Descriptions

DLC1 encodes a Rho GTPase-activating protein (RhoGAP) and negative regulator of specific Rho family proteins (RhoA-C and Cdc42). DLC1 is a multi-domain protein, with the RhoGAP catalytic domain flanked by an amino-terminal sterile motif (SAM) and a carboxyl-terminal START domain. In a study with human DLC1 isoform 1, truncation of SAM domain activates RhoGAP catalytic domain.

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

2 regional properties for B9VTT2

Type Name Position InterPro Accession
domain Rho GTPase-activating protein domain 641 - 847 IPR000198
domain Sterile alpha motif domain 17 - 76 IPR001660

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cell junction, focal adhesion
  • Membrane ; Peripheral membrane protein
  • Colocalizes with EF1A1 at actin-rich regions in the cell periphery
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

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.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
A7E300 DLC1 Rho GTPase-activating protein 7 Bos taurus (Bovine) SS
Q9R0Z9 Dlc1 Rho GTPase-activating protein 7 Mus musculus (Mouse) SS
Q63744 Dlc1 Rho GTPase-activating protein 7 Rattus norvegicus (Rat) SS
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