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Q9Z1X1

- ESYT1_RAT

UniProt

Q9Z1X1 - ESYT1_RAT

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Protein
Extended synaptotagmin-1
Gene
Esyt1, Fam62a, Mbc2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 3 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi336 – 3361Calcium 1; via carbonyl oxygen By similarity
Metal bindingi337 – 3371Calcium 1 By similarity
Metal bindingi337 – 3371Calcium 2 By similarity
Metal bindingi349 – 3491Calcium 2 By similarity
Metal bindingi396 – 3961Calcium 1 By similarity
Metal bindingi396 – 3961Calcium 2 By similarity
Metal bindingi398 – 3981Calcium 1 By similarity
Metal bindingi398 – 3981Calcium 2 By similarity
Metal bindingi398 – 3981Calcium 3; via carbonyl oxygen By similarity
Metal bindingi400 – 4001Calcium 3; via carbonyl oxygen By similarity
Metal bindingi402 – 4021Calcium 3 By similarity
Metal bindingi403 – 4031Calcium 1 By similarity

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: Chromosome 7

Organism-specific databases

RGDi3053. Esyt1.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei31 – 5121Helical; Reviewed prediction
Add
BLAST
Topological domaini52 – 543Lumenal Reviewed prediction
Transmembranei55 – 7521Helical; Reviewed prediction
Add
BLAST
Topological domaini76 – 10881013Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of endoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei316 – 3161Phosphoserine; by CDK5 By similarity
Modified residuei806 – 8061N6-acetyllysine By similarity
Modified residuei809 – 8091Phosphoserine By similarity
Modified residuei947 – 9471Phosphoserine By 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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9Z1X1.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni131 – 305175Glycerophospholipid-binding barrel-like domain By similarity
Add
BLAST
Regioni1002 – 10098Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane By 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.
Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior (By similarity).

Sequence similaritiesi

Contains 5 C2 domains.

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5038.
GeneTreeiENSGT00550000074417.
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

MERSPEEGAG PEPSGQSPAT DSTRERDGGS GVPPAGPGAA SEALAVLTSF     50
GRRLLVLVPV YLAGAAGLSV GFVLFGLALY LGWRRVRDGK ERSLRAARQL 100
LDDEERITAE TLYMSHRELP AWVSFPDVEK AEWLNKIVVQ VWPFLGQYME 150
KLLAETVAPA VRGANPHLQT FTFTRVELGE KPVRIIGVKV HPSQRKDQIL 200
LDLNVSYVGD LQIDVEVKKY FCKAGVKGMQ LHGVLRVILE PLIGDLPIVG 250
AVSMFFIKRP TLDINWTGMT NLLDIPGLSS LSDTMIMDSI AAFLVLPNRL 300
LVPLVPDLQD VAQLRSPLPR GIIRIHLLAA RGLSSKDKYV KGLIEGKSDP 350
YALVRVGTQT FCSRVIDEEL NPHWGETYEV IVHEVPGQEI EVEVFDKDPD 400
KDDFLGRMKL DVGKVLQAGV LDNWYPLQGG QGQVHLRLEW LSLLPDAEKL 450
DQVLQWNRGI TSRPEPPSAA ILVVYLDRAQ DLPLKKGNKE PNPMVQLSVQ 500
DVTQESKATY STNCPVWEEA FRFFLQDPRS QELDVQVKDD SRALTLGALT 550
LPLARLLTAS ELTLDQWFQL SSSGPNSRLY MKLVMRILYL DSSEMRLPTE 600
PGAQDWDSES PETGSSVDAP PRPYHTTPNS HFGTENVLRI HVLEAQDLIA 650
KDRFLGGLVK GKSDPYVKLK VAGRSLRTHV VREDLNPRWN EVFEVIVTSI 700
PGQELDIEVF DKDLDKDDFL GRYKVGLTTV LNSGFLDEWL TLEDVPSGRL 750
HLRLERLSPR PTAAELEEVL QVNSLIQTQK SSELAAALLS VYLERSEDLP 800
LRKGTKPPSP YAILTVGETS HKTKTVSQTS APIWEESASF LIRKPHAESL 850
ELQVRGEGTG TLGSISLPLS ELLQEEQLCL DRWFALSGQG QVLMRVQLGI 900
LVSQHSGVEA HSHSSSSLNE EPEVLGDPTH TASPVLEVRH RLTHGDSPSE 950
ALIGPLGQVK LTVWYHSDEQ KLISIIHSCR ALRQNGRDLP DPYVSVLLLP 1000
DKNRGTKRKT SQKKRTLNPE FNERFEWDLP LDGTLRRKLD VSVKSNSSFM 1050
SRERELLGKV QLDLAEIDLS QGAAQWYDLI DDRDKGGS 1088
Length:1,088
Mass (Da):121,159
Last modified:May 1, 1999 - v1
Checksum:iE7E12D9737FFB89D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti373 – 3731H → R in AAI01858. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF099138 mRNA. Translation: AAD10051.1.
BC101857 mRNA. Translation: AAI01858.1.
RefSeqiNP_058945.2. NM_017249.2.
UniGeneiRn.11636.

Genome annotation databases

EnsembliENSRNOT00000006119; ENSRNOP00000006119; ENSRNOG00000003909.
GeneIDi29579.
KEGGirno:29579.
UCSCiRGD:3053. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF099138 mRNA. Translation: AAD10051.1 .
BC101857 mRNA. Translation: AAI01858.1 .
RefSeqi NP_058945.2. NM_017249.2.
UniGenei Rn.11636.

3D structure databases

ProteinModelPortali Q9Z1X1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248212. 2 interactions.
IntActi Q9Z1X1. 1 interaction.
MINTi MINT-4568934.

PTM databases

PhosphoSitei Q9Z1X1.

Proteomic databases

PaxDbi Q9Z1X1.
PRIDEi Q9Z1X1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000006119 ; ENSRNOP00000006119 ; ENSRNOG00000003909 .
GeneIDi 29579.
KEGGi rno:29579.
UCSCi RGD:3053. rat.

Organism-specific databases

CTDi 23344.
RGDi 3053. Esyt1.

Phylogenomic databases

eggNOGi COG5038.
GeneTreei ENSGT00550000074417.
HOGENOMi HOG000043080.
HOVERGENi HBG055795.
InParanoidi Q9Z1X1.
OrthoDBi EOG7RNJZK.
PhylomeDBi Q9Z1X1.
TreeFami TF324255.

Miscellaneous databases

NextBioi 609682.

Gene expression databases

Genevestigatori Q9Z1X1.

Family and domain databases

Gene3Di 2.60.40.150. 5 hits.
InterProi IPR000008. C2_dom.
[Graphical view ]
Pfami PF00168. C2. 5 hits.
[Graphical view ]
PRINTSi PR00360. C2DOMAIN.
SMARTi SM00239. C2. 5 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 5 hits.
PROSITEi PS50004. C2. 4 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 87 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

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