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Protein

Rho GTPase-activating protein 7

Gene

Dlc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a GTPase-activating protein for the small GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream signaling. This induces morphological changes and detachment through cytoskeletal reorganization, playing a critical role in biological processes such as cell migration and proliferation. Also functions in vivo as an activator of the phospholipase PLCD1. Active DLC1 increases cell migration velocity but reduces directionality (By similarity).By similarity1 Publication

GO - Molecular functioni

  • GTPase activator activity Source: RGD
  • lipid binding Source: InterPro
  • phospholipase binding Source: RGD
  • vinculin binding Source: RGD

GO - Biological processi

  • activation of phospholipase C activity Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cytoskeleton organization Source: RGD
  • negative regulation of cell proliferation Source: UniProtKB
  • regulation of Rho protein signal transduction Source: InterPro
  • signal transduction Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 7
Alternative name(s):
Deleted in liver cancer 1 protein homolog
Short name:
DLC-1
Rho-type GTPase-activating protein 7
START domain-containing protein 12
Short name:
StARD12
StAR-related lipid transfer protein 12
p122-RhoGAP
Gene namesi
Name:Dlc1
Synonyms:Arhgap7, Rhogap, Stard12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68416. Dlc1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • focal adhesion Source: UniProtKB-SubCell
  • membrane raft Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi677 – 6771R → E: Loss of activity. 1 Publication
Mutagenesisi714 – 7141K → E: Loss of activity. 1 Publication
Mutagenesisi718 – 7181R → E: Loss of activity. 1 Publication
Mutagenesisi787 – 7871N → V: No loss of activity. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10911091Rho GTPase-activating protein 7PRO_0000056709Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei89 – 891PhosphoserineBy similarity
Modified residuei129 – 1291PhosphoserineCombined sources
Modified residuei321 – 3211PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ63744.
PRIDEiQ63744.

PTM databases

iPTMnetiQ63744.
PhosphoSiteiQ63744.

Interactioni

Subunit structurei

Interacts with EF1A1, facilitates EF1A1 distribution to the membrane periphery and ruffles upon growth factor stimulation and suppresses cell migration.By similarity

GO - Molecular functioni

  • phospholipase binding Source: RGD
  • vinculin binding Source: RGD

Protein-protein interaction databases

MINTiMINT-4542745.
STRINGi10116.ENSRNOP00000014923.

Structurei

3D structure databases

ProteinModelPortaliQ63744.
SMRiQ63744. Positions 1-81, 887-1078.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 7868SAMAdd
BLAST
Domaini641 – 847207Rho-GAPPROSITE-ProRule annotationAdd
BLAST
Domaini877 – 1084208STARTPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 447174Focal adhesion-targeting (FAT)By similarityAdd
BLAST
Regioni614 – 63623Polybasic cluster (PBR)By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi305 – 3117Poly-Ser
Compositional biasi431 – 4377Poly-Ser

Domaini

The SAM domain mediates interaction with EF1A1, and functions as an autoinhibitory regulator of RhoGAP Activity.By similarity
The polybasic cluster is required for activation and mediates binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) containing membranes.By similarity

Sequence similaritiesi

Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
Contains 1 START domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2200. Eukaryota.
ENOG410XQ10. LUCA.
HOGENOMiHOG000039960.
HOVERGENiHBG055955.
InParanoidiQ63744.
PhylomeDBiQ63744.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR028854. DLC1.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PANTHERiPTHR12659:SF2. PTHR12659:SF2. 1 hit.
PfamiPF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63744-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCRDEPDTMI LTQIEAKEAC DWLRVTGFPQ YAQLYEDLLF PIDIALVKRE
60 70 80 90 100
HDFLDRDAIE ALCRRLNTLN KCAVMKLEIS PHRKRSEDSD EEEPCAISGK
110 120 130 140 150
WTFQRDSKRW SRLEEFDVFS PKQDPIPGSP DNSRLQSATS RESMLTDLSE
160 170 180 190 200
HQEVSSIRSL SSTSSSAPTH VPHSGEATTP RTNSVISVCS SSHFVGNEDS
210 220 230 240 250
FSSLPSPKEL SSFSFSMKGH EKNTKSKTRS LLKRMESLKL KGSHHSKHKA
260 270 280 290 300
PSKLGLIISA PILQEGMDEE KLKQLNCVEI SALNGNHINV PMVRKRSVSN
310 320 330 340 350
STQTSSSSSQ SETSSAVSTP SPVTRTRSLS TCNKRVGMYL EGFDPFSQSA
360 370 380 390 400
FNNVTEQNYK NRESYPEDTV FYIPEDHKPG TFPKALSNGS FCPSGNSSVN
410 420 430 440 450
WRTGSFHGPG HLSLRRENSS DSPKELKRRN SSSSVSSRMS IYDNVPGSIL
460 470 480 490 500
YSSSGELADL ENEDIFPELD DILYHVKGMQ RIVNQWSEKF SDEGDSDSAL
510 520 530 540 550
DSVSPCPSSP KQIHLDVDHD RRTPSDLDST GNSLNEPEEP TDIPERRDSG
560 570 580 590 600
VGASLTRCNR HRLRWHSFQS SHRPSLNSVS LQINCQSVAQ MNLLQKYSLL
610 620 630 640 650
KLTALLEKYT PSNKHGFSWA VPKFMKRIKV PDYKDRSVFG VPLTVNVQRS
660 670 680 690 700
GQPLPQSIQQ AMRYLRNHCL DQVGLFRKSG VKSRIQALRQ MNESAEDYVN
710 720 730 740 750
YEGQSAYDVA DMLKQYFRDL PEPLMTNKLS ETFLQIYQYV PKDQRLQAIK
760 770 780 790 800
AAIMLLPDEN REVLQTLLYF LSHVTAAVKE NQMTPTNLAV CLAPSLFHLN
810 820 830 840 850
TLKRENSSPR VMQRKQSLGK PDQKDLNENL AATQGLAHMI AECKKLFQVP
860 870 880 890 900
EEMSRCRNSY TEQELKPLTL EALGHLSNDQ PADYRHFLQD CVDGLFKEVK
910 920 930 940 950
EKFKGWVSYP TSEQAELSYK KVSEGPPLRL WRATIEVPAA PEEILKRLLK
960 970 980 990 1000
EQHLWDVDLL DSKVIEILDS QTEIYQYVQN SMAPHPARDY VVLRTWRTNL
1010 1020 1030 1040 1050
PRGACALLFT SVDHDRAPVA GVRVNVLLSR YLIEPCGSGK SKLTYMCRAD
1060 1070 1080 1090
LRGHMPEWYT KSFGHLCAAE VVKIRDSFSN QSTESKDTRS R
Length:1,091
Mass (Da):123,414
Last modified:November 15, 2002 - v3
Checksum:iFB4A0924E0C36A15
GO

Sequence cautioni

The sequence BAA21675.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31962 mRNA. Translation: BAA21675.1. Different initiation.
UniGeneiRn.224563.
Rn.7255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31962 mRNA. Translation: BAA21675.1. Different initiation.
UniGeneiRn.224563.
Rn.7255.

3D structure databases

ProteinModelPortaliQ63744.
SMRiQ63744. Positions 1-81, 887-1078.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4542745.
STRINGi10116.ENSRNOP00000014923.

PTM databases

iPTMnetiQ63744.
PhosphoSiteiQ63744.

Proteomic databases

PaxDbiQ63744.
PRIDEiQ63744.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi68416. Dlc1.

Phylogenomic databases

eggNOGiKOG2200. Eukaryota.
ENOG410XQ10. LUCA.
HOGENOMiHOG000039960.
HOVERGENiHBG055955.
InParanoidiQ63744.
PhylomeDBiQ63744.

Miscellaneous databases

PROiQ63744.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
3.30.530.20. 1 hit.
InterProiIPR028854. DLC1.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PANTHERiPTHR12659:SF2. PTHR12659:SF2. 1 hit.
PfamiPF00620. RhoGAP. 1 hit.
PF07647. SAM_2. 1 hit.
PF01852. START. 1 hit.
[Graphical view]
SMARTiSM00324. RhoGAP. 1 hit.
SM00234. START. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48350. SSF48350. 1 hit.
PROSITEiPS50238. RHOGAP. 1 hit.
PS50848. START. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A dual functional signal mediator showing RhoGAP and phospholipase C-delta stimulating activities."
    Homma Y., Emori Y.
    EMBO J. 14:286-291(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Morphological changes and detachment of adherent cells induced by p122, a GTPase-activating protein for Rho."
    Sekimata M., Kabuyama Y., Emori Y., Homma Y.
    J. Biol. Chem. 274:17757-17762(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-677; LYS-714; ARG-718 AND ASN-787.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRHG07_RAT
AccessioniPrimary (citable) accession number: Q63744
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 6, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.