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Protein

Synaptotagmin 1

Gene

Syt1

Organism
Drosophila melanogaster (Fruit fly)
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.1 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi222 – 2221Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi223 – 2231Calcium 1By similarity
Metal bindingi223 – 2231Calcium 2By similarity
Metal bindingi229 – 2291Calcium 1By similarity
Metal bindingi282 – 2821Calcium 1By similarity
Metal bindingi282 – 2821Calcium 2By similarity
Metal bindingi283 – 2831Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi284 – 2841Calcium 1By similarity
Metal bindingi284 – 2841Calcium 2By similarity
Metal bindingi284 – 2841Calcium 3By similarity
Metal bindingi287 – 2871Calcium 3By similarity
Metal bindingi288 – 2881Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi290 – 2901Calcium 2By similarity
Metal bindingi290 – 2901Calcium 3By similarity

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: FlyBase
  • calcium ion binding Source: FlyBase
  • phosphatidylserine binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • SNARE binding Source: FlyBase

GO - Biological processi

  • calcium ion-regulated exocytosis of neurotransmitter Source: FlyBase
  • exocytosis Source: FlyBase
  • larval locomotory behavior Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • positive regulation of vesicle fusion Source: FlyBase
  • regulation of neuromuscular synaptic transmission Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • regulation of synapse structure or activity Source: FlyBase
  • rhythmic synaptic transmission Source: FlyBase
  • synaptic transmission Source: FlyBase
  • synaptic vesicle endocytosis Source: FlyBase
  • synaptic vesicle exocytosis Source: FlyBase
  • synaptic vesicle transport Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin 1
Alternative name(s):
p65
Gene namesi
Name:Syt1
Synonyms:syt
ORF Names:CG3139
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0004242. Syt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 107107VesicularAdd
BLAST
Transmembranei108 – 13427HelicalSequence analysisAdd
BLAST
Topological domaini135 – 474340CytoplasmicAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: GOC
  • integral component of membrane Source: FlyBase
  • integral component of synaptic vesicle membrane Source: FlyBase
  • membrane Source: FlyBase
  • neuromuscular junction Source: FlyBase
  • synaptic vesicle Source: FlyBase
  • synaptic vesicle membrane Source: UniProtKB-SubCell
  • terminal bouton Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474Synaptotagmin 1PRO_0000183986Add
BLAST

Proteomic databases

PaxDbiP21521.

Expressioni

Gene expression databases

BgeeiP21521.
ExpressionAtlasiP21521. differential.
GenevisibleiP21521. DM.

Interactioni

Subunit structurei

Homodimer or homotrimer (Potential). Interacts with StnA and StnB via its second C2 domain. This interaction may mediate its retrieval from the plasma membrane, thereby facilitating the internalization of multiple synaptic vesicles from the plasma membrane.Curated1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
stnAQ242112EBI-484504,EBI-604915
stnBQ242125EBI-484504,EBI-604879

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase
  • SNARE binding Source: FlyBase

Protein-protein interaction databases

BioGridi59696. 3 interactions.
IntActiP21521. 3 interactions.
MINTiMINT-783257.
STRINGi7227.FBpp0077410.

Structurei

3D structure databases

ProteinModelPortaliP21521.
SMRiP21521. Positions 191-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini206 – 29691C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini339 – 43092C2 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 434249Phospholipid bindingCuratedAdd
BLAST

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.
InParanoidiP21521.
KOiK15290.
OMAiETTHHSK.
OrthoDBiEOG78PV8W.
PhylomeDBiP21521.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
[Graphical view]
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]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P21521-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPPNAKSETD AKPEAEPAPA SEPAADLESV DQKLEETHHS KFREVDRQEQ
60 70 80 90 100
EVLAEKAAEA ASQRIAQVES TTRSATTEAQ ESTTTAVPVI KKIEHVGEVV
110 120 130 140 150
TEVIAERTGL PTWGVVAIII LVFLVVFGII FFCVRRFLKK RRTKDGKGKK
160 170 180 190 200
GVDMKSVQLL GSAYKEKVQP DMEELTENAE EGDEEDKQSE QKLGRLNFKL
210 220 230 240 250
EYDFNSNSLA VTVIQAEELP ALDMGGTSDP YVKVYLLPDK KKKFETKVHR
260 270 280 290 300
KTLSPVFNET FTFKSLPYAD AMNKTLVFAI FDFDRFSKHD QIGEVKVPLC
310 320 330 340 350
TIDLAQTIEE WRDLVSVEGE GGQEKLGDIC FSLRYVPTAG KLTVVILEAK
360 370 380 390 400
NLKKMDVGGL SDPYVKIAIM QNGKRLKKKK TSIKKCTLNP YYNESFSFEV
410 420 430 440 450
PFEQIQKICL VVTVVDYDRI GTSEPIGRCI LGCMGTGTEL RHWSDMLASP
460 470
RRPIAQWHTL KDPEETDEIL KNMK
Length:474
Mass (Da):53,260
Last modified:May 14, 2014 - v3
Checksum:i76F3A34EEABE875B
GO
Isoform B (identifier: P21521-2) [UniParc]FASTAAdd to basket

Also known as: C, I

The sequence of this isoform differs from the canonical sequence as follows:
     168-169: Missing.

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):53,033
Checksum:i40BB77BB9D468FCA
GO
Isoform E (identifier: P21521-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-325: Missing.

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):53,003
Checksum:i4B1802A7171FABC5
GO
Isoform G (identifier: P21521-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-331: EKLGDICF → VVLREVNI
     332-474: Missing.

Note: No experimental confirmation available.
Show »
Length:331
Mass (Da):37,049
Checksum:i6547B3F12C9300C6
GO
Isoform F (identifier: P21521-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-170: QP → SV
     171-474: Missing.

Note: No experimental confirmation available.
Show »
Length:170
Mass (Da):18,643
Checksum:iD7DE111600B3D9FF
GO

Sequence cautioni

The sequence AAM50109.1 differs from that shown.Intron retention.Curated
The sequence AAM50109.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261D → E in AAA28925 (PubMed:1840599).Curated

RNA editingi

Edited at positions 367, 379, 383 and 405.2 Publications
Partially edited.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti367 – 3671I → V in RNA edited version.
Natural varianti379 – 3791K → R in RNA edited version.
Natural varianti383 – 3831I → V in RNA edited version.
Natural varianti405 – 4051I → M in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei168 – 1692Missing in isoform B. 1 PublicationVSP_011862
Alternative sequencei169 – 1702QP → SV in isoform F. CuratedVSP_054628
Alternative sequencei171 – 474304Missing in isoform F. CuratedVSP_054629Add
BLAST
Alternative sequencei324 – 3318EKLGDICF → VVLREVNI in isoform G. CuratedVSP_054630
Alternative sequencei324 – 3252Missing in isoform E. CuratedVSP_054631
Alternative sequencei332 – 474143Missing in isoform G. CuratedVSP_054632Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55048 mRNA. Translation: AAA28925.1.
AE014134 Genomic DNA. Translation: AAF51205.1.
AE014134 Genomic DNA. Translation: AAF51206.2.
AE014134 Genomic DNA. Translation: AAS64625.2.
AE014134 Genomic DNA. Translation: AAN10415.1.
AE014134 Genomic DNA. Translation: AGB92502.1.
AE014134 Genomic DNA. Translation: AGB92503.1.
BT004498 mRNA. Translation: AAO42662.1.
AY119455 mRNA. Translation: AAM50109.1. Sequence problems.
PIRiB39052. BMFFSY.
RefSeqiNP_001259965.1. NM_001273036.1. [P21521-6]
NP_001259966.1. NM_001273037.1. [P21521-5]
NP_001285568.1. NM_001298639.1. [P21521-2]
NP_523460.2. NM_078736.3. [P21521-1]
NP_722838.1. NM_164501.2. [P21521-2]
NP_722839.1. NM_164502.2. [P21521-2]
NP_995619.2. NM_205897.2. [P21521-4]
UniGeneiDm.19478.

Genome annotation databases

EnsemblMetazoaiFBtr0077726; FBpp0077410; FBgn0004242. [P21521-1]
GeneIDi33473.
KEGGidme:Dmel_CG3139.

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55048 mRNA. Translation: AAA28925.1.
AE014134 Genomic DNA. Translation: AAF51205.1.
AE014134 Genomic DNA. Translation: AAF51206.2.
AE014134 Genomic DNA. Translation: AAS64625.2.
AE014134 Genomic DNA. Translation: AAN10415.1.
AE014134 Genomic DNA. Translation: AGB92502.1.
AE014134 Genomic DNA. Translation: AGB92503.1.
BT004498 mRNA. Translation: AAO42662.1.
AY119455 mRNA. Translation: AAM50109.1. Sequence problems.
PIRiB39052. BMFFSY.
RefSeqiNP_001259965.1. NM_001273036.1. [P21521-6]
NP_001259966.1. NM_001273037.1. [P21521-5]
NP_001285568.1. NM_001298639.1. [P21521-2]
NP_523460.2. NM_078736.3. [P21521-1]
NP_722838.1. NM_164501.2. [P21521-2]
NP_722839.1. NM_164502.2. [P21521-2]
NP_995619.2. NM_205897.2. [P21521-4]
UniGeneiDm.19478.

3D structure databases

ProteinModelPortaliP21521.
SMRiP21521. Positions 191-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59696. 3 interactions.
IntActiP21521. 3 interactions.
MINTiMINT-783257.
STRINGi7227.FBpp0077410.

Proteomic databases

PaxDbiP21521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077726; FBpp0077410; FBgn0004242. [P21521-1]
GeneIDi33473.
KEGGidme:Dmel_CG3139.

Organism-specific databases

CTDi6857.
FlyBaseiFBgn0004242. Syt1.

Phylogenomic databases

eggNOGiENOG410IT3Q. Eukaryota.
ENOG410Z15P. LUCA.
GeneTreeiENSGT00760000118973.
InParanoidiP21521.
KOiK15290.
OMAiETTHHSK.
OrthoDBiEOG78PV8W.
PhylomeDBiP21521.

Enzyme and pathway databases

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

Miscellaneous databases

GenomeRNAii33473.
PROiP21521.

Gene expression databases

BgeeiP21521.
ExpressionAtlasiP21521. differential.
GenevisibleiP21521. DM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
InterProiIPR000008. C2_dom.
IPR001565. Synaptotagmin.
[Graphical view]
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. "Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans."
    Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.
    J. Biol. Chem. 266:615-622(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], RNA EDITING OF POSITION 383 AND 405.
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), RNA EDITING OF POSITION 367.
    Strain: Berkeley.
    Tissue: Head.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-380 (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  6. "The products of the Drosophila stoned locus interact with synaptic vesicles via synaptotagmin."
    Phillips A.M., Smith M., Ramaswami M., Kelly L.E.
    J. Neurosci. 20:8254-8261(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STNA AND STNB.
  7. "Nervous system targets of RNA editing identified by comparative genomics."
    Hoopengardner B., Bhalla T., Staber C., Reenan R.
    Science 301:832-836(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITIONS 367; 379; 383 AND 405.

Entry informationi

Entry nameiSY65_DROME
AccessioniPrimary (citable) accession number: P21521
Secondary accession number(s): A4V023
, M9PB17, M9PE99, Q7KU16, Q86NN2, Q8MRR8, Q9VQG7, Q9VQG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 14, 2014
Last modified: June 8, 2016
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.