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Protein

Extended synaptotagmin-1

Gene

Esyt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi334 – 3341Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi335 – 3351Calcium 1By similarity
Metal bindingi335 – 3351Calcium 2By similarity
Metal bindingi347 – 3471Calcium 2By similarity
Metal bindingi394 – 3941Calcium 1By similarity
Metal bindingi394 – 3941Calcium 2By similarity
Metal bindingi396 – 3961Calcium 1By similarity
Metal bindingi396 – 3961Calcium 2By similarity
Metal bindingi396 – 3961Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi398 – 3981Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi400 – 4001Calcium 3By similarity
Metal bindingi401 – 4011Calcium 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extended synaptotagmin-1
Short name:
E-Syt1
Alternative name(s):
Membrane-bound C2 domain-containing protein
Gene namesi
Name:Esyt1
Synonyms:Fam62a, Mbc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1344426. Esyt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2828CytoplasmicSequence analysisAdd
BLAST
Transmembranei29 – 4921HelicalSequence analysisAdd
BLAST
Topological domaini50 – 523LumenalSequence analysis
Transmembranei53 – 7321HelicalSequence analysisAdd
BLAST
Topological domaini74 – 10921019CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi314 – 3141S → A: Abolished phosphorylation by CDK5. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10921092Extended synaptotagmin-1PRO_0000234345Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei314 – 3141Phosphoserine; by CDK51 Publication
Modified residuei804 – 8041N6-acetyllysineBy similarity
Modified residuei807 – 8071PhosphoserineBy similarity
Modified residuei937 – 9371PhosphoserineBy similarity
Modified residuei951 – 9511PhosphoserineCombined sources
Modified residuei997 – 9971PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on Ser residues in insulin-treated adipocytes (in vitro); this promotes interaction with SLC2A4.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ3U7R1.
MaxQBiQ3U7R1.
PaxDbiQ3U7R1.
PRIDEiQ3U7R1.

PTM databases

iPTMnetiQ3U7R1.
PhosphoSiteiQ3U7R1.
SwissPalmiQ3U7R1.

Expressioni

Gene expression databases

BgeeiQ3U7R1.
CleanExiMM_MBC2.
GenevisibleiQ3U7R1. MM.

Interactioni

Subunit structurei

Interacts with ESYT2 and ESYT3 (By similarity). Interacts (phosphorylated form) with SLC2A4.By similarity1 Publication

Protein-protein interaction databases

BioGridi204808. 1 interaction.
DIPiDIP-48746N.
IntActiQ3U7R1. 1 interaction.
MINTiMINT-2633603.
STRINGi10090.ENSMUSP00000026427.

Structurei

3D structure databases

ProteinModelPortaliQ3U7R1.
SMRiQ3U7R1. Positions 321-425, 630-886, 959-1086.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini306 – 407102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini455 – 54894C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini621 – 722102C2 3PROSITE-ProRule annotationAdd
BLAST
Domaini772 – 86493C2 4PROSITE-ProRule annotationAdd
BLAST
Domaini950 – 1065116C2 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 303175Glycerophospholipid-binding barrel-like domainBy similarityAdd
BLAST
Regioni1006 – 10138Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membraneBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi910 – 92112Poly-SerAdd
BLAST

Domaini

Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.By similarity
The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium. The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for translocation to the cell membrane in response to increased cytosolic calcium levels (By similarity).By similarity
Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior.By similarity

Sequence similaritiesi

Belongs to the extended synaptotagmin family.Curated
Contains 5 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1012. Eukaryota.
COG5038. LUCA.
GeneTreeiENSGT00550000074417.
HOGENOMiHOG000043080.
HOVERGENiHBG055795.
InParanoidiQ3U7R1.
OMAiSQHSGVE.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ3U7R1.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 5 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3U7R1-1) [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
MEHSPEEGAS PEPSGQPPAT DSTRDGGSGV PPAGPGAASE ALAVLTSFGR
60 70 80 90 100
RLLVLVPVYL AGAAGLSVGF VLFGLALYLG WRRVRDGKER SLRAARQLLD
110 120 130 140 150
DEERITAETL YMSHRELPAW VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL
160 170 180 190 200
LAETVAPAVR GANPHLQTFT FTRVELGEKP LRIIGVKVHP SQRKDQILLD
210 220 230 240 250
LNVSYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL TGDLPIVGAV
260 270 280 290 300
SMFFIKRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA FLVLPNRLLV
310 320 330 340 350
PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA
360 370 380 390 400
LVRVGTQTFC SRVIDEELNP HWGETYEVIV HEVPGQEIEV EVFDKDPDKD
410 420 430 440 450
DFLGRMKLDV GKVLQAGVLD NWYPLQGGQG QVHLRLEWLS LLPDAEKLDQ
460 470 480 490 500
VLQWNRGITS RPEPPSAAIL VVYLDRAQDL PLKKGNKEPN PMVQLSVQDV
510 520 530 540 550
TRESKATYST NSPVWEEAFR FFLQDPRSQE LDVQVKDDSR ALTLGALTLP
560 570 580 590 600
LARLLTASEL TLDQWFQLSS SGPNSRLYMK LVMRILYLDY SEIRFPTVPG
610 620 630 640 650
AQDWDRESLE TGSSVDAPPR PYHTTPNSHF GTENVLRIHV LEAQDLIAKD
660 670 680 690 700
RFLGGLVKGK SDPYVKLKVA GKSFRTHVVR EDLNPRWNEV FEVIVTSIPG
710 720 730 740 750
QELEIEVFDK DLDKDDFLGR YKVSLTTVLN SGFLDEWLTL EDVPSGRLHL
760 770 780 790 800
RLERLTPRPT AAELEEVLQV NSLIQTQKSS ELAAALLSVF LERAEDLPLR
810 820 830 840 850
KGTKPPSPYA TITVGETSHK TKTVSQSSAP VWEESASFLI RKPHAESLEL
860 870 880 890 900
QVRGEGTGTL GSVSLPLSEL LQEDQLCLDH WFALSGQGQV LMRAQLGILV
910 920 930 940 950
SQHSGVEAHS HSYSHSHSSS SLNDEPEALG GPTHPASPVL EVRHRLTHGD
960 970 980 990 1000
SPSEAPVGPL GQVKLTVWYH SDEQKLISII HSCRALRQNG RDLPDPYVSV
1010 1020 1030 1040 1050
LLLPDKNRST KRKTPQKKRT LNPEFNERFE WDLPLDGTLR RKLDVSVKSN
1060 1070 1080 1090
SSFMSREREL LGKVQLDLAE IDLSQGAAQW YDLMDDRDKG GS
Length:1,092
Mass (Da):121,554
Last modified:May 16, 2006 - v2
Checksum:i71A397EC52DE6DA9
GO
Isoform 2 (identifier: Q3U7R1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     852-893: VRGEGTGTLG...LSGQGQVLMR → ACFIHLLFLF...CGNLWATAHS
     894-1092: Missing.

Note: No experimental confirmation available.
Show »
Length:893
Mass (Da):99,673
Checksum:i956808B5CD6450E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti385 – 3851G → R in BAC32020 (PubMed:15489334).Curated
Sequence conflicti392 – 3943VFD → IQH in AAD10190 (PubMed:10350628).Curated
Sequence conflicti829 – 84113APVWE…SFLIR → GFGLEAKIRHEGG in AAD10189 (PubMed:10350628).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei852 – 89342VRGEG…QVLMR → ACFIHLLFLFERGREQRTVF EFEVFGVNSFPPCGNLWATA HS in isoform 2. 1 PublicationVSP_018278Add
BLAST
Alternative sequencei894 – 1092199Missing in isoform 2. 1 PublicationVSP_018279Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008224 mRNA. Translation: BAB25542.1.
AK044656 mRNA. Translation: BAC32020.1.
AK152482 mRNA. Translation: BAE31254.1.
AK152554 mRNA. Translation: BAE31308.1.
BC011482 mRNA. Translation: AAH11482.1.
AF098633 mRNA. Translation: AAD10189.1.
AF098634 mRNA. Translation: AAD10190.1.
CCDSiCCDS24280.1. [Q3U7R1-1]
RefSeqiNP_035973.1. NM_011843.2. [Q3U7R1-1]
UniGeneiMm.66056.

Genome annotation databases

EnsembliENSMUST00000026427; ENSMUSP00000026427; ENSMUSG00000025366. [Q3U7R1-1]
GeneIDi23943.
KEGGimmu:23943.
UCSCiuc007hng.1. mouse. [Q3U7R1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008224 mRNA. Translation: BAB25542.1.
AK044656 mRNA. Translation: BAC32020.1.
AK152482 mRNA. Translation: BAE31254.1.
AK152554 mRNA. Translation: BAE31308.1.
BC011482 mRNA. Translation: AAH11482.1.
AF098633 mRNA. Translation: AAD10189.1.
AF098634 mRNA. Translation: AAD10190.1.
CCDSiCCDS24280.1. [Q3U7R1-1]
RefSeqiNP_035973.1. NM_011843.2. [Q3U7R1-1]
UniGeneiMm.66056.

3D structure databases

ProteinModelPortaliQ3U7R1.
SMRiQ3U7R1. Positions 321-425, 630-886, 959-1086.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204808. 1 interaction.
DIPiDIP-48746N.
IntActiQ3U7R1. 1 interaction.
MINTiMINT-2633603.
STRINGi10090.ENSMUSP00000026427.

PTM databases

iPTMnetiQ3U7R1.
PhosphoSiteiQ3U7R1.
SwissPalmiQ3U7R1.

Proteomic databases

EPDiQ3U7R1.
MaxQBiQ3U7R1.
PaxDbiQ3U7R1.
PRIDEiQ3U7R1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026427; ENSMUSP00000026427; ENSMUSG00000025366. [Q3U7R1-1]
GeneIDi23943.
KEGGimmu:23943.
UCSCiuc007hng.1. mouse. [Q3U7R1-1]

Organism-specific databases

CTDi23344.
MGIiMGI:1344426. Esyt1.

Phylogenomic databases

eggNOGiKOG1012. Eukaryota.
COG5038. LUCA.
GeneTreeiENSGT00550000074417.
HOGENOMiHOG000043080.
HOVERGENiHBG055795.
InParanoidiQ3U7R1.
OMAiSQHSGVE.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ3U7R1.
TreeFamiTF324255.

Miscellaneous databases

ChiTaRSiEsyt1. mouse.
PROiQ3U7R1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3U7R1.
CleanExiMM_MBC2.
GenevisibleiQ3U7R1. MM.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 5 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-632 AND 955-1092 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Retina and Small intestine.
  2. "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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Salivary gland.
  3. "Cloning and preliminary characterization of a 121 kDa protein with multiple predicted C2 domains."
    Morris N.J., Ross S.A., Neveu J.M., Lane W.S., Lienhard G.E.
    Biochim. Biophys. Acta 1431:525-530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 392-1092 (ISOFORM 1).
    Tissue: Mammary gland.
  4. "The atypical kinase Cdk5 is activated by insulin, regulates the association between GLUT4 and E-Syt1, and modulates glucose transport in 3T3-L1 adipocytes."
    Lalioti V., Muruais G., Dinarina A., van Damme J., Vandekerckhove J., Sandoval I.V.
    Proc. Natl. Acad. Sci. U.S.A. 106:4249-4253(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-314, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-314, INTERACTION WITH SLC2A4.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-951, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiESYT1_MOUSE
AccessioniPrimary (citable) accession number: Q3U7R1
Secondary accession number(s): Q8C8R1
, Q91X62, Q9CVH0, Q9Z1X5, Q9Z1X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: June 8, 2016
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

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.