RHG07_MOUSE
ID RHG07_MOUSE Reviewed; 1092 AA.
AC Q9R0Z9; Q3TRX3; Q3UH75; Q8R541;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rho GTPase-activating protein 7;
DE AltName: Full=Deleted in liver cancer 1 protein homolog;
DE Short=DLC-1;
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, Stard12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=10702663; DOI=10.1159/000015462;
RA Yuan B.-Z., Keck-Waggoner C.L., Zimonjic D.B., Thorgeirsson S.S.,
RA Popescu N.C.;
RT "Assignment and cloning of mouse Arhgap7 to chromosome 8A4-B2, a conserved
RT syntenic region of human chromosome 8p22-p21.";
RL Cytogenet. Cell Genet. 87:189-190(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=12034501; DOI=10.1016/s0378-1119(02)00462-6;
RA Durkin M.E., Yuan B.-Z., Thorgeirsson S.S., Popescu N.C.;
RT "Gene structure, tissue expression, and linkage mapping of the mouse DLC-1
RT gene (Arhgap7).";
RL Gene 288:119-127(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1064 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC {ECO:0000250}.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell junction, focal
CC adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Note=Colocalizes with EF1A1 at actin-rich
CC regions in the cell periphery. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9R0Z9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9R0Z9-2; Sequence=VSP_026144;
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest levels in heart,
CC liver and lung.
CC -!- DOMAIN: The SAM domain mediates interaction with EF1A1, and functions
CC as an autoinhibitory regulator of RhoGAP Activity. {ECO:0000250}.
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:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL87620.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF178078; AAD51760.1; -; mRNA.
DR EMBL; AF411442; AAL87620.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF411435; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411436; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411437; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411438; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411439; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411440; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AF411441; AAL87620.1; JOINED; Genomic_DNA.
DR EMBL; AK147539; BAE27982.1; -; mRNA.
DR EMBL; AK162413; BAE36903.1; -; mRNA.
DR CCDS; CCDS40322.1; -. [Q9R0Z9-1]
DR CCDS; CCDS57616.1; -. [Q9R0Z9-2]
DR RefSeq; NP_001181870.1; NM_001194941.1.
DR RefSeq; NP_056617.2; NM_015802.3.
DR AlphaFoldDB; Q9R0Z9; -.
DR SMR; Q9R0Z9; -.
DR BioGRID; 206100; 1.
DR IntAct; Q9R0Z9; 1.
DR STRING; 10090.ENSMUSP00000033923; -.
DR iPTMnet; Q9R0Z9; -.
DR PhosphoSitePlus; Q9R0Z9; -.
DR jPOST; Q9R0Z9; -.
DR MaxQB; Q9R0Z9; -.
DR PaxDb; Q9R0Z9; -.
DR PRIDE; Q9R0Z9; -.
DR ProteomicsDB; 253275; -. [Q9R0Z9-1]
DR ProteomicsDB; 253276; -. [Q9R0Z9-2]
DR GeneID; 50768; -.
DR KEGG; mmu:50768; -.
DR CTD; 10395; -.
DR MGI; MGI:1354949; Dlc1.
DR eggNOG; KOG2200; Eukaryota.
DR InParanoid; Q9R0Z9; -.
DR PhylomeDB; Q9R0Z9; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR BioGRID-ORCS; 50768; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Dlc1; mouse.
DR PRO; PR:Q9R0Z9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R0Z9; protein.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
DR GO; GO:0017166; F:vinculin binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0021575; P:hindbrain morphogenesis; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; ISO:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.530.20; -; 1.
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 Alternative splicing; Cell junction; Cytoplasm; GTPase activation;
KW Membrane; Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..1092
FT /note="Rho GTPase-activating protein 7"
FT /id="PRO_0000056708"
FT DOMAIN 11..78
FT /note="SAM"
FT DOMAIN 642..848
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 878..1085
FT /note="START"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT REGION 121..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..448
FT /note="Focal adhesion-targeting (FAT)"
FT /evidence="ECO:0000250"
FT REGION 297..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..637
FT /note="Polybasic cluster (PBR)"
FT /evidence="ECO:0000250"
FT COMPBIAS 129..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63744"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QB1"
FT VAR_SEQ 1..13
FT /note="MCRDEPDTMILTQ -> MGDPEGHVMARPLRGPLRRSFSDHIRDSTARALDA
FT IWKNTRERRLAE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026144"
FT CONFLICT 42
FT /note="V -> I (in Ref. 3; BAE36903/BAE27982)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="F -> S (in Ref. 3; BAE36903/BAE27982)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="G -> R (in Ref. 1; AAD51760)"
FT /evidence="ECO:0000305"
FT CONFLICT 421..422
FT /note="HD -> SH (in Ref. 1; AAD51760)"
FT /evidence="ECO:0000305"
FT CONFLICT 715..717
FT /note="KQY -> NRN (in Ref. 1; AAD51760)"
FT /evidence="ECO:0000305"
FT CONFLICT 730..735
FT /note="LSETFL -> FSEPSM (in Ref. 1; AAD51760)"
FT /evidence="ECO:0000305"
FT CONFLICT 917
FT /note="D -> E (in Ref. 3; BAE36903/BAE27982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1092 AA; 123367 MW; 9B5DC3103986A751 CRC64;
MCRDEPDTMI LTQIEAKEAC DWLRVTGFPQ YAQLYEDLLF PVDIALVKRE HDFLDRDAIE
ALCRRLNTLN KCAVMKLEIS PHRKRSEDSD EDEPCAISGK WTFQRDSKRW SRLEEFDVFF
PKQDPIPGSP DNSRLQSATS HESMLTDLSE HQEVASVRSL SSTSSSVPTH AAHSGDATTP
RTNSVISVCS SGHFVGNDDS FSSLPSPKEL SSFSFSMKGH HEKNTKSKTR SLLKRMESLK
LKGSHHSKHK APSKLGLIIS APILQEGMDE AKLKQLNCVE ISALNGNHIN VPMVRKRSVS
NSTQTSSSSS QSETSSAVST PSPVTRTRSL STCNKRVGMY LEGFDPFSQS TLNNVTEQNY
KNRESYPEDT VFYIPEDHKP GTFPKALSHG SFCPSGNSSV NWRTGSFHGP GHLSLRRENS
HDSPKELKRR NSSSSLSSRL SIYDNVPGSI LYSSSGELAD LENEDIFPEL DDILYHVKGM
QRIVNQWSEK FSDEGDSDSA LDSVSPCPSS PKQIHLDVDH DRRTPSDLDS TGNSLNEPEE
PTDIPERRDS GVGASLTRCN RHRLRWHSFQ SSHRPSLNSV SLQINCQSVA QMNLLQKYSL
LKLTALLEKY TPSNKHGFSW AVPKFMKRIK VPDYKDRSVF GVPLTVNVQR SGQPLPQSIQ
QAMRYLRNHC LDQVGLFRKS GVKSRIQALR QMNESAEDNV NYEGQSAYDV ADMLKQYFRD
LPEPLMTNKL SETFLQIYQY VPKDQRLQAI KAAIMLLPDE NREVLQTLLY FLSDVTAAVK
ENQMTPTNLA VCLAPSLFHL NTLKRENSSP RVMQRKQSLG KPDQKDLNEN LAATQGLAHM
IAECKKLFQV PEEMSRCRNS YTEQELKPLT LEALGHLNSD QPADYRHFLQ DCVDGLFKEV
KEKFKGWVSY PTSEQADLSY KKVSEGPPLR LWRSTIEVPA APEEILKRLL KEQHLWDVDL
LDSKVIEILD SQTEIYQYVQ NSMAPHPARD YVVLRTWRTN LPRGACALLL TSVDHDRAPV
AGVRVNVLLS RYLIEPCGSG KSKLTYMCRA DLRGHMPEWY SKSFGHLCAA EVVKIRDSFS
NQNTESKDTR SR
