B9VTT2
Gene name |
DLC1 (ARHGAP7, STARD12) |
Protein name |
Rho GTPase-activating protein 7 |
Names |
Deleted in liver cancer 1 protein homolog, DLC-1, Rho-type GTPase-activating protein 7, START domain-containing protein 12, StARD12, StAR-related lipid transfer protein 12 |
Species |
Canis lupus familiaris (Dog) (Canis familiaris) |
KEGG Pathway |
cfa:475607 |
EC number |
|
Protein Class |
|

Descriptions
Autoinhibitory domains (AIDs)
Target domain |
641-847 (Rho-GAP domain) |
Relief mechanism |
Cleavage |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

1 structures for B9VTT2
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-B9VTT2-F1 | Predicted | AlphaFoldDB |
No variants for B9VTT2
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for B9VTT2 |
No associated diseases with B9VTT2
Functions
3 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
2 GO annotations of molecular function
Name | Definition |
---|---|
GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
lipid binding | Binding to a lipid. |
3 GO annotations of biological process
Name | Definition |
---|---|
actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
regulation of Rho protein signal transduction | Any process that modulates the frequency, rate or extent of Rho protein signal transduction. |
signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
10 | 20 | 30 | 40 | 50 | 60 |
MCRRKPDIMI | LTQIEAKEAC | DWLRATGFPQ | YAQLYEDLLF | PIDISSVKRE | HDFLDRDAIE |
70 | 80 | 90 | 100 | 110 | 120 |
ALCRRLNTLN | KCAVMKLEIS | PHRKRSEDSD | EDEPCAISGK | WTFQRDSKRW | SRLEEFDVFS |
130 | 140 | 150 | 160 | 170 | 180 |
SKLDPAPGAP | AEAPLKTAAS | HESMLTELSE | RQEVASVLSL | SSTGSLPVHA | PHAGDAATPR |
190 | 200 | 210 | 220 | 230 | 240 |
TNSVISVCSS | GHFVGNDDSF | CSLPSPKELS | SFSFSMKGQE | KNAKSKTRSL | LKRMESLKLR |
250 | 260 | 270 | 280 | 290 | 300 |
GSPHSKHKAP | SKLGLIISGP | ILQEGMDEEK | LKQLNCVEIS | ALNGNRINVP | AVRKRSVSNS |
310 | 320 | 330 | 340 | 350 | 360 |
TQTSSSSSQS | ETSSAVSTPS | PVTRTRSLSA | CNKRVGMYLE | GFDPFNQSTF | NNVMEQNCKN |
370 | 380 | 390 | 400 | 410 | 420 |
RESYPEDTVF | YIPEDHKPGT | FPKALSNGSF | PPSGNNSSVN | WRTGSFHGPG | HISLRRENSS |
430 | 440 | 450 | 460 | 470 | 480 |
DSPKELKRRN | SSSSMSSRLS | IYDNVPGSIL | YSSSGDLADL | ENEDIFPELD | DILYHVKGMQ |
490 | 500 | 510 | 520 | 530 | 540 |
RIVNQWSEKF | SDEGDSDSAL | DSVSPCPSSP | KQIHLDVDND | RATPSDLDST | GNSLNEPEEP |
550 | 560 | 570 | 580 | 590 | 600 |
SDIPERRDSG | VGASLTRSNR | HRLRWHSFQS | SHRPSLNSVS | LQINCQSVAQ | MNLLQKYSLL |
610 | 620 | 630 | 640 | 650 | 660 |
KLTALLEKYT | PSNKHGFSWA | VPKFMKRIKV | PDYKDRNVFG | VPLTVNVQRT | GQPLPQSIQQ |
670 | 680 | 690 | 700 | 710 | 720 |
AMRYLRNHCL | DQVGLFRKSG | VKSRIQALRQ | MNESAIDCVN | YEGQSAYDVA | DMLKQYFRDL |
730 | 740 | 750 | 760 | 770 | 780 |
PEPLMTNKLS | ETFLQIYQCV | PKDQRLQAMK | AAIMLLPDEN | REVLQTLLYF | LSDVTAAVKE |
790 | 800 | 810 | 820 | 830 | 840 |
NQMTPTNLAV | CLAPSLFHLN | TLKRENSSPR | VMQRKQSLGK | PDQKDLNENL | AATQGLAHMI |
850 | 860 | 870 | 880 | 890 | 900 |
AECKKLFQVP | EEMSRCRNSY | TEQELKPLTL | EALGRLRNDE | SADYQHFLQD | CVDSLFKEVK |
910 | 920 | 930 | 940 | 950 | 960 |
EKFKGWVSYS | TSEQAELSYK | KVSEGPPLRL | WRSTIEVPAM | PEEILKRLLK | EQHLWDVDLL |
970 | 980 | 990 | 1000 | 1010 | 1020 |
DSKVIEILDS | QTEIYQYVQN | SMAPHPARDY | VVLRTWRTNL | PKGACALLLT | SVDHDRAPVV |
1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
GVRVNVLLSR | YLIEPCGSGK | SKLTYMCRAD | LRGHMPEWYT | KSFGHLCAAE | VVKIRDSFSN |
1090 | |||||
QNTETKDTKS | R |