Q3U7R1
Gene name |
Esyt1 (Fam62a, Mbc2) |
Protein name |
Extended synaptotagmin-1 |
Names |
E-Syt1, Membrane-bound C2 domain-containing protein |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:23943 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q3U7R1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3U7R1-F1 | Predicted | AlphaFoldDB |
61 variants for Q3U7R1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389099261 | 3 | H>Y | No | EVA | |
| rs3389137690 | 41 | A>T | No | EVA | |
| rs3389135202 | 52 | L>F | No | EVA | |
| rs3389146606 | 72 | L>I | No | EVA | |
| rs3402037922 | 82 | R>H | No | EVA | |
| rs3389146585 | 95 | A>T | No | EVA | |
| rs3389145701 | 96 | R>M | No | EVA | |
| rs3389135219 | 125 | D>N | No | EVA | |
| rs3389145709 | 148 | E>D | No | EVA | |
| rs3389131130 | 161 | G>E | No | EVA | |
| rs3413119018 | 182 | R>Q | No | EVA | |
| rs3411699068 | 195 | D>E | No | EVA | |
| rs3389107991 | 198 | L>M | No | EVA | |
| rs3401834546 | 213 | V>M | No | EVA | |
| rs3389146611 | 217 | K>* | No | EVA | |
| rs3389137522 | 223 | G>* | No | EVA | |
| rs3389099301 | 251 | S>Y | No | EVA | |
| rs3389137679 | 258 | P>L | No | EVA | |
| rs3389131195 | 262 | I>M | No | EVA | |
| rs3389107966 | 286 | D>V | No | EVA | |
| rs3389137661 | 318 | R>K | No | EVA | |
| rs3389122506 | 325 | L>Q | No | EVA | |
| rs3389145779 | 350 | A>G | No | EVA | |
| rs3389135200 | 413 | V>A | No | EVA | |
| rs3411699071 | 413 | V>I | No | EVA | |
| rs3389075157 | 461 | R>Q | No | EVA | |
| rs3389135222 | 464 | P>T | No | EVA | |
| rs3389107994 | 470 | L>V | No | EVA | |
| rs3389111009 | 488 | E>K | No | EVA | |
| rs3389145758 | 502 | R>L | No | EVA | |
| rs3389122482 | 516 | E>* | No | EVA | |
| rs3389107950 | 535 | V>L | No | EVA | |
| rs3413032925 | 546 | A>T | No | EVA | |
| rs3389075100 | 553 | R>H | No | EVA | |
| rs31472264 | 572 | G>S | No | EVA | |
| rs3389133925 | 605 | D>N | No | EVA | |
| rs3389139968 | 637 | R>L | No | EVA | |
| rs3389075093 | 673 | S>G | No | EVA | |
| rs264799167 | 673 | S>R | No | EVA | |
| rs3389140055 | 690 | V>F | No | EVA | |
| rs3389075133 | 691 | F>L | No | EVA | |
| rs3389137672 | 759 | P>L | No | EVA | |
| rs3401173616 | 783 | A>V | No | EVA | |
| rs3389139999 | 790 | F>S | No | EVA | |
| rs3389110979 | 801 | K>N | No | EVA | |
| rs236750611 | 805 | P>T | No | EVA | |
| rs3389122469 | 842 | K>R | No | EVA | |
| rs3402037913 | 881 | W>* | No | EVA | |
| rs3389131182 | 881 | W>R | No | EVA | |
| rs3389135974 | 953 | S>A | No | EVA | |
| rs3389129441 | 965 | L>V | No | EVA | |
| rs3401877195 | 966 | T>S | No | EVA | |
| rs3401774059 | 967 | V>L | No | EVA | |
| rs3389129450 | 975 | K>R | No | EVA | |
| rs3389137478 | 1016 | Q>H | No | EVA | |
| rs3389137461 | 1021 | L>R | No | EVA | |
| rs3389137503 | 1026 | N>K | No | EVA | |
| rs3389131198 | 1050 | N>K | No | EVA | |
| rs3389144390 | 1052 | S>T | No | EVA | |
| rs3389146627 | 1064 | V>L | No | EVA | |
| rs3389075149 | 1067 | D>V | No | EVA |
No associated diseases with Q3U7R1
12 regional properties for Q3U7R1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 302 - 425 | IPR000008-1 |
| domain | C2 domain | 444 - 570 | IPR000008-2 |
| domain | C2 domain | 616 - 740 | IPR000008-3 |
| domain | C2 domain | 769 - 886 | IPR000008-4 |
| domain | C2 domain | 959 - 1083 | IPR000008-5 |
| domain | Synaptotagmin-like mitochondrial-lipid-binding domain | 125 - 303 | IPR031468 |
| domain | Extended synaptotagmin, C2A domain | 319 - 438 | IPR037733-1 |
| domain | Extended synaptotagmin, C2A domain | 635 - 753 | IPR037733-2 |
| domain | Extended synaptotagmin, C2B domain | 469 - 573 | IPR037749-1 |
| domain | Extended synaptotagmin, C2B domain | 786 - 888 | IPR037749-2 |
| domain | Extended synaptotagmin, C-terminal C2 domain | 959 - 1084 | IPR037752 |
| domain | Synaptotagmin, SMP domain | 125 - 303 | IPR039010 |
Functions
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| extrinsic component of cytoplasmic side of plasma membrane | The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to its cytoplasmic surface, but not integrated into the hydrophobic region. |
| integral component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| intrinsic component of endoplasmic reticulum membrane | The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having either part of their peptide sequence embedded in the hydrophobic region of the membrane or some other covalently attached group such as a GPI anchor that is similarly embedded in the membrane. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium. |
| identical protein binding | Binding to an identical protein or proteins. |
| phosphatidylcholine binding | Binding to a phosphatidylcholine, a glycophospholipid in which a phosphatidyl group is esterified to the hydroxyl group of choline. |
| phosphatidylethanolamine binding | Binding to a phosphatidylethanolamine, a class of glycerophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of ethanolamine. |
| phosphatidylinositol binding | Binding to an inositol-containing glycerophospholipid, i.e. phosphatidylinositol (PtdIns) and its phosphorylated derivatives. |
| phospholipid transfer activity | Removes a phospholipid from a membrane or a monolayer lipid particle, transports it through the aqueous phase while protected in a hydrophobic pocket, and brings it to an acceptor membrane or lipid particle. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| endoplasmic reticulum-plasma membrane tethering | The attachment of an endoplasmic reticulum membrane to the plasma membrane via molecular tethers. |
| intermembrane lipid transfer | The transport of lipids between membranes in which a lipid molecule is transported through an aqueous phase from the outer leaflet of a donor membrane to the outer leaflet of an acceptor membrane. This process does not require metabolic energy and can be either spontaneous or mediated by lipid transfer proteins (LTPs). |
6 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9BSJ8 | ESYT1 | Extended synaptotagmin-1 | Homo sapiens (Human) | PR |
| Q3TZZ7 | Esyt2 | Extended synaptotagmin-2 | Mus musculus (Mouse) | PR |
| B6ETT4 | SYT2 | Synaptotagmin-2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| A0JJX5 | SYT4 | Synaptotagmin-4 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q7XA06 | SYT3 | Synaptotagmin-3 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9SKR2 | SYT1 | Synaptotagmin-1 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEHSPEEGAS | PEPSGQPPAT | DSTRDGGSGV | PPAGPGAASE | ALAVLTSFGR | RLLVLVPVYL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGAAGLSVGF | VLFGLALYLG | WRRVRDGKER | SLRAARQLLD | DEERITAETL | YMSHRELPAW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VSFPDVEKAE | WLNKIVAQVW | PFLGQYMEKL | LAETVAPAVR | GANPHLQTFT | FTRVELGEKP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LRIIGVKVHP | SQRKDQILLD | LNVSYVGDVQ | IDVEVKKYFC | KAGVKGMQLH | GVLRVILEPL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TGDLPIVGAV | SMFFIKRPTL | DINWTGMTNL | LDIPGLSSLS | DTMIMDSIAA | FLVLPNRLLV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLVPDLQDVA | QLRSPLPRGI | IRIHLLAARG | LSSKDKYVKG | LIEGKSDPYA | LVRVGTQTFC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SRVIDEELNP | HWGETYEVIV | HEVPGQEIEV | EVFDKDPDKD | DFLGRMKLDV | GKVLQAGVLD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NWYPLQGGQG | QVHLRLEWLS | LLPDAEKLDQ | VLQWNRGITS | RPEPPSAAIL | VVYLDRAQDL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| PLKKGNKEPN | PMVQLSVQDV | TRESKATYST | NSPVWEEAFR | FFLQDPRSQE | LDVQVKDDSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ALTLGALTLP | LARLLTASEL | TLDQWFQLSS | SGPNSRLYMK | LVMRILYLDY | SEIRFPTVPG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AQDWDRESLE | TGSSVDAPPR | PYHTTPNSHF | GTENVLRIHV | LEAQDLIAKD | RFLGGLVKGK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SDPYVKLKVA | GKSFRTHVVR | EDLNPRWNEV | FEVIVTSIPG | QELEIEVFDK | DLDKDDFLGR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| YKVSLTTVLN | SGFLDEWLTL | EDVPSGRLHL | RLERLTPRPT | AAELEEVLQV | NSLIQTQKSS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ELAAALLSVF | LERAEDLPLR | KGTKPPSPYA | TITVGETSHK | TKTVSQSSAP | VWEESASFLI |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RKPHAESLEL | QVRGEGTGTL | GSVSLPLSEL | LQEDQLCLDH | WFALSGQGQV | LMRAQLGILV |
| 910 | 920 | 930 | 940 | 950 | 960 |
| SQHSGVEAHS | HSYSHSHSSS | SLNDEPEALG | GPTHPASPVL | EVRHRLTHGD | SPSEAPVGPL |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| GQVKLTVWYH | SDEQKLISII | HSCRALRQNG | RDLPDPYVSV | LLLPDKNRST | KRKTPQKKRT |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| LNPEFNERFE | WDLPLDGTLR | RKLDVSVKSN | SSFMSREREL | LGKVQLDLAE | IDLSQGAAQW |
| 1090 | |||||
| YDLMDDRDKG | GS |