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Q9Z1X1 (ESYT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Extended synaptotagmin-1

Short name=E-Syt1
Alternative name(s):
Membrane-bound C2 domain-containing protein
vp115
Gene names
Name:Esyt1
Synonyms:Fam62a, Mbc2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1088 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell membrane; Peripheral membrane protein By similarity. Note: Localizes primarily to the endoplasmic reticulum. Recruited to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels By similarity.

Tissue specificity

Ubiquitously expressed with a higher expression in spleen and white adipose tissue. Ref.1

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 translocation to the cell membrane in response to increased cytosolic calcium levels By similarity.

Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the extended synaptotagmin family.

Contains 5 C2 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10881088Extended synaptotagmin-1
PRO_0000234347

Regions

Topological domain1 – 3030Cytoplasmic Potential
Transmembrane31 – 5121Helical; Potential
Topological domain52 – 543Lumenal Potential
Transmembrane55 – 7521Helical; Potential
Topological domain76 – 10881013Cytoplasmic Potential
Domain308 – 409102C2 1
Domain457 – 55094C2 2
Domain623 – 724102C2 3
Domain774 – 86693C2 4
Domain956 – 1061106C2 5
Region131 – 305175Glycerophospholipid-binding barrel-like domain By similarity
Region1002 – 10098Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane By similarity
Compositional bias912 – 9176Poly-Ser

Sites

Metal binding3361Calcium 1; via carbonyl oxygen By similarity
Metal binding3371Calcium 1 By similarity
Metal binding3371Calcium 2 By similarity
Metal binding3491Calcium 2 By similarity
Metal binding3961Calcium 1 By similarity
Metal binding3961Calcium 2 By similarity
Metal binding3981Calcium 1 By similarity
Metal binding3981Calcium 2 By similarity
Metal binding3981Calcium 3; via carbonyl oxygen By similarity
Metal binding4001Calcium 3; via carbonyl oxygen By similarity
Metal binding4021Calcium 3 By similarity
Metal binding4031Calcium 1 By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3161Phosphoserine; by CDK5 By similarity
Modified residue8061N6-acetyllysine By similarity
Modified residue8091Phosphoserine By similarity
Modified residue9471Phosphoserine By similarity

Experimental info

Sequence conflict3731H → R in AAI01858. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z1X1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E7E12D9737FFB89D

FASTA1,088121,159
        10         20         30         40         50         60 
MERSPEEGAG PEPSGQSPAT DSTRERDGGS GVPPAGPGAA SEALAVLTSF GRRLLVLVPV 

        70         80         90        100        110        120 
YLAGAAGLSV GFVLFGLALY LGWRRVRDGK ERSLRAARQL LDDEERITAE TLYMSHRELP 

       130        140        150        160        170        180 
AWVSFPDVEK AEWLNKIVVQ VWPFLGQYME KLLAETVAPA VRGANPHLQT FTFTRVELGE 

       190        200        210        220        230        240 
KPVRIIGVKV HPSQRKDQIL LDLNVSYVGD LQIDVEVKKY FCKAGVKGMQ LHGVLRVILE 

       250        260        270        280        290        300 
PLIGDLPIVG AVSMFFIKRP TLDINWTGMT NLLDIPGLSS LSDTMIMDSI AAFLVLPNRL 

       310        320        330        340        350        360 
LVPLVPDLQD VAQLRSPLPR GIIRIHLLAA RGLSSKDKYV KGLIEGKSDP YALVRVGTQT 

       370        380        390        400        410        420 
FCSRVIDEEL NPHWGETYEV IVHEVPGQEI EVEVFDKDPD KDDFLGRMKL DVGKVLQAGV 

       430        440        450        460        470        480 
LDNWYPLQGG QGQVHLRLEW LSLLPDAEKL DQVLQWNRGI TSRPEPPSAA ILVVYLDRAQ 

       490        500        510        520        530        540 
DLPLKKGNKE PNPMVQLSVQ DVTQESKATY STNCPVWEEA FRFFLQDPRS QELDVQVKDD 

       550        560        570        580        590        600 
SRALTLGALT LPLARLLTAS ELTLDQWFQL SSSGPNSRLY MKLVMRILYL DSSEMRLPTE 

       610        620        630        640        650        660 
PGAQDWDSES PETGSSVDAP PRPYHTTPNS HFGTENVLRI HVLEAQDLIA KDRFLGGLVK 

       670        680        690        700        710        720 
GKSDPYVKLK VAGRSLRTHV VREDLNPRWN EVFEVIVTSI PGQELDIEVF DKDLDKDDFL 

       730        740        750        760        770        780 
GRYKVGLTTV LNSGFLDEWL TLEDVPSGRL HLRLERLSPR PTAAELEEVL QVNSLIQTQK 

       790        800        810        820        830        840 
SSELAAALLS VYLERSEDLP LRKGTKPPSP YAILTVGETS HKTKTVSQTS APIWEESASF 

       850        860        870        880        890        900 
LIRKPHAESL ELQVRGEGTG TLGSISLPLS ELLQEEQLCL DRWFALSGQG QVLMRVQLGI 

       910        920        930        940        950        960 
LVSQHSGVEA HSHSSSSLNE EPEVLGDPTH TASPVLEVRH RLTHGDSPSE ALIGPLGQVK 

       970        980        990       1000       1010       1020 
LTVWYHSDEQ KLISIIHSCR ALRQNGRDLP DPYVSVLLLP DKNRGTKRKT SQKKRTLNPE 

      1030       1040       1050       1060       1070       1080 
FNERFEWDLP LDGTLRRKLD VSVKSNSSFM SRERELLGKV QLDLAEIDLS QGAAQWYDLI 


DDRDKGGS 

« Hide

References

« Hide 'large scale' references
[1]"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], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
[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].
Tissue: Prostate.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF099138 mRNA. Translation: AAD10051.1.
BC101857 mRNA. Translation: AAI01858.1.
RefSeqNP_058945.2. NM_017249.2.
UniGeneRn.11636.

3D structure databases

ProteinModelPortalQ9Z1X1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248212. 2 interactions.
IntActQ9Z1X1. 1 interaction.
MINTMINT-4568934.

PTM databases

PhosphoSiteQ9Z1X1.

Proteomic databases

PaxDbQ9Z1X1.
PRIDEQ9Z1X1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000006119; ENSRNOP00000006119; ENSRNOG00000003909.
GeneID29579.
KEGGrno:29579.
UCSCRGD:3053. rat.

Organism-specific databases

CTD23344.
RGD3053. Esyt1.

Phylogenomic databases

eggNOGCOG5038.
GeneTreeENSGT00550000074417.
HOGENOMHOG000043080.
HOVERGENHBG055795.
InParanoidQ9Z1X1.
OrthoDBEOG7RNJZK.
PhylomeDBQ9Z1X1.
TreeFamTF324255.

Gene expression databases

GenevestigatorQ9Z1X1.

Family and domain databases

Gene3D2.60.40.150. 5 hits.
InterProIPR000008. C2_dom.
[Graphical view]
PfamPF00168. C2. 5 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
SMARTSM00239. C2. 5 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 5 hits.
PROSITEPS50004. C2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio609682.

Entry information

Entry nameESYT1_RAT
AccessionPrimary (citable) accession number: Q9Z1X1
Secondary accession number(s): Q3T1L3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 86 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