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 Q80TT2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q80TT2-F1 | Predicted | AlphaFoldDB |
53 variants for Q80TT2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389443309 | 11 | V>E | No | EVA | |
| rs3389392672 | 32 | T>I | No | EVA | |
| rs3406598481 | 62 | D>H | No | EVA | |
| rs3389412023 | 83 | E>D | No | EVA | |
| rs3389412008 | 123 | D>N | No | EVA | |
| rs3412872411 | 136 | F>* | No | EVA | |
| rs3405724129 | 136 | F>L | No | EVA | |
| rs3389435273 | 150 | V>M | No | EVA | |
| rs33265719 | 197 | P>S | No | EVA | |
| rs3389411966 | 204 | R>P | No | EVA | |
| rs3389449835 | 227 | V>L | No | EVA | |
| rs3389422510 | 282 | T>I | No | EVA | |
| rs3389449839 | 342 | D>Y | No | EVA | |
| rs33773684 | 359 | S>N | No | EVA | |
| rs3389355700 | 368 | S>F | No | EVA | |
| rs3389411980 | 383 | V>E | No | EVA | |
| rs33773686 | 391 | W>G | No | EVA | |
| rs3389436638 | 426 | S>I | No | EVA | |
| rs3406524784 | 442 | L>Q* | No | EVA | |
| rs3389445620 | 449 | H>R | No | EVA | |
| rs3389442226 | 468 | F>L | No | EVA | |
| rs3389355677 | 482 | L>F | No | EVA | |
| rs3389443350 | 484 | D>N | No | EVA | |
| rs3389435502 | 536 | R>H | No | EVA | |
| rs3389442175 | 544 | N>T | No | EVA | |
| rs3389435232 | 545 | T>I | No | EVA | |
| rs3389403396 | 550 | E>K | No | EVA | |
| rs3413042379 | 568 | Y>S | No | EVA | |
| rs3389453896 | 662 | L>G | No | EVA | |
| rs3389459525 | 685 | A>N | No | EVA | |
| rs3389411979 | 695 | Q>I | No | EVA | |
| rs3389435257 | 698 | W>N | No | EVA | |
| rs3389421453 | 731 | L>K | No | EVA | |
| rs3389459506 | 800 | H>I | No | EVA | |
| rs3389411945 | 810 | L>S | No | EVA | |
| rs3411969401 | 836 | E>N | No | EVA | |
| rs241141244 | 838 | V>V | No | EVA | |
| rs3389459502 | 861 | L>R | No | EVA | |
| rs3389453932 | 867 | A>V | No | EVA | |
| rs3407565297 | 879 | A>S | No | EVA | |
| rs3389442188 | 909 | G>H | No | EVA | |
| rs3389421422 | 927 | E>R | No | EVA | |
| rs3389421448 | 928 | E>M | No | EVA | |
| rs3389355711 | 958 | F>H | No | EVA | |
| rs3389435493 | 978 | V>N | No | EVA | |
| rs3389392676 | 984 | L>V | No | EVA | |
| rs3389403455 | 991 | G>D | No | EVA | |
| rs3389442181 | 999 | V>G | No | EVA | |
| rs3389459513 | 1061 | F>Y | No | EVA | |
| rs3389421417 | 1080 | V>K | No | EVA | |
| rs3389421477 | 1102 | R>S | No | EVA | |
| rs3389443391 | 1121 | K>V | No | EVA | |
| rs3389453917 | 1130 | M>K | No | EVA |
No associated diseases with Q80TT2
4 regional properties for Q80TT2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Bicarbonate transporter-like, transmembrane domain | 680 - 1168 | IPR011531 |
| domain | Band 3 cytoplasmic domain | 352 - 619 | IPR013769 |
| conserved_site | Anion exchange, conserved site | 682 - 693 | IPR018241-1 |
| conserved_site | Anion exchange, conserved site | 829 - 843 | IPR018241-2 |
Functions
8 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| GABA-ergic synapse | A synapse that uses GABA as a neurotransmitter. These synapses are typically inhibitory. |
| late endosome membrane | The lipid bilayer surrounding a late endosome. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| presynapse | The part of a synapse that is part of the presynaptic cell. |
| recycling endosome membrane | The lipid bilayer surrounding a recycling endosome. |
| secretory vesicle | A cytoplasmic, membrane bound vesicle that is capable of fusing to the plasma membrane to release its contents into the extracellular space. |
| trans-Golgi network membrane | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. |
| SNARE binding | Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein. |
| syntaxin binding | Binding to a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| dense core granule maturation | Steps required to transform a dense core granule generated at the trans-Golgi network into a fully formed and transmissible dense core granule. Dense core granule maturation proceeds through clathrin-mediated membrane remodeling events and is essential for efficient processing of cargo within dense core granules as well as for removing factors that might otherwise interfere with dense core granule trafficking and exocytosis. |
| exocytosis | A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell. |
| G protein-coupled receptor signaling pathway | The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane. |
| modulation of chemical synaptic transmission | Any process that modulates the frequency or amplitude of synaptic transmission, the process of communication from a neuron to a target (neuron, muscle, or secretory cell) across a synapse. Amplitude, in this case, refers to the change in postsynaptic membrane potential due to a single instance of synaptic transmission. |
| positive regulation of insulin secretion involved in cellular response to glucose stimulus | Any process that increases the frequency, rate or extent of the regulated release of insulin that contributes to the response of a cell to glucose. |
| positive regulation of neurotransmitter secretion | Any process that activates or increases the frequency, rate or extent of the regulated release of a neurotransmitter. |
| regulation of behavior | Any process that modulates the frequency, rate or extent of behavior, the internally coordinated responses (actions or inactions) of whole living organisms (individuals or groups) to internal or external stimuli. |
| regulation of dense core granule exocytosis | Any process that modulates the frequency, rate or extent of dense core granule exocytosis. |
| regulation of synaptic transmission, GABAergic | Any process that modulates the frequency, rate or extent of GABAergic synaptic transmission, the process of communication from a neuron to another neuron across a synapse using the neurotransmitter gamma-aminobutyric acid (GABA). |
| retrograde transport, endosome to Golgi | The directed movement of membrane-bounded vesicles from endosomes back to the trans-Golgi network where they are recycled for further rounds of transport. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTLLDIKSS | VLRQVQVCPS | FRRKTEQEPE | VTNSQEPPTG | AWKPGDGVEF | FAHMRLILKK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GDGRQGLPCP | EVLLRSGSPA | PAEPVDPNRG | LRTLTQEEVE | MLYEEALYTV | LHRAGTMGPD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QVDDEEVLLS | YLQQVFGTSS | EEHMEAIMRV | KKAKAPTYAL | KVSVMRAKNL | LAKDPNGFSD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PYCMLGILPA | SSAPQEPSGQ | KEQRFGFRKG | SKRSSPLPAK | CIQVTEVKNS | TLNPVWKEHF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LFEIDDVNTD | QLHLDIWDHD | DDVSLAEACR | KLNEVIGLKG | MTRYFKQIVK | SARANGTAGP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TEDHTDDFLG | CLNIPIREVP | VAGADRWFKL | EPRSSASRVQ | GDCHLVLKLI | TTQRDTVMSQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RGRSGFLSYL | LLLSRVLRFE | HRVEEPNSSS | WRGELSGPGT | TVLCLHGAQS | NLSPLQLAVL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HWQVSSRHHQ | TRTLDYGYLL | GLLEDVQAHW | EEAASLPQEQ | EESLADSFSA | FSEFGLRLLR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QLRDYFPATN | STAVYRLELL | LKCLEKLQLF | QPAFEICPFE | TELSMDIAAA | LKRGNREWYD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QLLNTKSPRE | QPGPQRLAGL | VELADIIYED | LQLCYGVYAS | LFHGQVAEEA | WVLTEELSPK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MNLEVASGLF | ELYLTLADTQ | RFWSCIPGRE | SRSLALAGIH | TPFLPAVKLW | LQVLRDQAKW |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RLQGAVDVDT | LEPVDAASKH | SSSAATASLC | LSHIQELWVR | LAWPDPSQAQ | GLGTQLSQDM |
| 730 | 740 | 750 | 760 | 770 | 780 |
| CEASLFYTEL | LRKKVDTQPG | AAGEAVSEQL | CVVLNNVELV | RRASGQALRG | LAWSEGASGL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EGVLPRPLLS | CIQALDEDLH | REAHTVTAHL | TSKMVADIRK | YIQHISLSPD | SIQNDEAVAP |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LLKYLDEKLA | LLNDALVKEN | LNRVLEALWE | LLLQAILQAL | SANRDVSADF | YGRFHFTLEA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LVSFFHAEGQ | GLPLENLRDG | SYKRLQEELR | LHKCSTRECI | EQFYLDKLKQ | RSLEQNRFGR |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| LTVRCHYEAA | EQRLAVEVLH | AADLLPLDAN | GLSDPFVIVE | LGPPHLFPLV | RSQRTQVKAR |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| TLHPVYDELF | HFSVPAEACR | RRGACVLFTV | MDHDWLSTND | FAGEAALGLG | GISGIARPHV |
| 1090 | 1100 | 1110 | 1120 | 1130 | |
| GGGMRPGQPI | TLHLRRPRAQ | VRSALRMLEG | RTSREAQEFV | KKLKELEKCM | EADL |