Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00178
Entry Name
UniProt Accession
Theoretical PI
7.18
Molecular Weight
61744.03
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Synaptotagmin-1
Protein Synonyms/Alias
NTMC2T1.1; Synaptotagmin A;
Gene Name
SYT1
Gene Synonyms/Alias
SYTA; At2g20990; F26H11.25; F5H14.5;
Created Date
03-OCT-2012
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
11
Canonical
FSTILGFCGFGVGIS
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
Plays an important role in maintaining plasma membrane integrity during freezing and osmotic stresses. May function in membrane resealing during calcium-dependent freezing tolerance. May regulate endocytosis and endosome recycling at the plasma membrane and cell-to-cell trafficking of cabbage leaf curl virus (CaLCuV) and tobacco mosaic virus (TMV) movement proteins via plasmodesmata.
Sequence Annotation
Topological domain: 1 11 Extracellular.
Transmembrane: 12 32 Helical.
Topological domain: 33 541 Cytoplasmic.
Domain: 247 346 C2 1.
Domain: 407 505 C2 2.
Region: 227 509 Phospholipid binding.
Metal binding site: 276 276 Calcium.
Metal binding site: 282 282 Calcium.
Metal binding site: 332 332 Calcium.
Metal binding site: 334 334 Calcium.
Protein Length
541 AA.
Protein Sequence
(Canonical)
MGFFSTILGF CGFGVGISLG LVIGYVLFVY LLPNDVKDPE IRSIADQDPK AMLRMLPEIP  60
LWVKNPDFDR VDWINRFLEY MWPYLDKAIC KTAKNIAKPI IEEQIPKYKI DSVEFETLTL  120
GSLPPTFQGM KVYLTDEKEL IMEPCLKWAA NPNILVAIKA FGLKATVQVV DLQVFAQPRI  180
TLKPLVPSFP CFANIYVSLM EKPHVDFGLK LGGADLMSIP GLYRFVQEQI KDQVANMYLW  240
PKTLVVPILD PAKAFRRPVG IVHVKVVRAV GLRKKDLMGG ADPFVKIKLS EDKIPSKKTT  300
VKHKNLNPEW NEEFKFSVRD PQTQVLEFSV YDWEQVGNPE KMGMNVLALK EMVPDEHKAF  360
TLELRKTLDG GEDGQPPDKY RGKLEVELLY KPFTEEEMPK GFEETQAVQK APEGTPAAGG  420
MLVVIVHSAE DVEGKHHTNP YVRIYFKGEE RKTKHVKKNR DPRWNEEFTF MLEEPPVREK  480
LHVEVLSTSS RIGLLHPKET LGYVDIPVVD VVNNKRMNQK FHLIDSKNGK IQIELEWRTA  540
S                                                                  541
FASTA
(Canonical)
>LipidDB-3702-00178|Q9SKR2
MGFFSTILGFCGFGVGISLGLVIGYVLFVYLLPNDVKDPEIRSIADQDPKAMLRMLPEIP
LWVKNPDFDRVDWINRFLEYMWPYLDKAICKTAKNIAKPIIEEQIPKYKIDSVEFETLTL
GSLPPTFQGMKVYLTDEKELIMEPCLKWAANPNILVAIKAFGLKATVQVVDLQVFAQPRI
TLKPLVPSFPCFANIYVSLMEKPHVDFGLKLGGADLMSIPGLYRFVQEQIKDQVANMYLW
PKTLVVPILDPAKAFRRPVGIVHVKVVRAVGLRKKDLMGGADPFVKIKLSEDKIPSKKTT
VKHKNLNPEWNEEFKFSVRDPQTQVLEFSVYDWEQVGNPEKMGMNVLALKEMVPDEHKAF
TLELRKTLDGGEDGQPPDKYRGKLEVELLYKPFTEEEMPKGFEETQAVQKAPEGTPAAGG
MLVVIVHSAEDVEGKHHTNPYVRIYFKGEERKTKHVKKNRDPRWNEEFTFMLEEPPVREK
LHVEVLSTSSRIGLLHPKETLGYVDIPVVDVVNNKRMNQKFHLIDSKNGKIQIELEWRTA
S
Gene Ontology
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0008289; F:lipid binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0006897; P:endocytosis; IEA:UniProtKB-KW
GO:0016032; P:viral process; IEA:UniProtKB-KW
Interpro
InterPro; IPR000008; C2_dom
Pfam
Pfam; PF00168; C2;
SMART
SMART; SM00239; C2;
PROSITE
PROSITE; PS50004; C2;
PRINTS
PRINTS; PR00360; C2DOMAIN;