Q12466
PR
Gene name |
TCB1 (YOR086C, YOR3141c) |
Protein name |
Tricalbin-1 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YOR086C |
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 Q12466
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q12466-F1 | Predicted | AlphaFoldDB |
18 variants for Q12466
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s15-486513 | 90 | T>S | No | SGRP | |
| s15-486511 | 91 | R>G | No | SGRP | |
| s15-486510 | 91 | R>K | No | SGRP | |
| s15-486496 | 96 | D>N | No | SGRP | |
| s15-486330 | 151 | K>I | No | SGRP | |
| s15-486245 | 179 | L>F | No | SGRP | |
| s15-485751 | 344 | A>D | No | SGRP | |
| s15-484944 | 613 | L>* | No | SGRP | |
| s15-484573 | 737 | L>V | No | SGRP | |
| s15-484526 | 752 | E>D | No | SGRP | |
| s15-484009 | 925 | A>S | No | SGRP | |
| s15-483973 | 937 | V>I | No | SGRP | |
| s15-483753 | 1010 | N>S | No | SGRP | |
| s15-483613 | 1057 | V>F | No | SGRP | |
| s15-483472 | 1104 | Q>K | No | SGRP | |
| s15-483468 | 1105 | D>G | No | SGRP | |
| s15-483279 | 1168 | G>D | No | SGRP | |
| s15-483255 | 1176 | N>S | No | SGRP |
No associated diseases with Q12466
9 regional properties for Q12466
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 366 - 487 | IPR000008-1 |
| domain | C2 domain | 512 - 636 | IPR000008-2 |
| domain | C2 domain | 640 - 757 | IPR000008-3 |
| domain | C2 domain | 976 - 1094 | IPR000008-4 |
| domain | Synaptotagmin-like mitochondrial-lipid-binding domain | 172 - 375 | IPR031468 |
| domain | Tricalbin, C2D domain | 994 - 1110 | IPR037756 |
| domain | Tricalbin, C2A domain | 385 - 508 | IPR037761 |
| domain | Tricalbin, C2C domain | 658 - 778 | IPR037762 |
| domain | Tricalbin, C2B domain | 524 - 642 | IPR037765 |
Functions
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell periphery | The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures. |
| cortical endoplasmic reticulum | A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements. |
| 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. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| lipid binding | Binding to a lipid. |
| metal ion binding | Binding to a metal ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an endoplasmic reticulum membrane. |
| 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. |
| regulation of phosphatidylinositol dephosphorylation | Any process that modulates the frequency, rate or extent of the chemical reaction involving the removal of one or more phosphate groups from a phosphatidylinositol. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAKEDTGVTA | PKKPETAQVA | NINGIDKLEP | PKTKEETESS | KSVSSEKAAH | ASDESFKRSI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HEASYVGWKQ | IGGWEDKDEL | TLDDELMDMT | RETFLDNIIP | DSLYGDWYHS | VAIFFIGGVA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SFALGHYKFS | MGSAFFVIVI | TSLLYRTSAK | KYRGSIRELV | QKEFTVQKVE | NDYESLEWLN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AFLDKYWPIL | EPSVSQLIVQ | QANEQMATNE | AIPKFITQLW | IDELTLGVKP | PRVDLVKTFQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NTASDVVVMD | WGISFTPHDL | CDMSAKQVRN | YVNELAVVKA | KIFGITIPVS | VSDIAFKAHA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RVKFKLMTPF | PHVETVNIQL | LKVPDFDFVA | TLFGRSIFNW | EILAIPGLMT | LIQKMAKKYM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GPILLPPFSL | QLNIPQLLSG | SNLSIGILEI | TVKNAKGLKR | TSSILNESID | PYLSFEFNDI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SIAKTRTVRD | TLNPVWDETL | YVLLNSFTDP | LTISVYDKRA | KLKDKVLGRI | QYNLNTLHDK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TTQRNLKAQF | LRNSKPVGEL | TFDLRFFPTL | EEKKLPDGSV | EELPDLNTGI | AKVVVEEGSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FAEEEQKVTA | YVEVYLNAKL | VLTTGKATDT | GTLKWNSDYE | AVIADRRKTR | YKFVVKDGKG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EEIGSTIQTL | NDLIDRSQVN | KNLIPLKNQK | GDIKITTYWR | PVRLEIGSNS | VAYTPPIGAI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RVFIEKANDL | RNLEKFGTID | PYCKVLVNGL | SKGRTDFKSQ | TLNPVWNQVI | YVAVTSPNQR |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ITLQCMDVET | VNKDRSLGEF | NVNVQDLFKK | DENDKYEETI | DEKAKVGRLV | MPKKKPKGTI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| TYYTSFYPAL | PVLTLEEIQD | LDKVNKKKKA | LELRKSAIDE | KKISKEDKAK | FDQEWNEVKE |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LEDMYSNRQK | LDLPELLQYN | QGVLAVTVLN | GELPDSGLYV | QAFFDDNGHP | RFVSPRIPSR |
| 910 | 920 | 930 | 940 | 950 | 960 |
| IVKNGWSGDV | IIKELDKSIT | TFRVAKNKNY | NRVEKCVCEV | ELPTQELVKN | CYYKPSILHL |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| SGEGSAKLML | QISWFPIDTK | QLPANDLITN | SGDLTIMSRS | AENLIASDLN | GYSDPYLKYY |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| INNEEDCAYK | TKVVKKTLNP | KWNDEGTIQI | NNRLNDVLRI | KVMDWDSTSA | DDTIGTAEIP |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| LNKVKVEGTT | ELDVPVEGLE | NAGQDGGMLH | LAFSFKPRYT | ISVSKREKKV | GDIASKGLGT |
| 1150 | 1160 | 1170 | 1180 | ||
| GLKAGTTVIG | GGVGAIGKIK | KGVFGGLGSL | TNHKKNHEMG | EEETKF |