SYT1_ARATH
ID SYT1_ARATH Reviewed; 541 AA.
AC Q9SKR2; Q94AS0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Synaptotagmin-1;
DE AltName: Full=NTMC2T1.1;
DE AltName: Full=Synaptotagmin A;
GN Name=SYT1; Synonyms=SYTA; OrderedLocusNames=At2g20990;
GN ORFNames=F26H11.25, F5H14.5;
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].
RX PubMed=12801916; DOI=10.1093/jb/mvg082;
RA Fukuda M.;
RT "Molecular cloning, expression, and characterization of a novel class of
RT synaptotagmin (Syt XIV) conserved from Drosophila to humans.";
RL J. Biochem. 133:641-649(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15238157; DOI=10.1186/1471-2164-5-43;
RA Craxton M.A.;
RT "Synaptotagmin gene content of the sequenced genomes.";
RL BMC Genomics 5:43-43(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19088328; DOI=10.1105/tpc.108.201211;
RA Eckardt N.A.;
RT "Arabidopsis synaptotagmin1 maintains plasma membrane integrity.";
RL Plant Cell 20:3182-3182(2008).
RN [7]
RP FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19088329; DOI=10.1105/tpc.108.063859;
RA Schapire A.L., Voigt B., Jasik J., Rosado A., Lopez-Cobollo R., Menzel D.,
RA Salinas J., Mancuso S., Valpuesta V., Baluska F., Botella M.A.;
RT "Arabidopsis synaptotagmin 1 is required for the maintenance of plasma
RT membrane integrity and cell viability.";
RL Plant Cell 20:3374-3388(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19088330; DOI=10.1105/tpc.108.062679;
RA Yamazaki T., Kawamura Y., Minami A., Uemura M.;
RT "Calcium-dependent freezing tolerance in Arabidopsis involves membrane
RT resealing via synaptotagmin SYT1.";
RL Plant Cell 20:3389-3404(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20498364; DOI=10.1074/jbc.m109.084046;
RA Yamazaki T., Takata N., Uemura M., Kawamura Y.;
RT "Arabidopsis synaptotagmin SYT1, a type I signal-anchor protein, requires
RT tandem C2 domains for delivery to the plasma membrane.";
RL J. Biol. Chem. 285:23165-23176(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CABBAGE LEAF CURL
RP VIRUS BC1 AND TOBACCO MOSAIC VIRUS MP.
RX PubMed=20133785; DOI=10.1073/pnas.0909080107;
RA Lewis J.D., Lazarowitz S.G.;
RT "Arabidopsis synaptotagmin SYTA regulates endocytosis and virus movement
RT protein cell-to-cell transport.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2491-2496(2010).
RN [11]
RP INTERACTION WITH ROSY1.
RX PubMed=27044028; DOI=10.1016/j.jplph.2016.03.011;
RA Dalal J., Lewis D.R., Tietz O., Brown E.M., Brown C.S., Palme K.,
RA Muday G.K., Sederoff H.W.;
RT "ROSY1, a novel regulator of gravitropic response is a stigmasterol binding
RT protein.";
RL J. Plant Physiol. 196:28-40(2016).
CC -!- FUNCTION: Plays an important role in maintaining plasma membrane
CC integrity during freezing and osmotic stresses. May function in
CC membrane resealing during calcium-dependent freezing tolerance. May
CC regulate endocytosis and endosome recycling at the plasma membrane and
CC cell-to-cell trafficking of cabbage leaf curl virus (CaLCuV) and
CC tobacco mosaic virus (TMV) movement proteins via plasmodesmata.
CC {ECO:0000269|PubMed:19088328, ECO:0000269|PubMed:19088329,
CC ECO:0000269|PubMed:19088330, ECO:0000269|PubMed:20133785,
CC ECO:0000269|PubMed:20498364}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19088329};
CC -!- SUBUNIT: Interacts with cabbage leaf curl virus (CaLCuV) BC1 protein
CC and tobacco mosaic virus (TMV) MP protein (PubMed:20133785). Interacts
CC with ROSY1 (PubMed:27044028). {ECO:0000269|PubMed:20133785,
CC ECO:0000269|PubMed:27044028}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC {ECO:0000305}; Cytoplasmic side. Endosome membrane; Single-pass
CC membrane protein.
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=Q9SKR2-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, rosette and cauline
CC leaves, inflorescences, and siliques. In roots, expressed in vascular
CC bundle, epidermis, the differential zone of the tips of root hairs, and
CC the quiescent center and columella of root tips.
CC {ECO:0000269|PubMed:19088329, ECO:0000269|PubMed:20498364}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth. {ECO:0000269|PubMed:19088328,
CC ECO:0000269|PubMed:19088329}.
CC -!- MISCELLANEOUS: Phospholipid binding to the first C2 domain is calcium-
CC dependent, but binding to the second C2 domain is calcium-independent.
CC {ECO:0000305|PubMed:19088329}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family. {ECO:0000305}.
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DR EMBL; AB102951; BAC76812.1; -; mRNA.
DR EMBL; AJ617630; CAE85115.1; -; mRNA.
DR EMBL; AC006234; AAM15203.1; -; Genomic_DNA.
DR EMBL; AC006264; AAD29817.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07109.1; -; Genomic_DNA.
DR EMBL; AY045836; AAK76510.1; -; mRNA.
DR EMBL; BT004371; AAO42365.1; -; mRNA.
DR EMBL; AY087925; AAM65475.1; -; mRNA.
DR PIR; G84595; G84595.
DR RefSeq; NP_565495.1; NM_127668.4. [Q9SKR2-1]
DR PDB; 7AS6; X-ray; 2.00 A; A=253-397.
DR PDB; 7ATP; X-ray; 2.10 A; A=253-397.
DR PDBsum; 7AS6; -.
DR PDBsum; 7ATP; -.
DR AlphaFoldDB; Q9SKR2; -.
DR SASBDB; Q9SKR2; -.
DR SMR; Q9SKR2; -.
DR BioGRID; 1986; 6.
DR STRING; 3702.AT2G20990.3; -.
DR SwissPalm; Q9SKR2; -.
DR PRIDE; Q9SKR2; -.
DR EnsemblPlants; AT2G20990.1; AT2G20990.1; AT2G20990. [Q9SKR2-1]
DR GeneID; 816633; -.
DR Gramene; AT2G20990.1; AT2G20990.1; AT2G20990. [Q9SKR2-1]
DR KEGG; ath:AT2G20990; -.
DR Araport; AT2G20990; -.
DR eggNOG; KOG1012; Eukaryota.
DR InParanoid; Q9SKR2; -.
DR PhylomeDB; Q9SKR2; -.
DR PRO; PR:Q9SKR2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKR2; baseline and differential.
DR Genevisible; Q9SKR2; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR045050; Synaptotagmin_plant.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR PANTHER; PTHR10774; PTHR10774; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF17047; SMP_LBD; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS51847; SMP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Endocytosis;
KW Endosome; Host-virus interaction; Lipid transport; Lipid-binding; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..541
FT /note="Synaptotagmin-1"
FT /id="PRO_0000419238"
FT TOPO_DOM 1..11
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:19088330"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19088330"
FT DOMAIN 67..249
FT /note="SMP-LTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01194"
FT DOMAIN 240..362
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 401..521
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 227..509
FT /note="Phospholipid binding"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT STRAND 260..271
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 309..319
FT /evidence="ECO:0007829|PDB:7AS6"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 325..332
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 340..348
FT /evidence="ECO:0007829|PDB:7AS6"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:7AS6"
FT STRAND 383..392
FT /evidence="ECO:0007829|PDB:7AS6"
SQ SEQUENCE 541 AA; 61744 MW; 9988F60FEC0382D8 CRC64;
MGFFSTILGF CGFGVGISLG LVIGYVLFVY LLPNDVKDPE IRSIADQDPK AMLRMLPEIP
LWVKNPDFDR VDWINRFLEY MWPYLDKAIC KTAKNIAKPI IEEQIPKYKI DSVEFETLTL
GSLPPTFQGM KVYLTDEKEL IMEPCLKWAA NPNILVAIKA FGLKATVQVV DLQVFAQPRI
TLKPLVPSFP CFANIYVSLM EKPHVDFGLK LGGADLMSIP GLYRFVQEQI KDQVANMYLW
PKTLVVPILD PAKAFRRPVG IVHVKVVRAV GLRKKDLMGG ADPFVKIKLS EDKIPSKKTT
VKHKNLNPEW NEEFKFSVRD PQTQVLEFSV YDWEQVGNPE KMGMNVLALK EMVPDEHKAF
TLELRKTLDG GEDGQPPDKY RGKLEVELLY KPFTEEEMPK GFEETQAVQK APEGTPAAGG
MLVVIVHSAE DVEGKHHTNP YVRIYFKGEE RKTKHVKKNR DPRWNEEFTF MLEEPPVREK
LHVEVLSTSS RIGLLHPKET LGYVDIPVVD VVNNKRMNQK FHLIDSKNGK IQIELEWRTA
S
