RHG07_HUMAN
ID RHG07_HUMAN Reviewed; 1528 AA.
AC Q96QB1; B4DR10; B8PTI0; E9PDZ8; E9PF76; E9PGY9; O14868; O43199; Q7Z5R8;
AC Q86UC6; Q9C0E0; Q9H7A2;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Rho GTPase-activating protein 7;
DE AltName: Full=Deleted in liver cancer 1 protein;
DE Short=DLC-1;
DE AltName: Full=HP protein;
DE AltName: Full=Rho-type GTPase-activating protein 7;
DE AltName: Full=START domain-containing protein 12;
DE Short=StARD12;
DE AltName: Full=StAR-related lipid transfer protein 12;
GN Name=DLC1; Synonyms=ARHGAP7, KIAA1723, STARD12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-712; VAL-1199 AND
RP CYS-1209.
RX PubMed=9605766;
RA Yuan B.Z., Miller M.J., Keck C.L., Zimonjic D.B., Thorgeirsson S.S.,
RA Popescu N.C.;
RT "Cloning, characterization, and chromosomal localization of a gene
RT frequently deleted in human liver cancer (DLC-1) homologous to rat
RT RhoGAP.";
RL Cancer Res. 58:2196-2199(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-791.
RC TISSUE=Lung;
RA Wei M.-H., Pack S., Ivanov S., Lerman M.I.;
RT "Cloning and molecular characterization of the human ortholog of the rat
RT dual regulator p122RhoGAP.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT MET-791.
RA Jeong S.-J., Dimtchev A., Lerman M., Dritschilo A., Jung M.;
RT "Identification of HP/DLC1 exon and introns.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS HIS-254;
RP ASP-255 AND ILE-260 AND MET-791.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANTS
RP HIS-254; ASP-255; ILE-260 AND MET-791.
RC TISSUE=Smooth muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND VARIANT
RP ASP-255.
RC TISSUE=Brain, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-50 (ISOFORM 6), AND ALTERNATIVE PROMOTER
RP USAGE.
RC TISSUE=Liver;
RX PubMed=21217778; DOI=10.1038/onc.2010.576;
RA Low J.S., Tao Q., Ng K.M., Goh H.K., Shu X.S., Woo W.L., Ambinder R.F.,
RA Srivastava G., Shamay M., Chan A.T., Popescu N.C., Hsieh W.S.;
RT "A novel isoform of the 8p22 tumor suppressor gene DLC1 suppresses tumor
RT growth and is frequently silenced in multiple common tumors.";
RL Oncogene 30:1923-1935(2011).
RN [9]
RP FUNCTION, DOMAIN SAM, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-879.
RX PubMed=18786931; DOI=10.1074/jbc.m800617200;
RA Kim T.Y., Healy K.D., Der C.J., Sciaky N., Bang Y.J., Juliano R.L.;
RT "Effects of structure of Rho GTPase-activating protein DLC-1 on cell
RT morphology and migration.";
RL J. Biol. Chem. 283:32762-32770(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND FOCAL ADHESION TARGETING.
RX PubMed=19170769; DOI=10.1111/j.1365-2443.2008.01265.x;
RA Kawai K., Iwamae Y., Yamaga M., Kiyota M., Ishii H., Hirata H., Homma Y.,
RA Yagisawa H.;
RT "Focal adhesion-localization of START-GAP1/DLC1 is essential for cell
RT motility and morphology.";
RL Genes Cells 14:227-241(2009).
RN [11]
RP FUNCTION, AND LIPID-BINDING REGION.
RX PubMed=19710422; DOI=10.1091/mbc.e09-03-0247;
RA Erlmann P., Schmid S., Horenkamp F.A., Geyer M., Pomorski T.G.,
RA Olayioye M.A.;
RT "DLC1 activation requires lipid interaction through a polybasic region
RT preceding the RhoGAP domain.";
RL Mol. Biol. Cell 20:4400-4411(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523; SER-526 AND SER-757, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP STRUCTURE BY NMR OF 438-518.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SAM-domain of rho-GTPase-activating protein 7.";
RL Submitted (APR-2007) to the PDB data bank.
RN [15]
RP STRUCTURE BY NMR OF 454-513.
RX PubMed=19317456; DOI=10.1021/bi9000936;
RA Yang S., Noble C.G., Yang D.;
RT "Characterization of DLC1-SAM equilibrium unfolding at the amino acid
RT residue level.";
RL Biochemistry 48:4040-4049(2009).
RN [16]
RP STRUCTURE BY NMR OF 451-513, MUTAGENESIS OF PHE-475; LEU-476 AND ARG-1114,
RP INTERACTION WITH EF1A1, AND SUBCELLULAR LOCATION.
RX PubMed=19158340; DOI=10.1242/jcs.027482;
RA Zhong D., Zhang J., Yang S., Soh U.J., Buschdorf J.P., Zhou Y.T., Yang D.,
RA Low B.C.;
RT "The SAM domain of the RhoGAP DLC1 binds EF1A1 to regulate cell
RT migration.";
RL J. Cell Sci. 122:414-424(2009).
RN [17]
RP VARIANTS SER-712; MET-791; ALA-959; GLN-998; ALA-1025; VAL-1199 AND
RP CYS-1209.
RX PubMed=10649492;
RX DOI=10.1002/(sici)1098-1004(200002)15:2<156::aid-humu4>3.0.co;2-4;
RA Wilson P.J., McGlinn E., Marsh A., Evans T., Arnold J., Wright K.,
RA Biden K., Young J., Wainwright B., Wicking C., Chenevix-Trench G.;
RT "Sequence variants of DLC1 in colorectal and ovarian tumours.";
RL Hum. Mutat. 15:156-165(2000).
CC -!- FUNCTION: Functions as a GTPase-activating protein for the small
CC GTPases RHOA, RHOB, RHOC and CDC42, terminating their downstream
CC signaling. This induces morphological changes and detachment through
CC cytoskeletal reorganization, playing a critical role in biological
CC processes such as cell migration and proliferation. Also functions in
CC vivo as an activator of the phospholipase PLCD1. Active DLC1 increases
CC cell migration velocity but reduces directionality.
CC {ECO:0000269|PubMed:18786931, ECO:0000269|PubMed:19170769,
CC ECO:0000269|PubMed:19710422}.
CC -!- SUBUNIT: Interacts with EF1A1, facilitates EF1A1 distribution to the
CC membrane periphery and ruffles upon growth factor stimulation and
CC suppresses cell migration. {ECO:0000269|PubMed:19158340}.
CC -!- INTERACTION:
CC Q96QB1; P20936: RASA1; NbExp=7; IntAct=EBI-2608428, EBI-1026476;
CC Q96QB1; Q923Q2: Stard13; Xeno; NbExp=2; IntAct=EBI-2608428, EBI-8393503;
CC Q96QB1-1; Q04205: TNS; Xeno; NbExp=7; IntAct=EBI-15638708, EBI-2607590;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, focal adhesion.
CC Membrane; Peripheral membrane protein. Note=Colocalizes with EF1A1 at
CC actin-rich regions in the cell periphery.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=2;
CC IsoId=Q96QB1-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q96QB1-1; Sequence=VSP_037871, VSP_037872;
CC Name=3;
CC IsoId=Q96QB1-3; Sequence=VSP_037873, VSP_037874;
CC Name=4;
CC IsoId=Q96QB1-4; Sequence=VSP_037871, VSP_044651;
CC Name=5;
CC IsoId=Q96QB1-5; Sequence=VSP_046331, VSP_046332;
CC Name=6; Synonyms=i-4;
CC IsoId=Q96QB1-6; Sequence=VSP_053836, VSP_053837;
CC -!- TISSUE SPECIFICITY: Highest level of expression in the spleen, with
CC rather lower levels in prostate, testis, ovary, small intestine and
CC colon, but none in the thymus.
CC -!- DOMAIN: The SAM domain mediates interaction with EF1A1, and functions
CC as an autoinhibitory regulator of RhoGAP Activity.
CC {ECO:0000269|PubMed:18786931}.
CC -!- DOMAIN: The polybasic cluster is required for activation and mediates
CC binding to phosphatidylinositol-4,5-bisphosphate (PI(4,5)P(2))
CC containing membranes. {ECO:0000269|PubMed:18786931}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative promoter usage.
CC ubiquitously expressed, significantly down-regulated in multiple
CC carcinoma cell lines. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81637.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB21814.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DLC1ID40328ch8p22.html";
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DR EMBL; AF035119; AAB87700.1; -; mRNA.
DR EMBL; AF026219; AAB81637.1; ALT_INIT; mRNA.
DR EMBL; AF408781; AAK97501.1; -; Genomic_DNA.
DR EMBL; AF408768; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408769; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408770; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408771; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408772; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408773; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408774; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408775; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408776; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408777; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408778; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408779; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AF408780; AAK97501.1; JOINED; Genomic_DNA.
DR EMBL; AB051510; BAB21814.1; ALT_INIT; mRNA.
DR EMBL; AK024774; BAB14996.1; -; mRNA.
DR EMBL; AK299049; BAG61122.1; -; mRNA.
DR EMBL; AC015641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC019270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049842; AAH49842.1; -; mRNA.
DR EMBL; BC054511; AAH54511.1; -; mRNA.
DR EMBL; EU159199; ABX83661.1; -; mRNA.
DR EMBL; EU159200; ABX83662.1; -; mRNA.
DR CCDS; CCDS55201.1; -. [Q96QB1-4]
DR CCDS; CCDS5989.1; -. [Q96QB1-2]
DR CCDS; CCDS5990.1; -. [Q96QB1-1]
DR CCDS; CCDS5991.2; -. [Q96QB1-5]
DR CCDS; CCDS83253.1; -. [Q96QB1-6]
DR RefSeq; NP_001157743.1; NM_001164271.1. [Q96QB1-4]
DR RefSeq; NP_001303597.1; NM_001316668.1. [Q96QB1-6]
DR RefSeq; NP_001335010.1; NM_001348081.1. [Q96QB1-2]
DR RefSeq; NP_001335011.1; NM_001348082.1. [Q96QB1-4]
DR RefSeq; NP_001335012.1; NM_001348083.1. [Q96QB1-4]
DR RefSeq; NP_001335013.1; NM_001348084.1. [Q96QB1-4]
DR RefSeq; NP_006085.2; NM_006094.4. [Q96QB1-1]
DR RefSeq; NP_079043.3; NM_024767.3. [Q96QB1-5]
DR RefSeq; NP_872584.2; NM_182643.2. [Q96QB1-2]
DR RefSeq; XP_005273431.1; XM_005273374.1. [Q96QB1-2]
DR PDB; 2DKY; NMR; -; A=451-515.
DR PDB; 2GYT; NMR; -; A=451-513.
DR PDB; 2KAP; NMR; -; A=454-513.
DR PDB; 2LOZ; NMR; -; B=811-824.
DR PDB; 3KUQ; X-ray; 2.30 A; A=1074-1283.
DR PDB; 5FZT; X-ray; 2.10 A; B=904-926.
DR PDBsum; 2DKY; -.
DR PDBsum; 2GYT; -.
DR PDBsum; 2KAP; -.
DR PDBsum; 2LOZ; -.
DR PDBsum; 3KUQ; -.
DR PDBsum; 5FZT; -.
DR AlphaFoldDB; Q96QB1; -.
DR BMRB; Q96QB1; -.
DR SMR; Q96QB1; -.
DR BioGRID; 115667; 56.
DR CORUM; Q96QB1; -.
DR DIP; DIP-56928N; -.
DR IntAct; Q96QB1; 40.
DR MINT; Q96QB1; -.
DR STRING; 9606.ENSP00000276297; -.
DR iPTMnet; Q96QB1; -.
DR PhosphoSitePlus; Q96QB1; -.
DR BioMuta; DLC1; -.
DR DMDM; 313104315; -.
DR EPD; Q96QB1; -.
DR jPOST; Q96QB1; -.
DR MassIVE; Q96QB1; -.
DR MaxQB; Q96QB1; -.
DR PaxDb; Q96QB1; -.
DR PeptideAtlas; Q96QB1; -.
DR PRIDE; Q96QB1; -.
DR ProteomicsDB; 19782; -.
DR ProteomicsDB; 20045; -.
DR ProteomicsDB; 20421; -.
DR ProteomicsDB; 77848; -. [Q96QB1-2]
DR ProteomicsDB; 77849; -. [Q96QB1-1]
DR ProteomicsDB; 77850; -. [Q96QB1-3]
DR Antibodypedia; 22182; 227 antibodies from 36 providers.
DR CPTC; Q96QB1; 3 antibodies.
DR DNASU; 10395; -.
DR Ensembl; ENST00000276297.9; ENSP00000276297.4; ENSG00000164741.15. [Q96QB1-2]
DR Ensembl; ENST00000316609.9; ENSP00000321034.5; ENSG00000164741.15. [Q96QB1-3]
DR Ensembl; ENST00000358919.6; ENSP00000351797.2; ENSG00000164741.15. [Q96QB1-1]
DR Ensembl; ENST00000511869.1; ENSP00000425878.1; ENSG00000164741.15. [Q96QB1-5]
DR Ensembl; ENST00000512044.6; ENSP00000422595.2; ENSG00000164741.15. [Q96QB1-6]
DR Ensembl; ENST00000520226.5; ENSP00000428028.1; ENSG00000164741.15. [Q96QB1-4]
DR GeneID; 10395; -.
DR KEGG; hsa:10395; -.
DR MANE-Select; ENST00000276297.9; ENSP00000276297.4; NM_182643.3; NP_872584.2.
DR UCSC; uc003wwk.2; human. [Q96QB1-2]
DR CTD; 10395; -.
DR DisGeNET; 10395; -.
DR GeneCards; DLC1; -.
DR HGNC; HGNC:2897; DLC1.
DR HPA; ENSG00000164741; Low tissue specificity.
DR MalaCards; DLC1; -.
DR MIM; 604258; gene.
DR neXtProt; NX_Q96QB1; -.
DR OpenTargets; ENSG00000164741; -.
DR PharmGKB; PA27351; -.
DR VEuPathDB; HostDB:ENSG00000164741; -.
DR eggNOG; KOG2200; Eukaryota.
DR GeneTree; ENSGT00950000183061; -.
DR HOGENOM; CLU_004367_1_0_1; -.
DR InParanoid; Q96QB1; -.
DR OMA; AMSHESM; -.
DR OrthoDB; 218349at2759; -.
DR PhylomeDB; Q96QB1; -.
DR TreeFam; TF314044; -.
DR PathwayCommons; Q96QB1; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR SignaLink; Q96QB1; -.
DR SIGNOR; Q96QB1; -.
DR BioGRID-ORCS; 10395; 12 hits in 1079 CRISPR screens.
DR ChiTaRS; DLC1; human.
DR EvolutionaryTrace; Q96QB1; -.
DR GeneWiki; DLC1; -.
DR GenomeRNAi; 10395; -.
DR Pharos; Q96QB1; Tbio.
DR PRO; PR:Q96QB1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96QB1; protein.
DR Bgee; ENSG00000164741; Expressed in adrenal tissue and 180 other tissues.
DR ExpressionAtlas; Q96QB1; baseline and differential.
DR Genevisible; Q96QB1; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0030900; P:forebrain development; ISS:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0021575; P:hindbrain morphogenesis; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
DR IDEAL; IID00677; -.
DR InterPro; IPR028854; DLC1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR023393; START-like_dom_sf.
DR InterPro; IPR002913; START_lipid-bd_dom.
DR PANTHER; PTHR12659:SF2; PTHR12659:SF2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF01852; START; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50848; START; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Cell junction; Cytoplasm; GTPase activation; Membrane; Phosphoprotein;
KW Reference proteome; Tumor suppressor.
FT CHAIN 1..1528
FT /note="Rho GTPase-activating protein 7"
FT /id="PRO_0000056707"
FT DOMAIN 448..515
FT /note="SAM"
FT DOMAIN 1078..1284
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 1314..1521
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 72..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..884
FT /note="Focal adhesion-targeting (FAT)"
FT REGION 732..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..990
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1073
FT /note="Polybasic cluster (PBR)"
FT COMPBIAS 76..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63744"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..437
FT /note="Missing (in isoform 1 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9605766, ECO:0000303|Ref.2"
FT /id="VSP_037871"
FT VAR_SEQ 1..45
FT /note="MSVAIRKRSWEEHVTHWMGQPFNSDDRNTACHHGLVADSLQASME -> MGD
FT PKAHVMARPLRAPLRRSFSDHIRDSTARALDVIWKNTRDRRL (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21217778"
FT /id="VSP_053836"
FT VAR_SEQ 46..448
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21217778"
FT /id="VSP_053837"
FT VAR_SEQ 438..511
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044651"
FT VAR_SEQ 438..450
FT /note="TAIQGISEKEKAE -> MCRKKPDTMILTQ (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9605766, ECO:0000303|Ref.2"
FT /id="VSP_037872"
FT VAR_SEQ 450..498
FT /note="EIEAKEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEA ->
FT AVKSVKLEVDEDKSTKGSNFSNSEVAIGLSPYTFPQKRLFHVAGEENIT (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037873"
FT VAR_SEQ 450..463
FT /note="EIEAKEACDWLRAT -> GKLTFWFCFLANLF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046331"
FT VAR_SEQ 464..1528
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046332"
FT VAR_SEQ 499..1528
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037874"
FT VARIANT 27
FT /note="R -> C (in dbSNP:rs34575560)"
FT /id="VAR_059293"
FT VARIANT 81
FT /note="L -> V (in dbSNP:rs3816748)"
FT /id="VAR_059294"
FT VARIANT 254
FT /note="Q -> H (in dbSNP:rs11203495)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_059295"
FT VARIANT 255
FT /note="N -> D (in dbSNP:rs11203494)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_059296"
FT VARIANT 260
FT /note="T -> I (in dbSNP:rs3816747)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_059297"
FT VARIANT 320
FT /note="Q -> H (in dbSNP:rs34591797)"
FT /id="VAR_059298"
FT VARIANT 712
FT /note="N -> S (in dbSNP:rs1044092)"
FT /evidence="ECO:0000269|PubMed:10649492,
FT ECO:0000269|PubMed:9605766"
FT /id="VAR_014229"
FT VARIANT 791
FT /note="V -> M (in dbSNP:rs532841)"
FT /evidence="ECO:0000269|PubMed:10649492,
FT ECO:0000269|PubMed:11214970, ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT /id="VAR_014230"
FT VARIANT 959
FT /note="T -> A (in dbSNP:rs121908500)"
FT /evidence="ECO:0000269|PubMed:10649492"
FT /id="VAR_014231"
FT VARIANT 998
FT /note="H -> Q (in dbSNP:rs149295187)"
FT /evidence="ECO:0000269|PubMed:10649492"
FT /id="VAR_014232"
FT VARIANT 1025
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:10649492"
FT /id="VAR_014233"
FT VARIANT 1199
FT /note="E -> V (in dbSNP:rs1044093)"
FT /evidence="ECO:0000269|PubMed:10649492,
FT ECO:0000269|PubMed:9605766"
FT /id="VAR_014234"
FT VARIANT 1209
FT /note="S -> C (in dbSNP:rs1044094)"
FT /evidence="ECO:0000269|PubMed:10649492,
FT ECO:0000269|PubMed:9605766"
FT /id="VAR_014235"
FT MUTAGEN 475
FT /note="F->G: Abolishes interaction with EF1A1."
FT /evidence="ECO:0000269|PubMed:19158340"
FT MUTAGEN 476
FT /note="L->G: Abolishes interaction with EF1A1."
FT /evidence="ECO:0000269|PubMed:19158340"
FT MUTAGEN 879
FT /note="Y->F: Unable to displace endogenous DLC1 from focal
FT adhesions."
FT /evidence="ECO:0000269|PubMed:18786931"
FT MUTAGEN 1114
FT /note="R->E: No catalytic activity."
FT /evidence="ECO:0000269|PubMed:19158340"
FT CONFLICT 43
FT /note="S -> C (in Ref. 5; BAB14996)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="T -> I (in Ref. 5; BAB14996)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="H -> L (in Ref. 4; BAB21814)"
FT /evidence="ECO:0000305"
FT CONFLICT 1114
FT /note="R -> K (in Ref. 1; AAB87700)"
FT /evidence="ECO:0000305"
FT CONFLICT 1364
FT /note="P -> R (in Ref. 1; AAB87700)"
FT /evidence="ECO:0000305"
FT HELIX 449..463
FT /evidence="ECO:0007829|PDB:2DKY"
FT HELIX 468..473
FT /evidence="ECO:0007829|PDB:2DKY"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:2KAP"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:2DKY"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2DKY"
FT HELIX 493..509
FT /evidence="ECO:0007829|PDB:2DKY"
FT TURN 510..514
FT /evidence="ECO:0007829|PDB:2DKY"
FT HELIX 906..920
FT /evidence="ECO:0007829|PDB:5FZT"
FT HELIX 1080..1087
FT /evidence="ECO:0007829|PDB:3KUQ"
FT STRAND 1088..1091
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1093..1105
FT /evidence="ECO:0007829|PDB:3KUQ"
FT TURN 1110..1114
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1119..1129
FT /evidence="ECO:0007829|PDB:3KUQ"
FT STRAND 1131..1134
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1143..1156
FT /evidence="ECO:0007829|PDB:3KUQ"
FT STRAND 1157..1159
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1166..1176
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1179..1181
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1182..1191
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1195..1213
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1215..1218
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1222..1234
FT /evidence="ECO:0007829|PDB:3KUQ"
FT HELIX 1260..1278
FT /evidence="ECO:0007829|PDB:3KUQ"
FT CONFLICT Q96QB1-6:49..50
FT /note="EA -> KP (in Ref. 8; ABX83661/ABX83662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1528 AA; 170591 MW; 5D20F29CC606302E CRC64;
MSVAIRKRSW EEHVTHWMGQ PFNSDDRNTA CHHGLVADSL QASMEKDATL NVDRKEKCVS
LPDCCHGSEL RDFPGRPMGH LSKDVDENDS HEGEDQFLSL EASTETLVHV SDEDNNADLC
LTDDKQVLNT QGQKTSGQHM IQGAGSLEKA LPIIQSNQVS SNSWGIAGET ELALVKESGE
RKVTDSISKS LELCNEISLS EIKDAPKVNA VDTLNVKDIA PEKQLLNSAV IAQQRRKPDP
PKDENERSTC NVVQNEFLDT PCTNRGLPLL KTDFGSCLLQ PPSCPNGMSA ENGLEKSGFS
QHQNKSPPKV KAEDGMQCLQ LKETLATQEP TDNQVRLRKR KEIREDRDRA RLDSMVLLIM
KLDQLDQDIE NALSTSSSPS GTPTNLRRHV PDLESGSESG ADTISVNQTR VNLSSDTEST
DLPSSTPVAN SGTKPKTTAI QGISEKEKAE IEAKEACDWL RATGFPQYAQ LYEDFLFPID
ISLVKREHDF LDRDAIEALC RRLNTLNKCA VMKLEISPHR KRSDDSDEDE PCAISGKWTF
QRDSKRWSRL EEFDVFSPKQ DLVPGSPDDS HPKDGPSPGG TLMDLSERQE VSSVRSLSST
GSLPSHAPPS EDAATPRTNS VISVCSSSNL AGNDDSFGSL PSPKELSSFS FSMKGHEKTA
KSKTRSLLKR MESLKLKSSH HSKHKAPSKL GLIISGPILQ EGMDEEKLKQ LNCVEISALN
GNRINVPMVR KRSVSNSTQT SSSSSQSETS SAVSTPSPVT RTRSLSACNK RVGMYLEGFD
PFNQSTFNNV VEQNFKNRES YPEDTVFYIP EDHKPGTFPK ALTNGSFSPS GNNGSVNWRT
GSFHGPGHIS LRRENSSDSP KELKRRNSSS SMSSRLSIYD NVPGSILYSS SGDLADLENE
DIFPELDDIL YHVKGMQRIV NQWSEKFSDE GDSDSALDSV SPCPSSPKQI HLDVDNDRTT
PSDLDSTGNS LNEPEEPSEI PERRDSGVGA SLTRSNRHRL RWHSFQSSHR PSLNSVSLQI
NCQSVAQMNL LQKYSLLKLT ALLEKYTPSN KHGFSWAVPK FMKRIKVPDY KDRSVFGVPL
TVNVQRTGQP LPQSIQQAMR YLRNHCLDQV GLFRKSGVKS RIQALRQMNE GAIDCVNYEG
QSAYDVADML KQYFRDLPEP LMTNKLSETF LQIYQYVPKD QRLQAIKAAI MLLPDENREV
LQTLLYFLSD VTAAVKENQM TPTNLAVCLA PSLFHLNTLK RENSSPRVMQ RKQSLGKPDQ
KDLNENLAAT QGLAHMIAEC KKLFQVPEEM SRCRNSYTEQ ELKPLTLEAL GHLGNDDSAD
YQHFLQDCVD GLFKEVKEKF KGWVSYSTSE QAELSYKKVS EGPPLRLWRS VIEVPAVPEE
ILKRLLKEQH LWDVDLLDSK VIEILDSQTE IYQYVQNSMA PHPARDYVVL RTWRTNLPKG
ACALLLTSVD HDRAPVVGVR VNVLLSRYLI EPCGPGKSKL TYMCRVDLRG HMPEWYTKSF
GHLCAAEVVK IRDSFSNQNT ETKDTKSR
