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Protein

Synaptotagmin-1

Gene

Syt1

Organism
Mus musculus (Mouse)
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.

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 bindingi171 – 1711Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi172 – 1721Calcium 1By similarity
Metal bindingi172 – 1721Calcium 2By similarity
Metal bindingi178 – 1781Calcium 1By similarity
Metal bindingi230 – 2301Calcium 1By similarity
Metal bindingi230 – 2301Calcium 2By similarity
Metal bindingi231 – 2311Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi232 – 2321Calcium 1By similarity
Metal bindingi232 – 2321Calcium 2By similarity
Metal bindingi232 – 2321Calcium 3By similarity
Metal bindingi235 – 2351Calcium 3By similarity
Metal bindingi236 – 2361Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi238 – 2381Calcium 2By similarity
Metal bindingi238 – 2381Calcium 3By similarity

GO - Molecular functioni

GO - Biological processi

  • fast, calcium ion-dependent exocytosis of neurotransmitter Source: ParkinsonsUK-UCL
  • neurotransmitter secretion Source: MGI
  • positive regulation of calcium ion-dependent exocytosis Source: Ensembl
  • positive regulation of dendrite extension Source: MGI
  • positive regulation of synaptic transmission Source: ParkinsonsUK-UCL
  • positive regulation of vesicle fusion Source: Ensembl
  • regulation of calcium ion-dependent exocytosis Source: CACAO
  • regulation of regulated secretory pathway Source: ParkinsonsUK-UCL
  • regulation of synaptic transmission, glutamatergic Source: ParkinsonsUK-UCL
  • response to calcium ion Source: Ensembl
  • synaptic vesicle endocytosis Source: GO_Central
  • synaptic vesicle exocytosis Source: MGI
  • vesicle docking Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_281668. Acetylcholine Neurotransmitter Release Cycle.
REACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_319523. GABA synthesis, release, reuptake and degradation.
REACT_325189. Norepinephrine Neurotransmitter Release Cycle.

Protein family/group databases

TCDBi9.A.48.1.1. the unconventional protein secretion (ups) system.

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name:
SytI
p65
Gene namesi
Name:Syt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:99667. Syt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757VesicularSequence AnalysisAdd
BLAST
Transmembranei58 – 7922HelicalSequence AnalysisAdd
BLAST
Topological domaini80 – 421342CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • chromaffin granule membrane Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • dense core granule Source: MGI
  • excitatory synapse Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • neuron projection Source: ParkinsonsUK-UCL
  • plasma membrane Source: UniProtKB
  • presynaptic membrane Source: MGI
  • secretory granule Source: MGI
  • SNARE complex Source: Ensembl
  • synaptic vesicle Source: UniProtKB
  • synaptic vesicle membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 421421Synaptotagmin-1PRO_0000183938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi24 – 241N-linked (GlcNAc...)By similarity
Lipidationi74 – 741S-palmitoyl cysteineBy similarity
Lipidationi75 – 751S-palmitoyl cysteineBy similarity
Lipidationi77 – 771S-palmitoyl cysteineBy similarity
Lipidationi79 – 791S-palmitoyl cysteineBy similarity
Lipidationi82 – 821S-palmitoyl cysteineBy similarity
Modified residuei128 – 1281PhosphothreonineBy similarity
Modified residuei229 – 2291Phosphotyrosine1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP46096.
PaxDbiP46096.
PRIDEiP46096.

PTM databases

PhosphoSiteiP46096.

Expressioni

Gene expression databases

BgeeiP46096.
CleanExiMM_SYT1.
ExpressionAtlasiP46096. baseline and differential.
GenevisibleiP46096. MM.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SCAMP5Q8TAC92EBI-445340,EBI-2695784From a different organism.

Protein-protein interaction databases

BioGridi203611. 4 interactions.
DIPiDIP-31322N.
IntActiP46096. 13 interactions.
MINTiMINT-4136555.
STRINGi10090.ENSMUSP00000063293.

Structurei

3D structure databases

ProteinModelPortaliP46096.
SMRiP46096. Positions 140-418.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini143 – 244102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini274 – 377104C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 381247Phospholipid bindingCuratedAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi80 – 11940Lys-richAdd
BLAST

Domaini

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

eggNOGiCOG5038.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP46096.
KOiK15290.
OMAiHDIIGEY.
OrthoDBiEOG78PV8W.
PhylomeDBiP46096.
TreeFamiTF315600.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF183. PTHR10024:SF183. 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.

P46096-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSASRPEAL 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):47,418
Last modified:November 1, 1995 - v1
Checksum:i7FDEFF37170BD169
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37792 mRNA. Translation: BAA07040.1.
AK078790 mRNA. Translation: BAC37395.1.
BC042519 mRNA. Translation: AAH42519.1.
CCDSiCCDS24163.1.
RefSeqiNP_001239270.1. NM_001252341.1.
NP_001239271.1. NM_001252342.1.
NP_033332.1. NM_009306.3.
XP_006513509.1. XM_006513446.1.
XP_006513510.1. XM_006513447.1.
XP_006513511.1. XM_006513448.1.
UniGeneiMm.289702.
Mm.489829.

Genome annotation databases

EnsembliENSMUST00000064054; ENSMUSP00000063293; ENSMUSG00000035864.
ENSMUST00000105276; ENSMUSP00000100912; ENSMUSG00000035864.
GeneIDi20979.
KEGGimmu:20979.
UCSCiuc007gzg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D37792 mRNA. Translation: BAA07040.1.
AK078790 mRNA. Translation: BAC37395.1.
BC042519 mRNA. Translation: AAH42519.1.
CCDSiCCDS24163.1.
RefSeqiNP_001239270.1. NM_001252341.1.
NP_001239271.1. NM_001252342.1.
NP_033332.1. NM_009306.3.
XP_006513509.1. XM_006513446.1.
XP_006513510.1. XM_006513447.1.
XP_006513511.1. XM_006513448.1.
UniGeneiMm.289702.
Mm.489829.

3D structure databases

ProteinModelPortaliP46096.
SMRiP46096. Positions 140-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203611. 4 interactions.
DIPiDIP-31322N.
IntActiP46096. 13 interactions.
MINTiMINT-4136555.
STRINGi10090.ENSMUSP00000063293.

Protein family/group databases

TCDBi9.A.48.1.1. the unconventional protein secretion (ups) system.

PTM databases

PhosphoSiteiP46096.

Proteomic databases

MaxQBiP46096.
PaxDbiP46096.
PRIDEiP46096.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064054; ENSMUSP00000063293; ENSMUSG00000035864.
ENSMUST00000105276; ENSMUSP00000100912; ENSMUSG00000035864.
GeneIDi20979.
KEGGimmu:20979.
UCSCiuc007gzg.2. mouse.

Organism-specific databases

CTDi6857.
MGIiMGI:99667. Syt1.

Phylogenomic databases

eggNOGiCOG5038.
GeneTreeiENSGT00760000118973.
HOGENOMiHOG000232127.
HOVERGENiHBG005010.
InParanoidiP46096.
KOiK15290.
OMAiHDIIGEY.
OrthoDBiEOG78PV8W.
PhylomeDBiP46096.
TreeFamiTF315600.

Enzyme and pathway databases

ReactomeiREACT_281668. Acetylcholine Neurotransmitter Release Cycle.
REACT_287745. Glutamate Neurotransmitter Release Cycle.
REACT_319523. GABA synthesis, release, reuptake and degradation.
REACT_325189. Norepinephrine Neurotransmitter Release Cycle.

Miscellaneous databases

ChiTaRSiSyt1. mouse.
NextBioi299964.
PROiP46096.
SOURCEiSearch...

Gene expression databases

BgeeiP46096.
CleanExiMM_SYT1.
ExpressionAtlasiP46096. baseline and differential.
GenevisibleiP46096. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1.
[Graphical view]
PANTHERiPTHR10024:SF183. PTHR10024:SF183. 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. "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of IP4BP/synaptotagmin II."
    Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K.
    J. Biol. Chem. 269:29206-29211(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  4. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 183-189; 201-233; 245-260; 273-281; 289-297; 302-313; 333-366 AND 376-388, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. Cited for: INTERACTION WITH SV2B; SYNTAXIN-1 AND SNAP25.
  6. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiSYT1_MOUSE
AccessioniPrimary (citable) accession number: P46096
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 148 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.