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Protein

Synaptotagmin-3

Gene

Syt3

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

Functioni

Ca2+ sensor involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain. Ca2+ induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (PubMed:11823420, PubMed:18508778). Plays a role in dendrite formation by melanocytes (By similarity).By similarity2 Publications

Cofactori

Ca2+2 PublicationsNote: Binds 3 Ca2+ ions per subunit. The ions are bound to the C2 domains.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi328 – 3281Calcium 1Combined sources1 Publication
Metal bindingi328 – 3281Calcium 2Combined sources1 Publication
Metal bindingi334 – 3341Calcium 1Combined sources1 Publication
Metal bindingi386 – 3861Calcium 1Combined sources1 Publication
Metal bindingi386 – 3861Calcium 2Combined sources1 Publication
Metal bindingi387 – 3871Calcium 1; via carbonyl oxygenCombined sources1 Publication
Metal bindingi388 – 3881Calcium 1Combined sources1 Publication
Metal bindingi388 – 3881Calcium 2Combined sources1 Publication
Metal bindingi388 – 3881Calcium 3Combined sources1 Publication
Metal bindingi391 – 3911Calcium 3Combined sources1 Publication
Metal bindingi394 – 3941Calcium 2Combined sources1 Publication
Metal bindingi394 – 3941Calcium 3Combined sources1 Publication

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: RGD
  • calcium ion binding Source: RGD
  • clathrin binding Source: BHF-UCL
  • phosphatidylinositol-4,5-bisphosphate binding Source: ParkinsonsUK-UCL
  • phosphatidylserine binding Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: RGD

GO - Biological processi

  • calcium ion regulated exocytosis Source: RGD
  • calcium ion-regulated exocytosis of neurotransmitter Source: GO_Central
  • cell differentiation Source: UniProtKB-KW
  • positive regulation of vesicle fusion Source: RGD
  • regulation of calcium ion-dependent exocytosis Source: ParkinsonsUK-UCL
  • response to calcium ion Source: RGD
  • synaptic vesicle exocytosis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-3
Alternative name(s):
Synaptotagmin III
Short name:
SytIII
Gene namesi
Name:Syt3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3805. Syt3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5454VesicularSequence analysisAdd
BLAST
Transmembranei55 – 7521HelicalSequence analysisAdd
BLAST
Topological domaini76 – 588513CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi334 – 3341D → N: Abolishes Ca(2+)-dependent phospholipid-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 588588Synaptotagmin-3PRO_0000183947Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP40748.
PRIDEiP40748.

PTM databases

iPTMnetiP40748.
PhosphoSiteiP40748.

Expressioni

Tissue specificityi

Brain, various endocrine tissues and hormone-secreting clonal cells.1 Publication

Gene expression databases

BgeeiENSRNOG00000019318.

Interactioni

Subunit structurei

Homodimer; disulfide-linked via the cysteine motif. Can also form heterodimers with SYT6, SYT9 and SYT10.By similarity

GO - Molecular functioni

  • clathrin binding Source: BHF-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: RGD

Protein-protein interaction databases

BioGridi247760. 1 interaction.
IntActiP40748. 2 interactions.
STRINGi10116.ENSRNOP00000026251.

Structurei

Secondary structure

1
588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi300 – 3067Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi313 – 32210Combined sources
Beta strandi335 – 3406Combined sources
Beta strandi344 – 3507Combined sources
Beta strandi361 – 3699Combined sources
Helixi372 – 3754Combined sources
Beta strandi381 – 3866Combined sources
Beta strandi389 – 3913Combined sources
Beta strandi395 – 4006Combined sources
Helixi406 – 4083Combined sources
Beta strandi412 – 4143Combined sources
Beta strandi416 – 4194Combined sources
Beta strandi432 – 4409Combined sources
Turni441 – 4444Combined sources
Beta strandi445 – 45511Combined sources
Beta strandi460 – 4634Combined sources
Beta strandi467 – 4715Combined sources
Beta strandi478 – 4847Combined sources
Beta strandi490 – 4934Combined sources
Beta strandi495 – 4984Combined sources
Beta strandi501 – 5033Combined sources
Helixi507 – 5104Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi523 – 5253Combined sources
Beta strandi528 – 5325Combined sources
Helixi542 – 5498Combined sources
Beta strandi551 – 5577Combined sources
Beta strandi561 – 5644Combined sources
Helixi568 – 5703Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQVX-ray3.20A293-588[»]
3HN8X-ray3.50A/B/C292-587[»]
ProteinModelPortaliP40748.
SMRiP40748. Positions 295-569.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40748.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini299 – 400102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini431 – 534104C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 3425Cysteine motifBy similarityAdd
BLAST

Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.1 Publication
The cysteine motif mediates homo- or heterodimer formation via formation of disulfide bonds.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

eggNOGiENOG410KDMB. Eukaryota.
COG5038. LUCA.
HOGENOMiHOG000232128.
HOVERGENiHBG005010.
InParanoidiP40748.
KOiK19903.
PhylomeDBiP40748.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028682. SYT3.
[Graphical view]
PANTHERiPTHR10024:SF176. PTHR10024:SF176. 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.

P40748-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDYEDDLC RRALILVSDL CARIRDADTN DRCQEFNELR IRGYPRGPDA
60 70 80 90 100
DISVSLLSVI VTFCGIVLLG VSLFVSWKLC WVPWRDKGGS AVGGGPLRKD
110 120 130 140 150
LAPGVGLAGL VGGGGHHLGA SLGGHPLLGG PHHHAHPAHH PPFAELLEPG
160 170 180 190 200
GLGGSEPPEP SYLDMDSYPE AAVASVVAAG VKPSQTSPEL PSEGGTGSGL
210 220 230 240 250
LLLPPSGGGL PSAQSHQQVT SLAPTTRYPA LPRPLTQQTL TTQADPSSEE
260 270 280 290 300
RPPALPLPLP GGEEKAKLIG QIKPELYQGT GPGGRRTGGG SGEAGAPCGR
310 320 330 340 350
ISFALRYLYG SDQLVVRILQ ALDLPAKDSN GFSDPYVKIY LLPDRKKKFQ
360 370 380 390 400
TKVHRKTLNP IFNETFQFSV PLAELAQRKL HFSVYDFDRF SRHDLIGQVV
410 420 430 440 450
LDNLLELAEQ PPDRPLWRDI LEGGSEKADL GELNFSLCYL PTAGLLTVTI
460 470 480 490 500
IKASNLKAMD LTGFSDPYVK ASLISEGRRL KKRKTSIKKN TLNPTYNEAL
510 520 530 540 550
VFDVAPESVE NVGLSIAVVD YDCIGHNEVI GVCRVGPEAA DPHGREHWAE
560 570 580
MLANPRKPVE HWHQLVEEKT LSSFTKGGKG LSEKENSE
Length:588
Mass (Da):63,313
Last modified:February 1, 1995 - v1
Checksum:i9D9D33CF5BAD8331
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871T → S in AAK56959 (Ref. 2) Curated
Sequence conflicti445 – 4451L → R in AAK56959 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28512 mRNA. Translation: BAA05870.1.
AF375464 mRNA. Translation: AAK56959.1.
PIRiA53563.
RefSeqiNP_061995.1. NM_019122.1.
XP_006229040.1. XM_006228978.2.
XP_006229041.1. XM_006228979.2.
XP_008757546.1. XM_008759324.1.
XP_008757547.1. XM_008759325.1.
UniGeneiRn.48884.

Genome annotation databases

GeneIDi25731.
KEGGirno:25731.
UCSCiRGD:3805. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28512 mRNA. Translation: BAA05870.1.
AF375464 mRNA. Translation: AAK56959.1.
PIRiA53563.
RefSeqiNP_061995.1. NM_019122.1.
XP_006229040.1. XM_006228978.2.
XP_006229041.1. XM_006228979.2.
XP_008757546.1. XM_008759324.1.
XP_008757547.1. XM_008759325.1.
UniGeneiRn.48884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQVX-ray3.20A293-588[»]
3HN8X-ray3.50A/B/C292-587[»]
ProteinModelPortaliP40748.
SMRiP40748. Positions 295-569.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247760. 1 interaction.
IntActiP40748. 2 interactions.
STRINGi10116.ENSRNOP00000026251.

PTM databases

iPTMnetiP40748.
PhosphoSiteiP40748.

Proteomic databases

PaxDbiP40748.
PRIDEiP40748.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25731.
KEGGirno:25731.
UCSCiRGD:3805. rat.

Organism-specific databases

CTDi84258.
RGDi3805. Syt3.

Phylogenomic databases

eggNOGiENOG410KDMB. Eukaryota.
COG5038. LUCA.
HOGENOMiHOG000232128.
HOVERGENiHBG005010.
InParanoidiP40748.
KOiK19903.
PhylomeDBiP40748.
TreeFamiTF315600.

Miscellaneous databases

EvolutionaryTraceiP40748.
PROiP40748.

Gene expression databases

BgeeiENSRNOG00000019318.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028682. SYT3.
[Graphical view]
PANTHERiPTHR10024:SF176. PTHR10024:SF176. 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...

Entry informationi

Entry nameiSYT3_RAT
AccessioniPrimary (citable) accession number: P40748
Secondary accession number(s): Q925B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 146 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.