O35536
SS
Gene name |
Tfpi2 |
Protein name |
Tissue factor pathway inhibitor 2 |
Names |
TFPI-2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:21789 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
MARK1 is a Ser/Thr protein kinase involved in various cellular processes. It is part of the CAMK-like kinase family and has roles in diseases like Alzheimer’s and cancer. The kinase’s autoinhibition is mediated by its C-terminal KA1 domain, which interacts with the kinase domain to prevent substrate binding and activation. The KA1 domain binds to the αD-helix, blocking the peptide substrate binding site and inhibiting the kinase. This autoinhibition is alleviated by the binding of anionic phospholipid membranes to the KA1 domain, which reverses MARK1 autoinhibition and stimulates kinase activity.
Autoinhibitory domains (AIDs)
Target domain |
33-87 (Pancreatic trypsin inhibitor Kunitz domain) |
Relief mechanism |
PTM |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O35536
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O35536-F1 | Predicted | AlphaFoldDB |
13 variants for O35536
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388813426 | 3 | P>H | No | EVA | |
| rs37026717 | 8 | Q>R | No | EVA | |
| rs3388815282 | 21 | L>H | No | EVA | |
| rs249673599 | 58 | Q>H | No | EVA | |
| rs3388813328 | 64 | F>V | No | EVA | |
| rs238647899 | 83 | Q>E | No | EVA | |
| rs263720055 | 94 | P>Q | No | EVA | |
| rs265943979 | 111 | R>Q | No | EVA | |
| rs36318687 | 133 | I>M | No | EVA | |
| rs255970186 | 140 | A>T | No | EVA | |
| rs1135179125 | 171 | R>C | No | EVA | |
| rs3396010315 | 202 | C>* | No | EVA | |
| rs3396418179 | 204 | R>G | No | EVA |
No associated diseases with O35536
6 regional properties for O35536
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 56 - 307 | IPR000719 |
| domain | Kinase associated domain 1 (KA1) | 704 - 753 | IPR001772 |
| active_site | Serine/threonine-protein kinase, active site | 174 - 186 | IPR008271 |
| domain | Ubiquitin-associated domain | 326 - 365 | IPR015940 |
| binding_site | Protein kinase, ATP binding site | 62 - 85 | IPR017441 |
| domain | Serine/threonine-protein kinase MARK 1-4, catalytic domain | 55 - 307 | IPR049508 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| serine-type endopeptidase inhibitor activity | Binds to and stops, prevents or reduces the activity of a serine-type endopeptidase. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| blood coagulation | The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages |
| cellular response to fluid shear stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a fluid shear stress stimulus. Fluid shear stress is the force acting on an object in a system where the fluid is moving across a solid surface. |
13 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q7YRQ8 | TFPI2 | Tissue factor pathway inhibitor 2 | Bos taurus (Bovine) | SS |
| Q868Z9 | Ppn | Papilin | Drosophila melanogaster (Fruit fly) | SS |
| M9PE65 | axo | Axotactin | Drosophila melanogaster (Fruit fly) | SS |
| P49223 | SPINT3 | Kunitz-type protease inhibitor 3 | Homo sapiens (Human) | SS |
| O43291 | SPINT2 | Kunitz-type protease inhibitor 2 | Homo sapiens (Human) | EV |
| O43278 | SPINT1 | Kunitz-type protease inhibitor 1 | Homo sapiens (Human) | EV |
| P10646 | TFPI | Tissue factor pathway inhibitor | Homo sapiens (Human) | SS |
| P48307 | TFPI2 | Tissue factor pathway inhibitor 2 | Homo sapiens (Human) | SS |
| Q9R097 | Spint1 | Kunitz-type protease inhibitor 1 | Mus musculus (Mouse) | SS |
| Q9WU03 | Spint2 | Kunitz-type protease inhibitor 2 | Mus musculus (Mouse) | SS |
| O54819 | Tfpi | Tissue factor pathway inhibitor | Mus musculus (Mouse) | SS |
| Q02445 | Tfpi | Tissue factor pathway inhibitor | Rattus norvegicus (Rat) | SS |
| Q28864 | TFPI | Tissue factor pathway inhibitor | Macaca mulatta (Rhesus macaque) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTRTPLPTV | NERDTENHIS | HGDGRQEVTS | RTGRSGARCR | NSIASCADEQ | PHIGNYRLLK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TIGKGNFAKV | KLARHILTGR | EVAIKIIDKT | QLNPTSLQKL | FREVRIMKIL | NHPNIVKLFE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIETEKTLYL | IMEYASGGEV | FDYLVAHGRM | KEKEARAKFR | QIVSAVQYCH | QKRIVHRDLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AENLLLDADM | NIKIADFGFS | NEFTVGSKLD | TFCGSPPYAA | PELFQGKKYD | GPEVDVWSLG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VILYTLVSGS | LPFDGQNLKE | LRERVLRGKY | RIPFYMSTDC | ENLLKRFLVL | NPVKRGTLEQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IMKDRWINAG | HEEDELKPFV | EPELDISDQK | RIDIMVGMGY | SQEEIQESLS | KMKYDEITAT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YLLLGRKSAE | LDASDSSSSS | NLSLAKVRPN | SDLSNSTGQS | PHHKGQRSVS | SSQKQRRYSD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HAGPAIPSVV | AYPKRSQTST | ADSDLKEDGI | PSRKSSSSAV | GGKGIAPASP | MLGNAGNPNK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ADIPERKKSP | AVPSSNTASG | GMTRRNTYVC | SERCAADRHS | VIQNGKENSA | IPDERTPVAS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| THSISSATTP | DRIRFPRGTA | SRSTFHGQPR | ERRTATYNGP | PASPSLSHEA | TPLSQTRSRG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| STNLFSKLTS | KLTRRNMSFR | FIKRLPTEYE | RNGRYEGSSR | NVSSEQKDEN | REAKPRSLRF |
| 670 | 680 | 690 | 700 | 710 | 720 |
| TWSMKTTSSM | DPSDMMREIR | KVLDANNCDY | EQRERFLLFC | VHGDGHAENL | VQWEMEVCKL |
| 730 | 740 | 750 | |||
| PRLSLNGVRF | KRISGTSIAF | KNIASKIANE | LKL |