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Protein

Extended synaptotagmin-1

Gene

Esyt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 bindingi336 – 3361Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi337 – 3371Calcium 1By similarity
Metal bindingi337 – 3371Calcium 2By similarity
Metal bindingi349 – 3491Calcium 2By similarity
Metal bindingi396 – 3961Calcium 1By similarity
Metal bindingi396 – 3961Calcium 2By similarity
Metal bindingi398 – 3981Calcium 1By similarity
Metal bindingi398 – 3981Calcium 2By similarity
Metal bindingi398 – 3981Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi400 – 4001Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi402 – 4021Calcium 3By similarity
Metal bindingi403 – 4031Calcium 1By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phospholipid binding Source: GO_Central

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
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
vp115
Gene namesi
Name:Esyt1
Synonyms:Fam62a, Mbc2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3053. Esyt1.

Subcellular locationi

  1. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity
  2. Cell membrane By similarity; Peripheral membrane protein By similarity

  3. 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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei31 – 5121HelicalSequence AnalysisAdd
BLAST
Topological domaini52 – 543LumenalSequence Analysis
Transmembranei55 – 7521HelicalSequence AnalysisAdd
BLAST
Topological domaini76 – 10881013CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of endoplasmic reticulum membrane Source: UniProtKB
  2. intrinsic component of endoplasmic reticulum membrane Source: GO_Central
  3. organelle membrane contact site Source: GO_Central
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10881088Extended synaptotagmin-1PRO_0000234347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei316 – 3161Phosphoserine; by CDK5By similarity
Modified residuei806 – 8061N6-acetyllysineBy similarity
Modified residuei809 – 8091PhosphoserineBy similarity
Modified residuei933 – 9331PhosphoserineBy similarity
Modified residuei947 – 9471PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z1X1.
PRIDEiQ9Z1X1.

PTM databases

PhosphoSiteiQ9Z1X1.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ9Z1X1.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi248212. 2 interactions.
IntActiQ9Z1X1. 1 interaction.
MINTiMINT-4568934.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1X1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini308 – 409102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini457 – 55094C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini623 – 724102C2 3PROSITE-ProRule annotationAdd
BLAST
Domaini774 – 86693C2 4PROSITE-ProRule annotationAdd
BLAST
Domaini956 – 1061106C2 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 305175Glycerophospholipid-binding barrel-like domainBy similarityAdd
BLAST
Regioni1002 – 10098Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membraneBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi912 – 9176Poly-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 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

eggNOGiCOG5038.
HOGENOMiHOG000043080.
HOVERGENiHBG055795.
InParanoidiQ9Z1X1.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ9Z1X1.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
[Graphical view]
PfamiPF00168. C2. 5 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1X1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSPEEGAG PEPSGQSPAT DSTRERDGGS GVPPAGPGAA SEALAVLTSF
60 70 80 90 100
GRRLLVLVPV YLAGAAGLSV GFVLFGLALY LGWRRVRDGK ERSLRAARQL
110 120 130 140 150
LDDEERITAE TLYMSHRELP AWVSFPDVEK AEWLNKIVVQ VWPFLGQYME
160 170 180 190 200
KLLAETVAPA VRGANPHLQT FTFTRVELGE KPVRIIGVKV HPSQRKDQIL
210 220 230 240 250
LDLNVSYVGD LQIDVEVKKY FCKAGVKGMQ LHGVLRVILE PLIGDLPIVG
260 270 280 290 300
AVSMFFIKRP TLDINWTGMT NLLDIPGLSS LSDTMIMDSI AAFLVLPNRL
310 320 330 340 350
LVPLVPDLQD VAQLRSPLPR GIIRIHLLAA RGLSSKDKYV KGLIEGKSDP
360 370 380 390 400
YALVRVGTQT FCSRVIDEEL NPHWGETYEV IVHEVPGQEI EVEVFDKDPD
410 420 430 440 450
KDDFLGRMKL DVGKVLQAGV LDNWYPLQGG QGQVHLRLEW LSLLPDAEKL
460 470 480 490 500
DQVLQWNRGI TSRPEPPSAA ILVVYLDRAQ DLPLKKGNKE PNPMVQLSVQ
510 520 530 540 550
DVTQESKATY STNCPVWEEA FRFFLQDPRS QELDVQVKDD SRALTLGALT
560 570 580 590 600
LPLARLLTAS ELTLDQWFQL SSSGPNSRLY MKLVMRILYL DSSEMRLPTE
610 620 630 640 650
PGAQDWDSES PETGSSVDAP PRPYHTTPNS HFGTENVLRI HVLEAQDLIA
660 670 680 690 700
KDRFLGGLVK GKSDPYVKLK VAGRSLRTHV VREDLNPRWN EVFEVIVTSI
710 720 730 740 750
PGQELDIEVF DKDLDKDDFL GRYKVGLTTV LNSGFLDEWL TLEDVPSGRL
760 770 780 790 800
HLRLERLSPR PTAAELEEVL QVNSLIQTQK SSELAAALLS VYLERSEDLP
810 820 830 840 850
LRKGTKPPSP YAILTVGETS HKTKTVSQTS APIWEESASF LIRKPHAESL
860 870 880 890 900
ELQVRGEGTG TLGSISLPLS ELLQEEQLCL DRWFALSGQG QVLMRVQLGI
910 920 930 940 950
LVSQHSGVEA HSHSSSSLNE EPEVLGDPTH TASPVLEVRH RLTHGDSPSE
960 970 980 990 1000
ALIGPLGQVK LTVWYHSDEQ KLISIIHSCR ALRQNGRDLP DPYVSVLLLP
1010 1020 1030 1040 1050
DKNRGTKRKT SQKKRTLNPE FNERFEWDLP LDGTLRRKLD VSVKSNSSFM
1060 1070 1080
SRERELLGKV QLDLAEIDLS QGAAQWYDLI DDRDKGGS
Length:1,088
Mass (Da):121,159
Last modified:May 1, 1999 - v1
Checksum:iE7E12D9737FFB89D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3731H → R in AAI01858 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099138 mRNA. Translation: AAD10051.1.
BC101857 mRNA. Translation: AAI01858.1.
RefSeqiNP_058945.2. NM_017249.2.
UniGeneiRn.11636.

Genome annotation databases

GeneIDi29579.
KEGGirno:29579.
UCSCiRGD:3053. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099138 mRNA. Translation: AAD10051.1.
BC101857 mRNA. Translation: AAI01858.1.
RefSeqiNP_058945.2. NM_017249.2.
UniGeneiRn.11636.

3D structure databases

ProteinModelPortaliQ9Z1X1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248212. 2 interactions.
IntActiQ9Z1X1. 1 interaction.
MINTiMINT-4568934.

PTM databases

PhosphoSiteiQ9Z1X1.

Proteomic databases

PaxDbiQ9Z1X1.
PRIDEiQ9Z1X1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29579.
KEGGirno:29579.
UCSCiRGD:3053. rat.

Organism-specific databases

CTDi23344.
RGDi3053. Esyt1.

Phylogenomic databases

eggNOGiCOG5038.
HOGENOMiHOG000043080.
HOVERGENiHBG055795.
InParanoidiQ9Z1X1.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ9Z1X1.
TreeFamiTF324255.

Miscellaneous databases

NextBioi609682.
PROiQ9Z1X1.

Gene expression databases

GenevestigatoriQ9Z1X1.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
[Graphical view]
PfamiPF00168. C2. 5 hits.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiESYT1_RAT
AccessioniPrimary (citable) accession number: Q9Z1X1
Secondary accession number(s): Q3T1L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 93 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.