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

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Cell membrane ; Peripheral membrane protein
  • 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
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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