Q8K0T7
Gene name |
Unc13c |
Protein name |
Protein unc-13 homolog C |
Names |
Munc13-3 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:208898 |
EC number |
|
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
1535-2024 (MUN domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
1535-2024 (MUN domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
1535-2024 (MUN domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q8K0T7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8K0T7-F1 | Predicted | AlphaFoldDB |
107 variants for Q8K0T7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs32919647 | 4 | S>N | No | EVA | |
| rs3400341522 | 13 | Y>VYKLKSSS* | No | EVA | |
| rs3399804563 | 14 | I>V | No | EVA | |
| rs3400433641 | 15 | H>Y | No | EVA | |
| rs3389058967 | 29 | T>R | No | EVA | |
| rs237975954 | 39 | K>Q | No | EVA | |
| rs3389056533 | 64 | K>R | No | EVA | |
| rs3389056347 | 71 | S>F | No | EVA | |
| rs3389045689 | 74 | N>Y | No | EVA | |
| rs3400256889 | 108 | N>D | No | EVA | |
| rs3389038588 | 176 | G>D | No | EVA | |
| rs3389025263 | 215 | A>T | No | EVA | |
| rs3389066384 | 244 | F>C | No | EVA | |
| rs3389061109 | 261 | R>L | No | EVA | |
| rs3389056527 | 275 | S>F | No | EVA | |
| rs3389065327 | 315 | K>T | No | EVA | |
| rs3389058127 | 338 | I>F | No | EVA | |
| rs29938276 | 354 | I>M | No | EVA | |
| rs3413072033 | 357 | A>T | No | EVA | |
| rs3389052928 | 402 | S>Y | No | EVA | |
| rs3389003469 | 408 | Y>F | No | EVA | |
| rs3389065367 | 408 | Y>H | No | EVA | |
| rs3389056313 | 412 | E>K | No | EVA | |
| rs3389065388 | 453 | E>K | No | EVA | |
| rs3389058183 | 498 | D>Y | No | EVA | |
| rs3547336637 | 502 | R>P | No | EVA | |
| rs3389066324 | 522 | A>T | No | EVA | |
| rs32916913 | 536 | L>P | No | EVA | |
| rs3389052904 | 559 | S>N | No | EVA | |
| rs3389065373 | 560 | Q>K | No | EVA | |
| rs3389051250 | 578 | L>H | No | EVA | |
| rs3389052948 | 578 | L>I | No | EVA | |
| rs3389051250 | 578 | L>P | No | EVA | |
| rs244931009 | 586 | M>I | No | EVA | |
| rs3400341507 | 587 | P>H | No | EVA | |
| rs220027191 | 601 | T>S | No | EVA | |
| rs3389065371 | 610 | E>G | No | EVA | |
| rs3389066349 | 617 | V>L | No | EVA | |
| rs3389052899 | 622 | S>N | No | EVA | |
| rs3389003561 | 628 | A>S | No | EVA | |
| rs3389051264 | 632 | R>* | No | EVA | |
| rs3389059011 | 632 | R>L | No | EVA | |
| rs3389033272 | 656 | G>W | No | EVA | |
| rs216553720 | 686 | L>I | No | EVA | |
| rs3389033275 | 689 | K>N | No | EVA | |
| rs3389033336 | 733 | Q>R | No | EVA | |
| rs3389038615 | 755 | M>I | No | EVA | |
| rs32916905 | 763 | Q>K | No | EVA | |
| rs231817757 | 807 | V>M | No | EVA | |
| rs3400433656 | 828 | R>G | No | EVA | |
| rs3389062258 | 870 | S>I | No | EVA | |
| rs32916193 | 892 | T>I | No | EVA | |
| rs3389062301 | 931 | L>P | No | EVA | |
| rs3400341471 | 940 | E>Q | No | EVA | |
| rs3389056524 | 949 | Q>P | No | EVA | |
| rs244143394 | 995 | M>V | No | EVA | |
| rs32915259 | 997 | E>V | No | EVA | |
| rs3389058996 | 998 | K>R | No | EVA | |
| rs3389033296 | 1098 | V>I | No | EVA | |
| rs3389025265 | 1104 | P>H | No | EVA | |
| rs3389045653 | 1114 | L>M | No | EVA | |
| rs3389056343 | 1118 | A>P | No | EVA | |
| rs3389003546 | 1124 | C>* | No | EVA | |
| rs3389056532 | 1125 | L>V | No | EVA | |
| rs3389062271 | 1127 | C>S | No | EVA | |
| rs3389062313 | 1134 | K>N | No | EVA | |
| rs237286295 | 1268 | F>Y | No | EVA | |
| rs1132162128 | 1295 | Q>L | No | EVA | |
| rs3389025266 | 1410 | G>R | No | EVA | |
| rs238068480 | 1413 | S>P | No | EVA | |
| rs3389065353 | 1437 | M>I | No | EVA | |
| rs3400471237 | 1441 | L>M | No | EVA | |
| rs3389061181 | 1495 | E>D | No | EVA | |
| rs3389051239 | 1618 | N>Y | No | EVA | |
| rs3389056494 | 1624 | A>V | No | EVA | |
| rs3389062312 | 1634 | D>E | No | EVA | |
| rs3389056460 | 1642 | H>Q | No | EVA | |
| rs3389058146 | 1660 | V>A | No | EVA | |
| rs3389045693 | 1729 | V>L | No | EVA | |
| rs3389051253 | 1748 | C>S | No | EVA | |
| rs3389058148 | 1756 | H>Y | No | EVA | |
| rs3389065364 | 1773 | A>S | No | EVA | |
| rs3389056300 | 1787 | E>G | No | EVA | |
| rs3389052891 | 1789 | V>L | No | EVA | |
| rs3389061140 | 1800 | L>Q | No | EVA | |
| rs3389062325 | 1806 | K>I | No | EVA | |
| rs3389058119 | 1807 | M>T | No | EVA | |
| rs3389056319 | 1814 | K>R | No | EVA | |
| rs3389065400 | 1830 | K>R | No | EVA | |
| rs232028180 | 1859 | A>T | No | EVA | |
| rs221250986 | 1873 | N>D | No | EVA | |
| rs256198267 | 1877 | A>G | No | EVA | |
| rs256198267 | 1877 | A>V | No | EVA | |
| rs3547388157 | 1879 | M>I | No | EVA | |
| rs242613892 | 1884 | V>A | No | EVA | |
| rs3399295605 | 1897 | S>N | No | EVA | |
| rs3400576911 | 1919 | V>L | No | EVA | |
| rs3389061146 | 2026 | E>G | No | EVA | |
| rs3400319090 | 2036 | K>T | No | EVA | |
| rs36821162 | 2075 | A>T | No | EVA | |
| rs3389033316 | 2102 | K>* | No | EVA | |
| rs3389033292 | 2159 | G>V | No | EVA | |
| rs3389037727 | 2161 | Y>F | No | EVA | |
| rs3389033267 | 2166 | P>L | No | EVA | |
| rs3389052945 | 2181 | L>V | No | EVA | |
| rs3399776189 | 2185 | S>F | No | EVA | |
| rs3400576894 | 2194 | K>E | No | EVA |
No associated diseases with Q8K0T7
7 regional properties for Q8K0T7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1199 - 1325 | IPR000008-1 |
| domain | C2 domain | 2038 - 2167 | IPR000008-2 |
| domain | Protein kinase C-like, phorbol ester/diacylglycerol-binding domain | 1093 - 1143 | IPR002219 |
| domain | MUN domain | 1535 - 2024 | IPR010439 |
| domain | Munc13 homology 1 | 1633 - 1776 | IPR014770 |
| domain | Mammalian uncoordinated homology 13, domain 2 | 1882 - 2024 | IPR014772 |
| domain | Protein Unc-13, C2B domain | 1216 - 1342 | IPR037302 |
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| calyx of Held | The terminal specialization of a calyciferous axon which forms large synapses in the mammalian auditory central nervous system. |
| neuromuscular junction | The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential. |
| parallel fiber to Purkinje cell synapse | An excitatory synapse formed by the parallel fibers of granule cells synapsing onto the dendrites of Purkinje cells. |
| 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. |
| presynaptic active zone cytoplasmic component | A specialized region below the presynaptic membrane, characterized by electron-dense material, a specialized cytoskeletal matrix and accumulated (associated) synaptic vesicles. |
| presynaptic membrane | A specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction; many synaptic junctions exhibit structural presynaptic characteristics, such as conical, electron-dense internal protrusions, that distinguish it from the remainder of the axon plasma membrane. |
| synaptic vesicle membrane | The lipid bilayer surrounding a synaptic vesicle. |
| terminal bouton | Terminal inflated portion of the axon, containing the specialized apparatus necessary to release neurotransmitters. The axon terminus is considered to be the whole region of thickening and the terminal bouton is a specialized region of it. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calmodulin binding | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. |
| diacylglycerol binding | Binding to a diacylglycerol, a diester of glycerol and two fatty acids. |
| non-kinase phorbol ester receptor activity | Combining with a phorbol ester and transmitting the signal by a mechanism independent of kinase activity. |
| phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. |
| syntaxin binding | Binding to a syntaxin, a SNAP receptor involved in the docking of synaptic vesicles at the presynaptic zone of a synapse. |
| syntaxin-1 binding | Binding to a syntaxin-1 SNAP receptor. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| chemical synaptic transmission | The vesicular release of classical neurotransmitter molecules from a presynapse, across a chemical synapse, the subsequent activation of neurotransmitter receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse. |
| dense core granule priming | A process that converts unprimed dense core granules (DCVs) to a pool of primed vesicles that are capable of fusing with the plasma membrane (fusion-competent) and thereby releasing their contents. Priming typically occurs after docking. |
| negative regulation of synaptic plasticity | A process that decreases synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers. |
| neuromuscular junction development | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a neuromuscular junction. |
| presynaptic dense core vesicle exocytosis | The secretion of molecules (e.g. neuropeptides and neuromodulators such as serotonin and dopamine) contained within a membrane-bounced dense in response to increased presynaptic cytosolic calcium levels. |
| synaptic transmission, glutamatergic | The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse. |
| synaptic vesicle docking | The initial (indirect) attachment of a synaptic vesicle membrane to the presynaptic active zone membrane, mediated by proteins protruding from the membrane and proteins of the presynaptic active zone cytoplasmic component. Synaptic vesicle tethering is the first step in this process. |
| synaptic vesicle exocytosis | Fusion of intracellular membrane-bounded vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft. |
| synaptic vesicle maturation | Steps required to form an initiated synaptic vesicle into a fully formed and transmissible synaptic vesicle. |
| synaptic vesicle priming | A process that converts synaptic vesicles to a state of competence for calcium triggered fusion with the active zone membrane by bringing the two membranes into very close proximity. Priming typically (but not always) occurs after docking (Jahn and Fasshauer, 2012). Primed vesicles are also capable of spontaneously fusing with the active zone membrane. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O14795 | UNC13B | Protein unc-13 homolog B | Homo sapiens (Human) | SS |
| Q9UPW8 | UNC13A | Protein unc-13 homolog A | Homo sapiens (Human) | SS |
| Q8NB66 | UNC13C | Protein unc-13 homolog C | Homo sapiens (Human) | SS |
| Q4KUS2 | Unc13a | Protein unc-13 homolog A | Mus musculus (Mouse) | SS |
| Q9Z1N9 | Unc13b | Protein unc-13 homolog B | Mus musculus (Mouse) | SS |
| Q62768 | Unc13a | Protein unc-13 homolog A | Rattus norvegicus (Rat) | SS |
| Q62769 | Unc13b | Protein unc-13 homolog B | Rattus norvegicus (Rat) | SS |
| Q62770 | Unc13c | Protein unc-13 homolog C | Rattus norvegicus (Rat) | SS |
| P27715 | unc-13 | Phorbol ester/diacylglycerol-binding protein unc-13 | Caenorhabditis elegans | EV |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVASLFKSLI | LAYIHKLCKG | MFTKKLGNTT | KKKENRQQKK | DQDFPTAGHT | KPPKLSNALK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| STVKKIAKCS | STRNFSIEDE | EGHKDFSLSP | TFSYRVAIAN | GLQTAVTNSD | EDLLQELSSI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ESSYSESFNE | LRSSTENQVQ | STHTMPVRRN | RKSSSSLAPS | EGSSDGERTL | HTLKLGALRK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LRKWKKSQEC | VSSDSELSTV | KKTWGIRSKS | LDRTARNPKT | NVLEPGFSSS | GCISQTHDVM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EMIFKELQGI | SQIETELSEL | RGHVNALKYS | IDEISSSVEV | VQSEIEQLRT | GFVQARRETR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DIHDYIKHLG | HMGSKVSLRF | LNVPEERHEY | VESVVYQILI | DKMGFSDVPN | AIKIEFAQRI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GQQRDCPNAK | PRPILVYFET | PQQRDSVLKK | SYKLKGTGIG | ISTDILTYDI | RERKEKGVLP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SSQTYESMDM | KLSTPEPKAK | KNAWLSPNDS | DRELESDLSR | SSYADSPAKG | SSSKSSSKSH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SARSKNKAAN | SRTSQKSDYN | KRPSQPPASS | TPEKQTPHYV | EATPPLWHSQ | SDFFTLKLSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SESDFSKLCQ | SYSEDFSESQ | FFCRTNGSSL | LSSSDRELWQ | RKQEGMPALY | HRLQDQGLDE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| TIPAVPGQAE | IENTETVDSG | MSNSMVCASG | DRSNYSGSQL | SLHEDLSPWK | EWNQAGQGTD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DVGLDSSTQE | PFDYDTNSLS | DQQLDLSSKD | LDDLGKCHSD | LQDDSESYDL | TQDDNSSPCP |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GLDNEPQGQW | VGQYDSYQEA | NSNDLYPNQS | HPSMMYRSQS | ELQSDDSEGA | QPKSWHSRLS |
| 790 | 800 | 810 | 820 | 830 | 840 |
| IDLSDKTFKF | PKFGSTLQRA | KSALEVVWNK | STQSLSGCED | SGSSLMGRFR | TLSQSTANES |
| 850 | 860 | 870 | 880 | 890 | 900 |
| STTLDSDIYT | EPYYYKAEEE | EDYCEPVADS | ETDYVEVMEQ | VLAKLENRTS | ITEVNEHIKD |
| 910 | 920 | 930 | 940 | 950 | 960 |
| YDHPSYETPY | ETPQDEGYDG | QADDIISEGE | LETLNEPAVE | MELAEDENQN | LPAESLEVMK |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| PKRIRPSFKE | AALRAYKKQM | AELEEKILAG | DSSSMDEKAR | IVSGNDLDAS | KFSALQVFGG |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| AGRGLYGIDS | MPDLRRKKTL | PIVRDVAMTL | AARKSGLSLA | MVIRTSLNNE | ELKMHVFRKT |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| LQALIYPISS | TTPHNFEVWT | ATTPTYCYEC | EGLLWGIARQ | GMKCLECGVK | CHEKCQDLLN |
| 1150 | 1160 | 1170 | 1180 | 1190 | 1200 |
| ADCLQRAAEK | SSKHGAEDKT | QTIITAMKER | MKIRERNRPE | VFEVIQEMFQ | ISKEDFVQYT |
| 1210 | 1220 | 1230 | 1240 | 1250 | 1260 |
| KAAKQSVLDG | TSKWSAKITI | TVVSAQGLQA | KDKTGSSDPY | VTVQVGKNKR | RTKTIFGNLN |
| 1270 | 1280 | 1290 | 1300 | 1310 | 1320 |
| PVWDEKFFFE | CHNSTDRIKV | RVWDEDDDIK | SRVKQHFKKE | SDDFLGQTIV | EVRTLSGEMD |
| 1330 | 1340 | 1350 | 1360 | 1370 | 1380 |
| VWYNLEKRTD | KSAVSGAIRL | KINVEIKGEE | KVAPYHIQYT | CLHENLFHYL | TEVKSNGSVK |
| 1390 | 1400 | 1410 | 1420 | 1430 | 1440 |
| IPEVKGDEAW | KVFFDDASQE | IVDEFAMRYG | VESIYQAMTH | FSCLSSKYMC | PGVPAVMSAL |
| 1450 | 1460 | 1470 | 1480 | 1490 | 1500 |
| LANINAFYAH | TTVSTNVQVS | ASDRFAATNF | GREKFIKLLD | QLHNSLRIDL | SKYRENFPAS |
| 1510 | 1520 | 1530 | 1540 | 1550 | 1560 |
| NSERLQDLKS | TVDLLTSITF | FRMKVLELQS | PPKASAVVKD | CVRACLDSTY | KYIFDNCHEL |
| 1570 | 1580 | 1590 | 1600 | 1610 | 1620 |
| YSQLIDPSKK | QDVPREDQGP | TTKNLDFWPQ | LITLMVTIID | EDKTAYTPVL | NQFPQELNMG |
| 1630 | 1640 | 1650 | 1660 | 1670 | 1680 |
| KISAEIMWSL | FALDMKYALE | EHEKQRLCKS | TDYMNLHFKV | KWFYNEYVRE | LPAFKDAVPE |
| 1690 | 1700 | 1710 | 1720 | 1730 | 1740 |
| YSLWFEPFVM | QWLDENEDVS | MEFLHGALGR | DKKDGFQQTS | DHALFSCSVV | DVFAQLNQSF |
| 1750 | 1760 | 1770 | 1780 | 1790 | 1800 |
| EIIKKLECPN | PEALSHLMRR | FAKTINKVLV | QYAAIVSNDF | SSYCDKETVP | CILMNNIQQL |
| 1810 | 1820 | 1830 | 1840 | 1850 | 1860 |
| RVQLEKMFES | MGGKELDPEA | STILKELQIK | LNGVLDALSI | TYGESFQLTI | EECIKQMGAE |
| 1870 | 1880 | 1890 | 1900 | 1910 | 1920 |
| LNQMRANGNS | TANKNSAAMD | AEIVLRPLMD | FLDKTLSLSA | KICEKTVLKR | VLKELWKLVL |
| 1930 | 1940 | 1950 | 1960 | 1970 | 1980 |
| NKIEKQIVLP | PLTDQTGPQM | IFIAAKDLGQ | LSKLKEHMIR | EDAKGLTPRQ | CAIVEVVLAT |
| 1990 | 2000 | 2010 | 2020 | 2030 | 2040 |
| IKQYFHAGGN | GLKKNFLEKS | PDLHSLRYAL | SLYTQTTDAL | IKKFIETQGS | QSRSSKDAVG |
| 2050 | 2060 | 2070 | 2080 | 2090 | 2100 |
| QISVHVDVTT | TPGTGDHKVT | VKVIAINDLN | WQTTAMFRPF | VEVCMLGPSL | GDKKRKQGTK |
| 2110 | 2120 | 2130 | 2140 | 2150 | 2160 |
| TKSNTWSPKY | NETFQFILGN | ENRPGAYELH | LSVKDYCFAR | EDRIIGMTVI | QLQNIAEKGS |
| 2170 | 2180 | 2190 | 2200 | ||
| YGAWYPLLKN | LSMDETGLTI | LRILSQRTSD | DVAKEFVRLK | SETRSIEESA |