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Q3TZZ7

- ESYT2_MOUSE

UniProt

Q3TZZ7 - ESYT2_MOUSE

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Protein
Extended synaptotagmin-2
Gene
Esyt2, D12Ertd551e, Fam62b
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi324 – 3241Calcium 1; via carbonyl oxygen By similarity
Metal bindingi325 – 3251Calcium 1 By similarity
Metal bindingi325 – 3251Calcium 2 By similarity
Metal bindingi337 – 3371Calcium 2 By similarity
Metal bindingi384 – 3841Calcium 1 By similarity
Metal bindingi384 – 3841Calcium 2 By similarity
Metal bindingi385 – 3851Calcium 2; via carbonyl oxygen By similarity
Metal bindingi386 – 3861Calcium 1 By similarity
Metal bindingi386 – 3861Calcium 2 By similarity
Metal bindingi386 – 3861Calcium 3; via carbonyl oxygen By similarity
Metal bindingi388 – 3881Calcium 3; via carbonyl oxygen By similarity
Metal bindingi390 – 3901Calcium 3 By similarity
Metal bindingi391 – 3911Calcium 1 By similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. calcium-dependent phospholipid binding Source: Ensembl
  3. phosphatidylcholine binding Source: UniProtKB
  4. phosphatidylethanolamine binding Source: UniProtKB
  5. phosphatidylinositol binding Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Lipid transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extended synaptotagmin-2
Short name:
E-Syt2
Gene namesi
Name:Esyt2
Synonyms:D12Ertd551e, Fam62b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:1261845. Esyt2.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2727Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei28 – 4821Helical; Reviewed prediction
Add
BLAST
Topological domaini49 – 513Lumenal Reviewed prediction
Transmembranei52 – 7221Helical; Reviewed prediction
Add
BLAST
Topological domaini73 – 845773Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  2. integral component of plasma membrane Source: Ensembl
  3. intrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  4. organelle membrane contact site Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 845845Extended synaptotagmin-2
PRO_0000278259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei615 – 6151Phosphoserine By similarity
Modified residuei662 – 6621Phosphoserine1 Publication
Modified residuei663 – 6631Phosphoserine By similarity
Modified residuei667 – 6671Phosphoserine By similarity
Modified residuei679 – 6791Phosphoserine By similarity
Modified residuei682 – 6821Phosphoserine1 Publication
Modified residuei685 – 6851Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3TZZ7.
PaxDbiQ3TZZ7.
PRIDEiQ3TZZ7.

PTM databases

PhosphoSiteiQ3TZZ7.

Expressioni

Gene expression databases

BgeeiQ3TZZ7.
CleanExiMM_D12ERTD551E.
GenevestigatoriQ3TZZ7.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

IntActiQ3TZZ7. 1 interaction.
MINTiMINT-4392453.
STRINGi10090.ENSMUSP00000098548.

Structurei

3D structure databases

ProteinModelPortaliQ3TZZ7.
SMRiQ3TZZ7. Positions 287-583, 680-841.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini296 – 397102C2 1
Add
BLAST
Domaini447 – 54195C2 2
Add
BLAST
Domaini712 – 816105C2 3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 294176Glycerophospholipid-binding barrel-like domain By similarity
Add
BLAST
Regioni757 – 7648Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi660 – 6634Poly-Ser

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 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 similaritiesi

Contains 3 C2 domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5038.
GeneTreeiENSGT00550000074417.
HOGENOMiHOG000043080.
HOVERGENiHBG055795.
InParanoidiB2RSN5.
OMAiVDVGQQP.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ3TZZ7.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
[Graphical view]
PfamiPF00168. C2. 3 hits.
[Graphical view]
SMARTiSM00239. C2. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q3TZZ7-1) [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

MSSAGGEGPE AGPGRAGGRS EPEAPGSALS VDLPGLLGQL ARSFALLLPV    50
YALGYLGLSF SWVLLALGLL AWCRRSRGLK ASRLCRALAL LEDEEQAVRL 100
GVRACDLPAW VHFPDTERAE WLNKTVKHMW PFICQFIEKL FRETIEPAVR 150
GANAHLSTFS FTKVDVGQQP LRVNGVKVYT ENVDKRQIIL DLQISFVGNC 200
EIDLEIKRYF CRAGVKSIQI HGTMRVILEP LIGDMPLVGA LSIFFLRKPL 250
LEINWTGLTN LLDIPGLNGL SDTIILDIIS NYLVLPNRIT VPLVSEVQIA 300
QLRFPIPKGV LRIHFIEAQD LQGKDTYLKG LVKGKSDPYG IIRVGNQIFQ 350
SKVIKENLSP KWNEVYEALV YEHPGQELEI ELFDEDPDKD DFLGSLMIDL 400
IEVEKERLLD EWFTLDEVPK GKLHLKLEWL TLMPDAANLD KVLADIRADK 450
DQASDGLSSA LLILYLDSAR NLPSGKKINS NPNPLVQMSV GHKAQESKIR 500
YKTSEPVWEE NFTFFIHNPR RQDLEVEVKD EQHQCSLGSL RIPLSQLLTS 550
DNMTINQRFQ LSNSGPNSTL KMKIALRVLH LEKQERPPDY QHSAQVKRPS 600
VSKEGRKMPI KSQMSASPGT GGANTAPSTP VMGVDDKPAM EEKPQPPEAS 650
PLGHRDLGRS SSSLLASPSH IAAKEPTPSI ASDISLPIAT QELRQRLRQL 700
ENGTTLGQSP LGQIQLTIRH SSQRNKLIVV VHSCRNLIAF SEDGSDPYVR 750
MYLLPDKRRS GRRKTHVSKK TLNPVFDQSF DFSVSLPEVQ RRTLDVAVKN 800
SGGFLSKDKG LLGKVLVVLA SEELAKGWTQ WYDLTEDGTR PQVIT 845
Length:845
Mass (Da):94,139
Last modified:October 11, 2005 - v1
Checksum:i988F3D97D7F3CF6C
GO
Isoform 2 (identifier: Q3TZZ7-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:358
Mass (Da):39,884
Checksum:i6AE8B94A52027E24
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 487487Missing in isoform 2.
VSP_023243Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26211.1. [Q3TZZ7-1]
RefSeqiNP_083007.2. NM_028731.5. [Q3TZZ7-1]
XP_006516136.1. XM_006516073.1. [Q3TZZ7-1]
UniGeneiMm.273755.

Genome annotation databases

EnsembliENSMUST00000100986; ENSMUSP00000098548; ENSMUSG00000021171. [Q3TZZ7-1]
GeneIDi52635.
KEGGimmu:52635.
UCSCiuc007pho.1. mouse. [Q3TZZ7-1]
uc007phq.1. mouse. [Q3TZZ7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26211.1. [Q3TZZ7-1 ]
RefSeqi NP_083007.2. NM_028731.5. [Q3TZZ7-1 ]
XP_006516136.1. XM_006516073.1. [Q3TZZ7-1 ]
UniGenei Mm.273755.

3D structure databases

ProteinModelPortali Q3TZZ7.
SMRi Q3TZZ7. Positions 287-583, 680-841.
ModBasei Search...

Protein-protein interaction databases

IntActi Q3TZZ7. 1 interaction.
MINTi MINT-4392453.
STRINGi 10090.ENSMUSP00000098548.

PTM databases

PhosphoSitei Q3TZZ7.

Proteomic databases

MaxQBi Q3TZZ7.
PaxDbi Q3TZZ7.
PRIDEi Q3TZZ7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100986 ; ENSMUSP00000098548 ; ENSMUSG00000021171 . [Q3TZZ7-1 ]
GeneIDi 52635.
KEGGi mmu:52635.
UCSCi uc007pho.1. mouse. [Q3TZZ7-1 ]
uc007phq.1. mouse. [Q3TZZ7-2 ]

Organism-specific databases

CTDi 57488.
MGIi MGI:1261845. Esyt2.

Phylogenomic databases

eggNOGi COG5038.
GeneTreei ENSGT00550000074417.
HOGENOMi HOG000043080.
HOVERGENi HBG055795.
InParanoidi B2RSN5.
OMAi VDVGQQP.
OrthoDBi EOG7RNJZK.
PhylomeDBi Q3TZZ7.
TreeFami TF324255.

Miscellaneous databases

NextBioi 309245.
PROi Q3TZZ7.
SOURCEi Search...

Gene expression databases

Bgeei Q3TZZ7.
CleanExi MM_D12ERTD551E.
Genevestigatori Q3TZZ7.

Family and domain databases

Gene3Di 2.60.40.150. 3 hits.
InterProi IPR000008. C2_dom.
[Graphical view ]
Pfami PF00168. C2. 3 hits.
[Graphical view ]
SMARTi SM00239. C2. 3 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 3 hits.
PROSITEi PS50004. C2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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] (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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. 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].

Entry informationi

Entry nameiESYT2_MOUSE
AccessioniPrimary (citable) accession number: Q3TZZ7
Secondary accession number(s): B2RSN5, Q9D5Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: October 11, 2005
Last modified: September 3, 2014
This is version 77 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, 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

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