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Q3TZZ7 (ESYT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extended synaptotagmin-2

Short name=E-Syt2
Gene names
Name:Esyt2
Synonyms:D12Ertd551e, Fam62b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex By similarity.

Subunit structure

Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1 By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Detected at sites of contact between the endoplasmic reticulum membrane and the cell membrane. Recruited to the cell membrane via the third C2 domain By similarity.

Domain

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 location at the cell membrane By similarity.

Contains a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol By similarity.

Sequence similarities

Belongs to the extended synaptotagmin family.

Contains 3 C2 domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3TZZ7-1)

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.
Isoform 2 (identifier: Q3TZZ7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-487: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Extended synaptotagmin-2
PRO_0000278259

Regions

Topological domain1 – 2727Cytoplasmic Potential
Transmembrane28 – 4821Helical; Potential
Topological domain49 – 513Lumenal Potential
Transmembrane52 – 7221Helical; Potential
Topological domain73 – 845773Cytoplasmic Potential
Domain296 – 397102C2 1
Domain447 – 54195C2 2
Domain712 – 816105C2 3
Region119 – 294176Glycerophospholipid-binding barrel-like domain By similarity
Region757 – 7648Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane By similarity
Compositional bias660 – 6634Poly-Ser

Sites

Metal binding3241Calcium 1; via carbonyl oxygen By similarity
Metal binding3251Calcium 1 By similarity
Metal binding3251Calcium 2 By similarity
Metal binding3371Calcium 2 By similarity
Metal binding3841Calcium 1 By similarity
Metal binding3841Calcium 2 By similarity
Metal binding3851Calcium 2; via carbonyl oxygen By similarity
Metal binding3861Calcium 1 By similarity
Metal binding3861Calcium 2 By similarity
Metal binding3861Calcium 3; via carbonyl oxygen By similarity
Metal binding3881Calcium 3; via carbonyl oxygen By similarity
Metal binding3901Calcium 3 By similarity
Metal binding3911Calcium 1 By similarity

Amino acid modifications

Modified residue6151Phosphoserine By similarity
Modified residue6621Phosphoserine Ref.5
Modified residue6631Phosphoserine By similarity
Modified residue6671Phosphoserine By similarity
Modified residue6791Phosphoserine By similarity
Modified residue6821Phosphoserine Ref.5
Modified residue6851Phosphoserine Ref.3 Ref.5

Natural variations

Alternative sequence1 – 487487Missing in isoform 2.
VSP_023243

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 988F3D97D7F3CF6C

FASTA84594,139
        10         20         30         40         50         60 
MSSAGGEGPE AGPGRAGGRS EPEAPGSALS VDLPGLLGQL ARSFALLLPV YALGYLGLSF 

        70         80         90        100        110        120 
SWVLLALGLL AWCRRSRGLK ASRLCRALAL LEDEEQAVRL GVRACDLPAW VHFPDTERAE 

       130        140        150        160        170        180 
WLNKTVKHMW PFICQFIEKL FRETIEPAVR GANAHLSTFS FTKVDVGQQP LRVNGVKVYT 

       190        200        210        220        230        240 
ENVDKRQIIL DLQISFVGNC EIDLEIKRYF CRAGVKSIQI HGTMRVILEP LIGDMPLVGA 

       250        260        270        280        290        300 
LSIFFLRKPL LEINWTGLTN LLDIPGLNGL SDTIILDIIS NYLVLPNRIT VPLVSEVQIA 

       310        320        330        340        350        360 
QLRFPIPKGV LRIHFIEAQD LQGKDTYLKG LVKGKSDPYG IIRVGNQIFQ SKVIKENLSP 

       370        380        390        400        410        420 
KWNEVYEALV YEHPGQELEI ELFDEDPDKD DFLGSLMIDL IEVEKERLLD EWFTLDEVPK 

       430        440        450        460        470        480 
GKLHLKLEWL TLMPDAANLD KVLADIRADK DQASDGLSSA LLILYLDSAR NLPSGKKINS 

       490        500        510        520        530        540 
NPNPLVQMSV GHKAQESKIR YKTSEPVWEE NFTFFIHNPR RQDLEVEVKD EQHQCSLGSL 

       550        560        570        580        590        600 
RIPLSQLLTS DNMTINQRFQ LSNSGPNSTL KMKIALRVLH LEKQERPPDY QHSAQVKRPS 

       610        620        630        640        650        660 
VSKEGRKMPI KSQMSASPGT GGANTAPSTP VMGVDDKPAM EEKPQPPEAS PLGHRDLGRS 

       670        680        690        700        710        720 
SSSLLASPSH IAAKEPTPSI ASDISLPIAT QELRQRLRQL ENGTTLGQSP LGQIQLTIRH 

       730        740        750        760        770        780 
SSQRNKLIVV VHSCRNLIAF SEDGSDPYVR MYLLPDKRRS GRRKTHVSKK TLNPVFDQSF 

       790        800        810        820        830        840 
DFSVSLPEVQ RRTLDVAVKN SGGFLSKDKG LLGKVLVVLA SEELAKGWTQ WYDLTEDGTR 


PQVIT 

« Hide

Isoform 2 [UniParc].

Checksum: 6AE8B94A52027E24
Show »

FASTA35839,884

References

« Hide 'large scale' references
[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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Retina and Testis.
[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] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
Tissue: Brain.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Structural characterization of soluble E-Syt2."
Groer G.J., Haslbeck M., Roessle M., Gessner A.
FEBS Lett. 582:3941-3947(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM BINDING.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-682 AND SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014813 mRNA. Translation: BAB29565.1.
AK044360 mRNA. Translation: BAC31884.1.
AK157352 mRNA. Translation: BAE34059.1.
BC052440 mRNA. Translation: AAH52440.1.
BC054797 mRNA. Translation: AAH54797.1.
BC059230 mRNA. Translation: AAH59230.1.
BC138937 mRNA. Translation: AAI38938.1.
CCDSCCDS26211.1. [Q3TZZ7-1]
RefSeqNP_083007.2. NM_028731.5. [Q3TZZ7-1]
XP_006516136.1. XM_006516073.1. [Q3TZZ7-1]
UniGeneMm.273755.

3D structure databases

ProteinModelPortalQ3TZZ7.
SMRQ3TZZ7. Positions 287-583, 680-841.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3TZZ7. 1 interaction.
MINTMINT-4392453.
STRING10090.ENSMUSP00000098548.

PTM databases

PhosphoSiteQ3TZZ7.

Proteomic databases

MaxQBQ3TZZ7.
PaxDbQ3TZZ7.
PRIDEQ3TZZ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100986; ENSMUSP00000098548; ENSMUSG00000021171. [Q3TZZ7-1]
GeneID52635.
KEGGmmu:52635.
UCSCuc007pho.1. mouse. [Q3TZZ7-1]
uc007phq.1. mouse. [Q3TZZ7-2]

Organism-specific databases

CTD57488.
MGIMGI:1261845. Esyt2.

Phylogenomic databases

eggNOGCOG5038.
GeneTreeENSGT00550000074417.
HOGENOMHOG000043080.
HOVERGENHBG055795.
InParanoidB2RSN5.
OMAVDVGQQP.
OrthoDBEOG7RNJZK.
PhylomeDBQ3TZZ7.
TreeFamTF324255.

Gene expression databases

BgeeQ3TZZ7.
CleanExMM_D12ERTD551E.
GenevestigatorQ3TZZ7.

Family and domain databases

Gene3D2.60.40.150. 3 hits.
InterProIPR000008. C2_dom.
[Graphical view]
PfamPF00168. C2. 3 hits.
[Graphical view]
SMARTSM00239. C2. 3 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 3 hits.
PROSITEPS50004. C2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio309245.
PROQ3TZZ7.
SOURCESearch...

Entry information

Entry nameESYT2_MOUSE
AccessionPrimary (citable) accession number: Q3TZZ7
Secondary accession number(s): B2RSN5, Q9D5Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot