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Protein

Synaptotagmin-4

Gene

Syt4

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

Functioni

May be involved in Ca2+-independent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may serve as Ca2+ sensors in the process of vesicular trafficking and exocytosis (PubMed:7993622). Plays a role in dendrite formation by melanocytes (By similarity).By similarity1 Publication

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi184Calcium 1By similarity1
Metal bindingi184Calcium 2By similarity1
Metal bindingi191Calcium 1By similarity1
Metal bindingi245Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi246Calcium 1By similarity1
Metal bindingi246Calcium 2By similarity1
Metal bindingi246Calcium 3By similarity1
Metal bindingi249Calcium 3By similarity1
Metal bindingi252Calcium 2By similarity1
Metal bindingi252Calcium 3By similarity1

GO - Molecular functioni

  • clathrin binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylserine binding Source: RGD
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: ParkinsonsUK-UCL
  • syntaxin-3 binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • brain development Source: RGD
  • calcium ion regulated exocytosis Source: RGD
  • calcium ion-regulated exocytosis of neurotransmitter Source: GO_Central
  • negative regulation of calcium ion-dependent exocytosis Source: RGD
  • negative regulation of catecholamine secretion Source: ParkinsonsUK-UCL
  • negative regulation of dense core granule exocytosis Source: ParkinsonsUK-UCL
  • negative regulation of neurotransmitter secretion Source: ParkinsonsUK-UCL
  • negative regulation of protein secretion Source: Ensembl
  • negative regulation of synaptic vesicle exocytosis Source: Ensembl
  • negative regulation of vesicle fusion Source: ParkinsonsUK-UCL
  • neurotransmitter secretion Source: RGD
  • positive regulation of dendrite extension Source: Ensembl
  • regulation of endocytosis Source: ParkinsonsUK-UCL
  • regulation of vesicle fusion Source: ParkinsonsUK-UCL
  • secretory granule maturation Source: ParkinsonsUK-UCL
  • vesicle fusion with vesicle Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-4
Alternative name(s):
Synaptotagmin IV
Short name:
SytIV
Gene namesi
Name:Syt4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi68397. Syt4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16VesicularSequence analysisAdd BLAST16
Transmembranei17 – 37HelicalSequence analysisAdd BLAST21
Topological domaini38 – 425CytoplasmicSequence analysisAdd BLAST388

GO - Cellular componenti

  • astrocyte projection Source: ParkinsonsUK-UCL
  • axon Source: Ensembl
  • cell junction Source: UniProtKB-KW
  • dendrite Source: Ensembl
  • dense core granule Source: ParkinsonsUK-UCL
  • exocytic vesicle Source: ParkinsonsUK-UCL
  • Golgi apparatus Source: ParkinsonsUK-UCL
  • integral component of membrane Source: ParkinsonsUK-UCL
  • neuronal cell body Source: ParkinsonsUK-UCL
  • neuron projection Source: ParkinsonsUK-UCL
  • neuron projection terminus Source: ParkinsonsUK-UCL
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: GO_Central
  • secretory granule membrane Source: ParkinsonsUK-UCL
  • synaptic vesicle Source: ParkinsonsUK-UCL
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001839501 – 425Synaptotagmin-4Add BLAST425

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei135PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP50232.
PRIDEiP50232.

PTM databases

iPTMnetiP50232.
PhosphoSitePlusiP50232.

Expressioni

Tissue specificityi

Widely expressed (PubMed:7892240). Expressed in the brain (PubMed:7892240). Expressed in pituitary gland, cerebellum, cortex, hypothalamus and hippocampus (PubMed:7892240).2 Publications

Inductioni

Up-regulated by potassium depolarization, calcium ionophore, ATP and forskolin in culture cells (PubMed:7892240). Up-regulated by kainate in the hippocampus and piriform cortex (PubMed:7892240).1 Publication

Gene expression databases

BgeeiENSRNOG00000017333.
GenevisibleiP50232. RN.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Mapk10P491872EBI-540118,EBI-7155513
Mapk8P491855EBI-540118,EBI-7456505

GO - Molecular functioni

  • clathrin binding Source: BHF-UCL
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • SNARE binding Source: ParkinsonsUK-UCL
  • syntaxin-1 binding Source: ParkinsonsUK-UCL
  • syntaxin-3 binding Source: ParkinsonsUK-UCL
  • syntaxin binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

IntActiP50232. 5 interactors.
STRINGi10116.ENSRNOP00000023593.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi290 – 298Combined sources9
Turni299 – 302Combined sources4
Beta strandi303 – 313Combined sources11
Beta strandi325 – 333Combined sources9
Beta strandi336 – 342Combined sources7
Beta strandi350 – 361Combined sources12
Beta strandi364 – 367Combined sources4
Beta strandi370 – 378Combined sources9
Beta strandi386 – 394Combined sources9
Helixi400 – 410Combined sources11
Beta strandi416 – 421Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W15X-ray1.93A288-425[»]
1W16X-ray2.30A288-425[»]
ProteinModelPortaliP50232.
SMRiP50232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50232.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini155 – 258C2 1PROSITE-ProRule annotationAdd BLAST104
Domaini289 – 392C2 2PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni147 – 297Phospholipid bindingCuratedAdd BLAST151

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.
ENOG410XRME. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiP50232.
KOiK19904.
OMAiQIAKWHM.
OrthoDBiEOG091G09ZN.
PhylomeDBiP50232.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028683. SYT4.
[Graphical view]
PANTHERiPTHR10024:SF114. PTHR10024:SF114. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50232-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPITTSRVE FDEIPTVVGI FSAFGLVFTV SLFAWICCQR RSAKSNKTPP
60 70 80 90 100
YKFVHVLKGV DIYPENLSSK KKFGGDDKSE AKRKAALPNL SLHLDLEKRD
110 120 130 140 150
LNGNFPKTNP KAGSSSDLEN VTPKLFPETE KEAVSPESLK SSTSLTSEEK
160 170 180 190 200
QEKLGTLFLS LEYNFEKKAF VVNIKEAQGL PAMDEQSMTS DPYIKMTILP
210 220 230 240 250
EKKHKVKTRV LRKTLDPVFD ETFTFYGVPY PHIQELSLHF TVLSFDRFSR
260 270 280 290 300
DDVIGEVLVP LSGIELSDGK MLMTREIIKR NAKKSSGRGE LLVSLCYQST
310 320 330 340 350
TNTLTVVVLK ARHLPKSDVS GLSDPYVKVN LYHAKKRISK KKTHVKKCTP
360 370 380 390 400
NAVFNELFVF DIPCESLEEI SVEFLVLDSE RGSRNEVIGR LVLGATAEGS
410 420
GGGHWKEICD FPRRQIAKWH MLCDG
Length:425
Mass (Da):47,685
Last modified:October 1, 1996 - v1
Checksum:i6AC88E00878936BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14398 mRNA. Translation: AAA68519.1.
L38247 mRNA. Translation: AAA67327.1.
PIRiI59355.
RefSeqiNP_113881.1. NM_031693.2.
UniGeneiRn.126675.

Genome annotation databases

EnsembliENSRNOT00000023594; ENSRNOP00000023593; ENSRNOG00000017333.
GeneIDi64440.
KEGGirno:64440.
UCSCiRGD:68397. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14398 mRNA. Translation: AAA68519.1.
L38247 mRNA. Translation: AAA67327.1.
PIRiI59355.
RefSeqiNP_113881.1. NM_031693.2.
UniGeneiRn.126675.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W15X-ray1.93A288-425[»]
1W16X-ray2.30A288-425[»]
ProteinModelPortaliP50232.
SMRiP50232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50232. 5 interactors.
STRINGi10116.ENSRNOP00000023593.

PTM databases

iPTMnetiP50232.
PhosphoSitePlusiP50232.

Proteomic databases

PaxDbiP50232.
PRIDEiP50232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023594; ENSRNOP00000023593; ENSRNOG00000017333.
GeneIDi64440.
KEGGirno:64440.
UCSCiRGD:68397. rat.

Organism-specific databases

CTDi6860.
RGDi68397. Syt4.

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232126.
HOVERGENiHBG005010.
InParanoidiP50232.
KOiK19904.
OMAiQIAKWHM.
OrthoDBiEOG091G09ZN.
PhylomeDBiP50232.
TreeFamiTF315600.

Miscellaneous databases

EvolutionaryTraceiP50232.
PROiP50232.

Gene expression databases

BgeeiENSRNOG00000017333.
GenevisibleiP50232. RN.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR028683. SYT4.
[Graphical view]
PANTHERiPTHR10024:SF114. PTHR10024:SF114. 1 hit.
PfamiPF00168. C2. 2 hits.
[Graphical view]
PRINTSiPR00399. SYNAPTOTAGMN.
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
PROSITEiPS50004. C2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSYT4_RAT
AccessioniPrimary (citable) accession number: P50232
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 132 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.