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Entry version 205 (12 Aug 2020)
Sequence version 3 (02 May 2006)
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Protein

Synaptotagmin-1

Gene

Syt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium sensor that participates in triggering neurotransmitter release at the synapse (PubMed:30107533). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca2+-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca2+-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes.By similarity1 Publication
(Microbial infection) Receptor for C.botulinum neurotoxin type B (BoNT/B, botB); interaction is improved in the presence of gangliosides (PubMed:8144634, PubMed:14504267, PubMed:17167418). BoNT/B toxin binds to the membrane proximal vesicular domain of Syt1 (residues 32-51) (PubMed:14504267, PubMed:17167421).4 Publications
(Microbial infection) Receptor for C.botulinum neurotoxin type G (BoNT/G, botG); unlike the case with BoNT/B, interaction is not improved in the presence of gangliosides (PubMed:15123599, PubMed:20219474). BoNT/G toxin binds to the vesicular domain of Syt1 (residues 32-53) (PubMed:15123599, PubMed:20219474).2 Publications

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+PROSITE-ProRule annotation2 PublicationsNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domains.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi171Calcium 2; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi172Calcium 1PROSITE-ProRule annotation1
Metal bindingi172Calcium 2PROSITE-ProRule annotation1
Metal bindingi178Calcium 1PROSITE-ProRule annotation1
Metal bindingi230Calcium 1PROSITE-ProRule annotation1
Metal bindingi230Calcium 2PROSITE-ProRule annotation1
Metal bindingi231Calcium 1; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi232Calcium 1PROSITE-ProRule annotation1
Metal bindingi232Calcium 2PROSITE-ProRule annotation1
Metal bindingi232Calcium 3PROSITE-ProRule annotation1
Metal bindingi235Calcium 3PROSITE-ProRule annotation1
Metal bindingi236Calcium 3; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi238Calcium 2PROSITE-ProRule annotation1
Metal bindingi238Calcium 3PROSITE-ProRule annotation1
Metal bindingi303Calcium 4PROSITE-ProRule annotation1
Metal bindingi303Calcium 5PROSITE-ProRule annotation1
Metal bindingi309Calcium 4PROSITE-ProRule annotation1
Metal bindingi363Calcium 4PROSITE-ProRule annotation1
Metal bindingi363Calcium 5PROSITE-ProRule annotation1
Metal bindingi365Calcium 4PROSITE-ProRule annotation1
Metal bindingi365Calcium 5PROSITE-ProRule annotation1
Metal bindingi371Calcium 5PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processDifferentiation
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-181429, Serotonin Neurotransmitter Release Cycle
R-RNO-181430, Norepinephrine Neurotransmitter Release Cycle
R-RNO-210500, Glutamate Neurotransmitter Release Cycle
R-RNO-212676, Dopamine Neurotransmitter Release Cycle
R-RNO-264642, Acetylcholine Neurotransmitter Release Cycle
R-RNO-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-888590, GABA synthesis, release, reuptake and degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name:
SytI
p65
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Syt1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

Organism-specific databases

Rat genome database

More...
RGDi
3803, Syt1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 57VesicularSequence analysisAdd BLAST57
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei58 – 79HelicalSequence analysisAdd BLAST22
Topological domaini80 – 421CytoplasmicSequence analysisAdd BLAST342

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi47 – 50MNEL → FNEI: Greatly increased binding of fragment 1-53 to C.botulinum type B (BoNT/B, botB) heavy chain; increases its resemblance to Syt2. 1 Publication4
Mutagenesisi47M → F: Slightly increased binding of fragment 1-53 to BoNT/B heavy chain. 1 Publication1
Mutagenesisi50 – 51LH → IN: Binds to BoNT/B in the absence of gangliosides. 1 Publication2
Mutagenesisi50L → I: Increased binding of fragment 1-53 to BoNT/B heavy chain. 1 Publication1
Mutagenesisi233R → Q: Impaired Ca(2+)-affinity. 1 Publication1
Mutagenesisi302M → K: Fails to localize at nerve terminals. 1 Publication1
Mutagenesisi303D → G: Fails to relocalize to nerve terminals after stimulation of neurotransmitter release. 1 Publication1
Mutagenesisi365D → E: Fails to relocalize to nerve terminals after stimulation of neurotransmitter release. 1 Publication1
Mutagenesisi367I → T: Slows synaptic vesicle fusion kinetics and exocytosis. Impairs the kinetics of synaptic vesicle endocytosis. 2 Publications1
Mutagenesisi370N → K: Slows synaptic vesicle fusion kinetics and exocytosis. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001839401 – 421Synaptotagmin-1Add BLAST421

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi24N-linked (GlcNAc...) asparagine1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi74S-palmitoyl cysteine1 Publication1
Lipidationi75S-palmitoyl cysteine1 Publication1
Lipidationi77S-palmitoyl cysteine1 Publication1
Lipidationi79S-palmitoyl cysteine1 Publication1
Lipidationi82S-palmitoyl cysteine1 Publication1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei128PhosphothreonineCombined sources1
Modified residuei229PhosphotyrosineBy similarity1
Modified residuei264PhosphoserineBy similarity1
Modified residuei342PhosphoserineCombined sources1
Modified residuei344PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P21707

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P21707

PRoteomics IDEntifications database

More...
PRIDEi
P21707

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P21707, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P21707

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P21707

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P21707

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the brain (at protein level) (PubMed:17190793). Predominantly expressed in rostral, phylogenetically younger brain regions, and in some endocrine tissues.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000006426, Expressed in frontal cortex and 20 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P21707, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (Probable).

Interacts with SCAMP5 (By similarity).

Interacts with STON2 (By similarity).

Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity).

Interacts with SV2A, SV2B and SV2C (PubMed:8910372, PubMed:15866046).

Interacts with RIMS1 (PubMed:11438518).

Interacts with PRRT2 (By similarity).

Interacts with DNAJC5 in a phosphorylation-dependent manner (PubMed:11931641).

Interacts (via N-terminus) with RAB3A (PubMed:28057568).

Interacts with SYT12 (PubMed:17190793).

Interacts with calmodulin (By similarity).

By similarityCurated6 Publications

(Microbial infection) Interacts with C.botulinum neurotoxin type B (BoNT/B, botB). Has lower affinity for BoNT/B than Syt2; mutating its residues to match those in Syt2 increases its affinity (PubMed:17167421, PubMed:17167418).

5 Publications

(Microbial infection) Interacts with C.botulinum neurotoxin type G (BoNT/G, botG).

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
247745, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P21707

Database of interacting proteins

More...
DIPi
DIP-29064N

Protein interaction database and analysis system

More...
IntActi
P21707, 24 interactors

Molecular INTeraction database

More...
MINTi
P21707

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000049624

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1421
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P21707

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21707

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini141 – 260C2 1PROSITE-ProRule annotationAdd BLAST120
Domaini272 – 405C2 2PROSITE-ProRule annotationAdd BLAST134

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni135 – 381Phospholipid bindingCuratedAdd BLAST247

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi80 – 119Lys-richAdd BLAST40

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.2 Publications
The second C2 domain mediates interaction with SV2A and probably with STN2.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the synaptotagmin family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1028, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155394

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21707

KEGG Orthology (KO)

More...
KOi
K15290

Identification of Orthologs from Complete Genome Data

More...
OMAi
AQWHTLT

Database of Orthologous Groups

More...
OrthoDBi
925064at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P21707

TreeFam database of animal gene trees

More...
TreeFami
TF315600

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.150, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR001565, Synaptotagmin
IPR015428, Synaptotagmin1

The PANTHER Classification System

More...
PANTHERi
PTHR10024:SF239, PTHR10024:SF239, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00168, C2, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00360, C2DOMAIN
PR00399, SYNAPTOTAGMN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00239, C2, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50004, C2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P21707-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVSASHPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL
60 70 80 90 100
HKIPLPPWAL IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA
110 120 130 140 150
INMKDVKDLG KTMKDQALKD DDAETGLTDG EEKEEPKEEE KLGKLQYSLD
160 170 180 190 200
YDFQNNQLLV GIIQAAELPA LDMGGTSDPY VKVFLLPDKK KKFETKVHRK
210 220 230 240 250
TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII GEFKVPMNTV
260 270 280 290 300
DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK
310 320 330 340 350
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE
360 370 380 390 400
QIQKVQVVVT VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP
410 420
IAQWHTLQVE EEVDAMLAVK K
Length:421
Mass (Da):47,399
Last modified:May 2, 2006 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i06CE28F04C97A722
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti188D → E in CAA36981 (PubMed:2333096).Curated1
Sequence conflicti374G → D in CAA36981 (PubMed:2333096).Curated1
Sequence conflicti393M → I in CAA36981 (PubMed:2333096).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X52772 mRNA Translation: CAA36981.1
AJ617615 mRNA Translation: CAE85101.1
DQ181550 mRNA Translation: ABA00482.1

Protein sequence database of the Protein Information Resource

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PIRi
S09595

NCBI Reference Sequences

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RefSeqi
NP_001028852.2, NM_001033680.2
XP_017450168.1, XM_017594679.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000048880; ENSRNOP00000049624; ENSRNOG00000006426
ENSRNOT00000088950; ENSRNOP00000069194; ENSRNOG00000006426

Database of genes from NCBI RefSeq genomes

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GeneIDi
25716

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25716

UCSC genome browser

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UCSCi
RGD:3803, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52772 mRNA Translation: CAA36981.1
AJ617615 mRNA Translation: CAE85101.1
DQ181550 mRNA Translation: ABA00482.1
PIRiS09595
RefSeqiNP_001028852.2, NM_001033680.2
XP_017450168.1, XM_017594679.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BYNNMR-A140-267[»]
1K5WNMR-A270-421[»]
1RSYX-ray1.90A132-266[»]
1TJMX-ray1.18A271-421[»]
1TJXX-ray1.04A271-421[»]
1UOVX-ray1.65A271-421[»]
1UOWX-ray1.04A271-421[»]
2YOAX-ray1.50A/B271-421[»]
4WEEX-ray0.89A140-266[»]
5CCGX-ray3.50E/F/K141-421[»]
5CCHX-ray3.60E/F141-421[»]
5CCIX-ray4.10E/F141-421[»]
5CCJX-ray1.65A/B/C/D271-421[»]
5KJ7X-ray3.50E/F/K141-419[»]
5KJ8X-ray4.10E/F/K141-419[»]
5W5CX-ray1.85F140-421[»]
5W5DX-ray2.50F270-421[»]
6CXWX-ray1.83A140-182[»]
A201-265[»]
6MTIelectron microscopy10.401/6141-267[»]
2/3/4/5141-421[»]
SMRiP21707
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi247745, 2 interactors
CORUMiP21707
DIPiDIP-29064N
IntActiP21707, 24 interactors
MINTiP21707
STRINGi10116.ENSRNOP00000049624

PTM databases

GlyGeniP21707, 1 site
iPTMnetiP21707
PhosphoSitePlusiP21707
SwissPalmiP21707

Proteomic databases

jPOSTiP21707
PaxDbiP21707
PRIDEiP21707

Genome annotation databases

EnsembliENSRNOT00000048880; ENSRNOP00000049624; ENSRNOG00000006426
ENSRNOT00000088950; ENSRNOP00000069194; ENSRNOG00000006426
GeneIDi25716
KEGGirno:25716
UCSCiRGD:3803, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6857
RGDi3803, Syt1

Phylogenomic databases

eggNOGiKOG1028, Eukaryota
GeneTreeiENSGT00940000155394
InParanoidiP21707
KOiK15290
OMAiAQWHTLT
OrthoDBi925064at2759
PhylomeDBiP21707
TreeFamiTF315600

Enzyme and pathway databases

ReactomeiR-RNO-181429, Serotonin Neurotransmitter Release Cycle
R-RNO-181430, Norepinephrine Neurotransmitter Release Cycle
R-RNO-210500, Glutamate Neurotransmitter Release Cycle
R-RNO-212676, Dopamine Neurotransmitter Release Cycle
R-RNO-264642, Acetylcholine Neurotransmitter Release Cycle
R-RNO-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-888590, GABA synthesis, release, reuptake and degradation

Miscellaneous databases

EvolutionaryTraceiP21707

Protein Ontology

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PROi
PR:P21707

Gene expression databases

BgeeiENSRNOG00000006426, Expressed in frontal cortex and 20 other tissues
GenevisibleiP21707, RN

Family and domain databases

Gene3Di2.60.40.150, 2 hits
InterProiView protein in InterPro
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR001565, Synaptotagmin
IPR015428, Synaptotagmin1
PANTHERiPTHR10024:SF239, PTHR10024:SF239, 1 hit
PfamiView protein in Pfam
PF00168, C2, 2 hits
PRINTSiPR00360, C2DOMAIN
PR00399, SYNAPTOTAGMN
SMARTiView protein in SMART
SM00239, C2, 2 hits
PROSITEiView protein in PROSITE
PS50004, C2, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYT1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21707
Secondary accession number(s): Q3S2E6, Q707P5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 2, 2006
Last modified: August 12, 2020
This is version 205 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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