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Protein

Synaptotagmin-2

Gene

Syt2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits calcium-dependent phospholipid and inositol polyphosphate binding properties. May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. Plays a role in dendrite formation by melanocytes.By similarity

Cofactori

Ca2+1 PublicationNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domains.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi173 – 1731Calcium 1By similarity
Metal bindingi173 – 1731Calcium 2By similarity
Metal bindingi179 – 1791Calcium 1By similarity
Metal bindingi231 – 2311Calcium 1By similarity
Metal bindingi231 – 2311Calcium 2By similarity
Metal bindingi232 – 2321Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi233 – 2331Calcium 1By similarity
Metal bindingi233 – 2331Calcium 2By similarity
Metal bindingi233 – 2331Calcium 3By similarity
Metal bindingi236 – 2361Calcium 3By similarity
Metal bindingi237 – 2371Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi239 – 2391Calcium 2By similarity
Metal bindingi239 – 2391Calcium 3By similarity

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: BHF-UCL
  • calcium ion binding Source: RGD
  • inositol 1,3,4,5 tetrakisphosphate binding Source: UniProtKB
  • syntaxin binding Source: BHF-UCL

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • synaptic vesicle exocytosis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-2Curated
Alternative name(s):
Synaptotagmin II1 PublicationImported
Short name:
SytII1 Publication
Gene namesi
Name:Syt2Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3804. Syt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6060VesicularSequence analysisAdd
BLAST
Transmembranei61 – 8727HelicalSequence analysisAdd
BLAST
Topological domaini88 – 422335CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • chromaffin granule membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • synaptic vesicle membrane Source: RGD
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Synaptotagmin-2PRO_0000183944Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence analysis
Modified residuei125 – 1251PhosphothreonineCombined sources
Modified residuei128 – 1281PhosphothreonineCombined sources
Modified residuei230 – 2301PhosphotyrosineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP29101.
PRIDEiP29101.

PTM databases

iPTMnetiP29101.
PhosphoSiteiP29101.

Expressioni

Tissue specificityi

Predominantly expressed in brain regions such as the spinal cord, brain stem and cerebellum (PubMed:1856191).1 Publication

Interactioni

Subunit structurei

Homotetramer (Probable). Interacts with SCAMP5 (By similarity). Interacts with STON2 (By similarity).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
botBP108443EBI-458017,EBI-7661991From a different organism.
WNK1Q9H4A32EBI-458017,EBI-457907From a different organism.
Wnk1Q9JIH79EBI-458017,EBI-457953

GO - Molecular functioni

  • syntaxin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi246928. 1 interaction.
DIPiDIP-32642N.
IntActiP29101. 5 interactions.
MINTiMINT-1795534.
STRINGi10116.ENSRNOP00000006637.

Structurei

Secondary structure

1
422
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 5913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NM1X-ray2.15B44-60[»]
4ISRX-ray2.59D/E/F40-60[»]
ProteinModelPortaliP29101.
SMRiP29101. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29101.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini156 – 24590C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 37892C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni136 – 382247Phospholipid bindingCuratedAdd
BLAST

Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.By similarity
The second C2 domain mediates interaction with Stonin 2. The second C2 domain mediates phospholipid and inositol polyphosphate binding in a calcium-independent manner.By similarity

Sequence similaritiesi

Belongs to the synaptotagmin family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG4111B9R. LUCA.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP29101.
KOiK19902.
PhylomeDBiP29101.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR030543. Syt2.
[Graphical view]
PANTHERiPTHR10024:SF223. PTHR10024:SF223. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNIFKRNQE PIVAPATTTA TMPLAPAAPA DNSTESTGTG ESQEDMFAKL
60 70 80 90 100
KDKFFNEINK IPLPPWALIA MAVVAGLLLL TCCFCICKKC CCKKKKNKKE
110 120 130 140 150
KGKGMKNAMN MKDMKGGQDD DDAETGLTEG EGEGEEEKEP ENLGKLQFSL
160 170 180 190 200
DYDFQANQLT VGVLQAAELP ALDMGGTSDP YVKVFLLPDK KKKYETKVHR
210 220 230 240 250
KTLNPAFNET FTFKVPYQEL GGKTLVMAIY DFDRFSKHDI IGEVKVPMNT
260 270 280 290 300
VDLGQPIEEW RDLQGGEKEE PEKLGDICTS LRYVPTAGKL TVCILEAKNL
310 320 330 340 350
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT VKKKTLNPYF NESFSFEIPF
360 370 380 390 400
EQIQKVQVVV TVLDYDKLGK NEAIGKIFVG SNATGTELRH WSDMLANPRR
410 420
PIAQWHSLKP EEEVDALLGK NK
Length:422
Mass (Da):47,210
Last modified:December 1, 1992 - v1
Checksum:iD852AF5387E0C7FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64488 mRNA. Translation: AAA63502.1.
PIRiA39454. BMRT2Y.
RefSeqiNP_036797.1. NM_012665.1.
UniGeneiRn.88574.

Genome annotation databases

GeneIDi24805.
KEGGirno:24805.
UCSCiRGD:3804. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64488 mRNA. Translation: AAA63502.1.
PIRiA39454. BMRT2Y.
RefSeqiNP_036797.1. NM_012665.1.
UniGeneiRn.88574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NM1X-ray2.15B44-60[»]
4ISRX-ray2.59D/E/F40-60[»]
ProteinModelPortaliP29101.
SMRiP29101. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246928. 1 interaction.
DIPiDIP-32642N.
IntActiP29101. 5 interactions.
MINTiMINT-1795534.
STRINGi10116.ENSRNOP00000006637.

PTM databases

iPTMnetiP29101.
PhosphoSiteiP29101.

Proteomic databases

PaxDbiP29101.
PRIDEiP29101.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24805.
KEGGirno:24805.
UCSCiRGD:3804. rat.

Organism-specific databases

CTDi127833.
RGDi3804. Syt2.

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG4111B9R. LUCA.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP29101.
KOiK19902.
PhylomeDBiP29101.

Miscellaneous databases

EvolutionaryTraceiP29101.
NextBioi604476.
PROiP29101.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR030543. Syt2.
[Graphical view]
PANTHERiPTHR10024:SF223. PTHR10024:SF223. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Synaptotagmin II. A novel differentially distributed form of synaptotagmin."
    Geppert M., Archer B.T. III, Suedhof T.C.
    J. Biol. Chem. 266:13548-13552(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Synaptotagmins form a hierarchy of exocytotic Ca(2+) sensors with distinct Ca(2+) affinities."
    Sugita S., Shin O.H., Han W., Lao Y., Suedhof T.C.
    EMBO J. 21:270-280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125 AND THR-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYT2_RAT
AccessioniPrimary (citable) accession number: P29101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.