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Protein

Synaptotagmin-1

Gene

SYT1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 similarity

Cofactori

Ca2+By similarityNote: 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium, Calmodulin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiR-BTA-210500. Glutamate Neurotransmitter Release Cycle.
R-BTA-264642. Acetylcholine Neurotransmitter Release Cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name:
SytI
p65
Gene namesi
Name:SYT1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757VesicularSequence analysisAdd
BLAST
Transmembranei58 – 8023HelicalSequence analysisAdd
BLAST
Topological domaini81 – 422342CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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-1PRO_0000183935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251N-linked (GlcNAc...)Sequence analysis
Lipidationi75 – 751S-palmitoyl cysteineBy similarity
Lipidationi76 – 761S-palmitoyl cysteineBy similarity
Lipidationi78 – 781S-palmitoyl cysteineBy similarity
Lipidationi80 – 801S-palmitoyl cysteineBy similarity
Lipidationi83 – 831S-palmitoyl cysteineBy similarity
Modified residuei129 – 1291PhosphothreonineBy similarity
Modified residuei230 – 2301PhosphotyrosineBy similarity
Modified residuei265 – 2651PhosphoserineBy similarity
Modified residuei343 – 3431PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP48018.
PRIDEiP48018.

PTM databases

iPTMnetiP48018.

Interactioni

Subunit structurei

Homotetramer (Probable). Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1 and SNAP25 (By similarity). Interacts with calmodulin.By similarityCurated1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiP48018. 1 interaction.
MINTiMINT-1214882.
STRINGi9913.ENSBTAP00000008338.

Structurei

3D structure databases

ProteinModelPortaliP48018.
SMRiP48018. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini144 – 245102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 378104C2 2PROSITE-ProRule annotationAdd
BLAST

Region

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi81 – 12040Lys-richAdd
BLAST

Domaini

The first C2 domain mediates Ca2+-dependent phospholipid binding.By similarity
The second C2 domain mediates interaction with SV2A and probably with STN2.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

eggNOGiENOG410IT3Q. Eukaryota.
ENOG410Z15P. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP48018.
KOiK15290.
OMAiGEFKVAM.
OrthoDBiEOG78PV8W.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF239. PTHR10024:SF239. 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.

P48018-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSESHHEAL AAPPVTTVAT VLPHNATEPA SPGEGKEDAF SKLKEKFMNE
60 70 80 90 100
LHKIPLPPWA LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN
110 120 130 140 150
AINMKDVKDL GKTMKDQALK DDDAETGLTD GEEKEEPKEE EKLGKLQYSL
160 170 180 190 200
DYDFQNNQLL VGIIQAAELP ALDMGGTSDP YVKVFLLPDK KKKFETKVHR
210 220 230 240 250
KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI IGEFKVPMNT
260 270 280 290 300
VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL
310 320 330 340 350
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF
360 370 380 390 400
EQIQKVQVVV TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR
410 420
PIAQWHTLQV EEEVDAMLAV KK
Length:422
Mass (Da):47,623
Last modified:February 1, 1996 - v1
Checksum:iC158C34DAAE456EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05922 mRNA. Translation: AAA87360.1.
PIRiA45486.
RefSeqiNP_776617.1. NM_174192.3.
XP_005206087.1. XM_005206030.3.
UniGeneiBt.102207.
Bt.22951.

Genome annotation databases

EnsembliENSBTAT00000008338; ENSBTAP00000008338; ENSBTAG00000034693.
GeneIDi281511.
KEGGibta:281511.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05922 mRNA. Translation: AAA87360.1.
PIRiA45486.
RefSeqiNP_776617.1. NM_174192.3.
XP_005206087.1. XM_005206030.3.
UniGeneiBt.102207.
Bt.22951.

3D structure databases

ProteinModelPortaliP48018.
SMRiP48018. Positions 141-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP48018. 1 interaction.
MINTiMINT-1214882.
STRINGi9913.ENSBTAP00000008338.

PTM databases

iPTMnetiP48018.

Proteomic databases

PaxDbiP48018.
PRIDEiP48018.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000008338; ENSBTAP00000008338; ENSBTAG00000034693.
GeneIDi281511.
KEGGibta:281511.

Organism-specific databases

CTDi6857.

Phylogenomic databases

eggNOGiENOG410IT3Q. Eukaryota.
ENOG410Z15P. LUCA.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP48018.
KOiK15290.
OMAiGEFKVAM.
OrthoDBiEOG78PV8W.
TreeFamiTF315600.

Enzyme and pathway databases

ReactomeiR-BTA-210500. Glutamate Neurotransmitter Release Cycle.
R-BTA-264642. Acetylcholine Neurotransmitter Release Cycle.

Miscellaneous databases

NextBioi20805478.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF239. PTHR10024:SF239. 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

  1. "Phosphorylation of synaptotagmin I by casein kinase II."
    Davletov B., Sontag J.M., Hata Y., Petrenko A.G., Fykse E.M., Jahn R., Suedhof T.C.
    J. Biol. Chem. 268:6816-6822(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Glycosylation and transmembrane topography of bovine chromaffin granule p65."
    Tugal H.B., van Leeuwen F., Apps D.K., Haywood J., Phillips J.H.
    Biochem. J. 279:699-703(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 113-132, INTERACTION WITH CALMODULIN, GLYCOSYLATION.
    Tissue: Adrenal gland.

Entry informationi

Entry nameiSYT1_BOVIN
AccessioniPrimary (citable) accession number: P48018
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 137 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.