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 Q9UT00

Entry ID Method Resolution Chain Position Source
AF-Q9UT00-F1 Predicted AlphaFoldDB

17 variants for Q9UT00

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2906892_T_G 52 N>T No Jeffares_SNPs
I_2906856_T_C 64 Q>R No Jeffares_SNPs
I_2906765_G_T 94 D>E No Jeffares_SNPs
I_2906316_G_A 244 T>M No Jeffares_SNPs
I_2906272_T_C 259 I>V No Jeffares_SNPs
I_2905996_C_T 351 V>I No Jeffares_SNPs
I_2905890_C_T 386 G>D No Jeffares_SNPs
I_2905660_T_C 463 N>D No Jeffares_SNPs
I_2905650_T_C 466 D>G No Jeffares_SNPs
I_2905278_C_T 590 R>Q No Jeffares_SNPs
I_2904942_G_A 702 P>L No Jeffares_SNPs
I_2904943_G_A 702 P>S No Jeffares_SNPs
I_2904681_T_C 789 N>S No Jeffares_SNPs
I_2904610_C_T 813 V>I No Jeffares_SNPs
I_2904597_G_A 817 S>F No Jeffares_SNPs
I_2904460_T_C 863 I>V No Jeffares_SNPs
I_2904262_G_A 929 P>S No Jeffares_SNPs

No associated diseases with Q9UT00

9 regional properties for Q9UT00

Type Name Position InterPro Accession
domain C2 domain 413 - 534 IPR000008-1
domain C2 domain 559 - 670 IPR000008-2
domain C2 domain 685 - 803 IPR000008-3
domain C2 domain 1019 - 1138 IPR000008-4
domain Synaptotagmin-like mitochondrial-lipid-binding domain 217 - 422 IPR031468
domain Tricalbin, C2D domain 1039 - 1153 IPR037756
domain Tricalbin, C2A domain 434 - 555 IPR037761
domain Tricalbin, C2C domain 704 - 823 IPR037762
domain Tricalbin, C2B domain 581 - 686 IPR037765

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
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).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a 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.
plasma membrane of cell tip The portion of the plasma membrane surrounding the cell tip.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
protein-membrane adaptor activity The binding activity of a molecule that brings together a protein or a protein complex with a membrane, or bringing together two membranes, either via membrane lipid binding or by interacting with a membrane protein, to establish or maintain the localization of the protein, protein complex or organelle.

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.
lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSSQAEPSKG ASNADPNEKV EKMHLPTDTA GGGVKVKVKE QEASPSDKNN LNPQSAGVSE
70 80 90 100 110 120
VQVQDDTGAR GSGARDLKVP KQMQAPKSSE EKSDVDGVPT RPVSERELRK RDAMQFIQRH
130 140 150 160 170 180
QKVRNILAQY CPWLTDERLQ LCIELKILFM QHFQDSRLVL YTAVMSFLFG YLRFGFLSLF
190 200 210 220 230 240
IIMAVCIQYY RICDRRVKVN FKDDYTRYLS TRKLENDSET VTWLNTFLQQ FWYIFEPSLS
250 260 270 280 290 300
ERITEITDQI LSENVPSFID SMALSEFTLG TKSPRMGFIR SYPKTEEDTV MMDLRLAFSP
310 320 330 340 350 360
NDISDLTGRE IAACIKPKIA LDLKIGKSIA SAKMPVLIED LSFTGNLRVK VKLIDKYPYA
370 380 390 400 410 420
KTVGLTFTEK PVFSYILKPL GGDKFGFDIG NIPGLTTFIT EQIHNTLGPM MYSPNVYELD
430 440 450 460 470 480
IESMMGAAGL NTALGAVEFK LRKGDGFKDG LGGAVDPYVV IKNSADRVIG KSKVAHNTGS
490 500 510 520 530 540
PVFNETFYSV LNSFSENLNL EVYDFNDIRS DKLLGSAVLP LATLEAMPVT NDAFVELTLK
550 560 570 580 590 600
GKTVGRLNYD MKFHAVVPDS GEEITKVDGP GVLQFTVHQC KELSNDPSKR PTAYAKLIIN
610 620 630 640 650 660
NKEVYTTRKI KKNNNPSWEE SFGTLLPEGK NATLGVQIFT EESEHPFGTA NVSLQDLFAA
670 680 690 700 710 720
TKTGLLWFPL QHAPSGRVRM SVMWKPAQLN NDSISSMALA TPIGAIRIHL RSANNLHSKI
730 740 750 760 770 780
PGKKCDSYAR IMSHNTKQFR TVVIASNVNP FWDEYMYAPV ITKHDIFFLQ VMNYNSSGED
790 800 810 820 830 840
KLIGQTPINI SNFINQGENG ALMEYHDPRE LTVPLSSTRG IKGNATITFK CDFFPSAVTT
850 860 870 880 890 900
SLSPDVTPAP KASSTVATDK VNIEVLPESQ KTPTAVDNTS TSRGSTSVKT SKPKKISELL
910 920 930 940 950 960
MPSEAVNAAL DFESGFMGFD IISYKIAKPA QELAIFLDDL PHHIFLSSAL NVTGGATLHE
970 980 990 1000 1010 1020
YGNTFIRQLE YSQCTFKLLD GDKEVGSKTM LSRDLISKGA TKPLEIAFPD GASILVAFRL
1030 1040 1050 1060 1070 1080
TPVPVKLEEV EMYENMGEMT VDVIKATDLP AADSNGKSDP FVVFELQGEE VYRTKTHKRT
1090 1100 1110 1120 1130 1140
LNPTFNESFE VELPCKQTCN FVANVFDWDF GNKDDHLGSC VIDCKLLQQQ QQTNYEIPLD
1150 1160 1170 1180 1190 1200
SKQGVLYLRI TLSPKWVLRS KRAGNSSLVE GILGQTASIV GMPLKGISTV GNVAVDGVAS
1210 1220
VANLTNKMRK GISRGFKGIH HEKAK