PVC) in
CC roots, and junction of two vacuolar membranes in shoot apical meristem.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flower and green
CC siliques.
CC -!- DISRUPTION PHENOTYPE: The sgr3-1 mutant has a reduced gravitropic
CC response in inflorescence stem but a normal gravitropic response in
CC hypocotyls. Reduced formation of vacuolar membrane 'bulbs'.
CC {ECO:0000269|PubMed:21645145, ECO:0000269|PubMed:8819871}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U88045; AAC49823.1; -; mRNA.
DR EMBL; AB022221; BAA97220.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95437.1; -; Genomic_DNA.
DR EMBL; AF385695; AAK60288.1; -; mRNA.
DR EMBL; AY072015; AAL57708.1; -; mRNA.
DR EMBL; AY133666; AAM91496.1; -; mRNA.
DR EMBL; AY085121; AAM61675.1; -; mRNA.
DR RefSeq; NP_568671.1; NM_124057.4.
DR AlphaFoldDB; P93654; -.
DR SMR; P93654; -.
DR BioGRID; 19978; 58.
DR IntAct; P93654; 55.
DR STRING; 3702.AT5G46860.1; -.
DR iPTMnet; P93654; -.
DR PaxDb; P93654; -.
DR PRIDE; P93654; -.
DR ProteomicsDB; 228487; -.
DR EnsemblPlants; AT5G46860.1; AT5G46860.1; AT5G46860.
DR GeneID; 834730; -.
DR Gramene; AT5G46860.1; AT5G46860.1; AT5G46860.
DR KEGG; ath:AT5G46860; -.
DR Araport; AT5G46860; -.
DR TAIR; locus:3356150; AT5G46860.
DR eggNOG; KOG0811; Eukaryota.
DR HOGENOM; CLU_059257_3_0_1; -.
DR InParanoid; P93654; -.
DR OMA; HMENGLN; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; P93654; -.
DR PRO; PR:P93654; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P93654; baseline and differential.
DR Genevisible; P93654; 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:0000325; C:plant-type vacuole; IDA:TAIR.
DR GO; GO:0009705; C:plant-type vacuole membrane; IDA:TAIR.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; HDA: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:0009660; P:amyloplast organization; IMP:TAIR.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IGI:TAIR.
DR GO; GO:0009959; P:negative gravitropism; IMP:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
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; PF14523; Syntaxin_2; 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; Coiled coil; Membrane; Protein transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..268
FT /note="Syntaxin-22"
FT /id="PRO_0000210254"
FT TOPO_DOM 2..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 175..237
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 268 AA; 29481 MW; F908E43A42470BEE CRC64;
MSFQDLESGR GRSTRKFNGG RQDSTQAVAS GIFQINTGVS TFQRLVNTLG TPKDTPELRE
KLHKTRLHIG QLVKDTSAKL KEASETDHQS GVNPSKKIAD AKLARDFQAV LKEFQKAQQT
AAERETTYTP FVPQSALPSS YTAGEVDKVP EQRAQLQESK RQELVLLDNE IAFNEAVIEE
REQGIQEIHQ QIGEVNEIFK DLAVLVNDQG VMIDDIGTHI DNSRAATSQG KSQLVQAAKT
QKSNSSLTCL LLVIFGIVLL IVIIVLAA
