ARHG7_MOUSE
ID ARHG7_MOUSE Reviewed; 862 AA.
AC Q9ES28; O08757; Q3UTS5; Q6XPA5; Q6ZQI5; Q8C750; Q91ZZ6; Q9ES27;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Rho guanine nucleotide exchange factor 7;
DE AltName: Full=Beta-Pix;
DE AltName: Full=PAK-interacting exchange factor beta;
DE AltName: Full=p85SPR;
GN Name=Arhgef7; Synonyms=Kiaa0142, Pak3bp;
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 [LARGE SCALE MRNA] (ISOFORM E).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G AND H).
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=15120616; DOI=10.1016/j.bbrc.2004.04.039;
RA Rhee S., Yang S.J., Lee S.J., Park D.;
RT "betaPix-b(L), a novel isoform of betaPix, is generated by alternative
RT translation.";
RL Biochem. Biophys. Res. Commun. 318:415-421(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 59-862 (ISOFORM B), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 150-862 (ISOFORM C), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10860822; DOI=10.1006/bbrc.2000.2845;
RA Kim S., Kim T., Lee D., Park S.-H., Kim H., Park D.;
RT "Molecular cloning of neuronally expressed mouse betaPix isoforms.";
RL Biochem. Biophys. Res. Commun. 272:721-725(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-862 (ISOFORM E), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11266127;
RA Kim T., Park D.;
RT "Molecular cloning and characterization of a novel mouse betaPix isoform.";
RL Mol. Cells 11:89-94(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 126-862 (ISOFORM A).
RC TISSUE=Thymus;
RX PubMed=9207241; DOI=10.1006/bbrc.1997.6875;
RA Oh W.K., Yoo J.C., Jo D., Song Y.H., Kim M.G., Park D.;
RT "Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its
RT localization in focal adhesion.";
RL Biochem. Biophys. Res. Commun. 235:794-798(1997).
RN [8]
RP INTERACTION WITH GIT1.
RX PubMed=10428811; DOI=10.1074/jbc.274.32.22393;
RA Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T.,
RA Taylor S.J., Cerione R.A.;
RT "A tyrosine-phosphorylated protein that binds to an important regulatory
RT region on the cool family of p21-activated kinase-binding proteins.";
RL J. Biol. Chem. 274:22393-22400(1999).
RN [9]
RP INTERACTION WITH GIT1 AND TGFB1I1.
RX PubMed=12153727; DOI=10.1093/oxfordjournals.jbchem.a003222;
RA Nishiya N., Shirai T., Suzuki W., Nose K.;
RT "Hic-5 interacts with GIT1 with a different binding mode from paxillin.";
RL J. Biochem. 132:279-289(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [11]
RP INTERACTION WITH YWHAZ.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [12]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PTK2/FAK1.
RX PubMed=17093062; DOI=10.1091/mbc.e06-03-0207;
RA Chang F., Lemmon C.A., Park D., Romer L.H.;
RT "FAK potentiates Rac1 activation and localization to matrix adhesion sites:
RT a role for betaPIX.";
RL Mol. Biol. Cell 18:253-264(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-497, 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 [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PARVB.
RX PubMed=18325335; DOI=10.1016/j.febslet.2008.01.064;
RA Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H.,
RA Nishino I., Hayashi Y.K.;
RT "Affixin activates Rac1 via betaPIX in C2C12 myoblast.";
RL FEBS Lett. 582:1189-1196(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-155; SER-164;
RP SER-497; SER-673 AND SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 164-220.
RX PubMed=16307729; DOI=10.1016/j.bbrc.2005.10.212;
RA Li X., Liu X., Sun F., Gao J., Zhou H., Gao G.F., Bartlam M., Rao Z.;
RT "Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-
RT activated kinase-interacting exchange factor.";
RL Biochem. Biophys. Res. Commun. 339:407-414(2006).
CC -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and
CC can induce membrane ruffling. May function as a positive regulator of
CC apoptosis. Functions in cell migration, attachment and cell spreading.
CC Promotes targeting of RAC1 to focal adhesions. Downstream of NMDA
CC receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of
CC spines and synapses in hippocampal neurons (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:17093062}.
CC -!- SUBUNIT: Interacts with PAK kinases through the SH3 domain. Interacts
CC with unphosphorylated PAK1. Interacts with ITCH. Interacts with SCRIB;
CC interaction is direct and may play a role in regulation of apoptosis
CC (By similarity). Interacts with GIT1 and TGFB1I1. Interacts with FRMPD4
CC (via N-terminus). Interacts with CaMK1. Interacts with BIN2 (By
CC similarity). Interacts with PTK2/FAK1 and RAC1. Interacts with PARVB.
CC Interacts with YWHAZ (PubMed:16959763). {ECO:0000250,
CC ECO:0000269|PubMed:10428811, ECO:0000269|PubMed:12153727,
CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:17093062,
CC ECO:0000269|PubMed:18325335}.
CC -!- INTERACTION:
CC Q9ES28; Q68FF6: Git1; NbExp=2; IntAct=EBI-642580, EBI-645933;
CC Q9ES28; Q9JLQ2: Git2; NbExp=6; IntAct=EBI-642580, EBI-642860;
CC Q9ES28; Q9ES46: Parvb; NbExp=2; IntAct=EBI-642580, EBI-6914996;
CC Q9ES28; Q9Z272: Git1; Xeno; NbExp=2; IntAct=EBI-642580, EBI-3842379;
CC Q9ES28; Q14161: GIT2; Xeno; NbExp=2; IntAct=EBI-642580, EBI-1046878;
CC Q9ES28; Q9HBI1: PARVB; Xeno; NbExp=10; IntAct=EBI-642580, EBI-1047679;
CC Q9ES28-2; Q9WV48: Shank1; Xeno; NbExp=6; IntAct=EBI-8620514, EBI-80909;
CC Q9ES28-2; Q9QX74: Shank2; Xeno; NbExp=4; IntAct=EBI-8620514, EBI-397902;
CC Q9ES28-2; Q9JLU4: Shank3; Xeno; NbExp=2; IntAct=EBI-8620514, EBI-6271152;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell projection,
CC ruffle. Cytoplasm, cell cortex. Cell projection, lamellipodium.
CC Note=Detected at cell adhesions. A small proportion is detected at
CC focal adhesions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC Name=B;
CC IsoId=Q9ES28-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9ES28-2; Sequence=VSP_001817;
CC Name=C;
CC IsoId=Q9ES28-3; Sequence=VSP_001816;
CC Name=D;
CC IsoId=Q9ES28-4; Sequence=VSP_023052, VSP_023053, VSP_001817;
CC Name=E; Synonyms=d;
CC IsoId=Q9ES28-5; Sequence=VSP_023055, VSP_023057;
CC Name=F;
CC IsoId=Q9ES28-6; Sequence=VSP_023052, VSP_023053, VSP_023054,
CC VSP_023056;
CC Name=G; Synonyms=b(L);
CC IsoId=Q9ES28-7; Sequence=VSP_023052, VSP_023053;
CC Name=H; Synonyms=b;
CC IsoId=Q9ES28-8; Sequence=VSP_023051;
CC -!- TISSUE SPECIFICITY: Seems to be expressed in the central nervous
CC system. Isoform B, isoform C and isoform E are expressed with highest
CC levels in brain and testis. {ECO:0000269|PubMed:10860822,
CC ECO:0000269|PubMed:11266127}.
CC -!- PTM: Phosphorylated on Ser-673 by CaMK1; enhancement of GEF activity
CC and downstream activation of RAC1 (By similarity). Phosphorylated by
CC PTK2/FAK1; this promotes interaction with RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:17093062}.
CC -!- MISCELLANEOUS: [Isoform H]: Produced by alternative initiation at Met-
CC 158 of isoform G. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB57691.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG18017.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG18018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH44838.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK97363.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC35033.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC97874.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129064; BAC97874.1; ALT_INIT; mRNA.
DR EMBL; AY220301; AAO65479.1; -; mRNA.
DR EMBL; AK052545; BAC35033.1; ALT_INIT; mRNA.
DR EMBL; AK139156; BAE23905.1; -; mRNA.
DR EMBL; BC044838; AAH44838.1; ALT_INIT; mRNA.
DR EMBL; AF247654; AAG18017.1; ALT_INIT; mRNA.
DR EMBL; AF247655; AAG18018.1; ALT_INIT; mRNA.
DR EMBL; AF343877; AAK97363.1; ALT_INIT; mRNA.
DR EMBL; U96634; AAB57691.1; ALT_INIT; mRNA.
DR CCDS; CCDS52480.1; -. [Q9ES28-5]
DR CCDS; CCDS52481.1; -. [Q9ES28-8]
DR RefSeq; NP_001106989.1; NM_001113517.1. [Q9ES28-5]
DR RefSeq; NP_001106990.1; NM_001113518.1. [Q9ES28-8]
DR RefSeq; NP_059098.2; NM_017402.4.
DR RefSeq; XP_006508904.2; XM_006508841.2.
DR RefSeq; XP_006508906.2; XM_006508843.3.
DR RefSeq; XP_006508907.2; XM_006508844.2.
DR PDB; 2ESW; X-ray; 2.01 A; A/B=164-220.
DR PDB; 6JMT; X-ray; 2.80 A; I/J/K/L/M/N=685-705.
DR PDBsum; 2ESW; -.
DR PDBsum; 6JMT; -.
DR AlphaFoldDB; Q9ES28; -.
DR BMRB; Q9ES28; -.
DR SMR; Q9ES28; -.
DR BioGRID; 207566; 55.
DR CORUM; Q9ES28; -.
DR IntAct; Q9ES28; 23.
DR MINT; Q9ES28; -.
DR STRING; 10090.ENSMUSP00000106534; -.
DR iPTMnet; Q9ES28; -.
DR PhosphoSitePlus; Q9ES28; -.
DR SwissPalm; Q9ES28; -.
DR EPD; Q9ES28; -.
DR jPOST; Q9ES28; -.
DR MaxQB; Q9ES28; -.
DR PaxDb; Q9ES28; -.
DR PeptideAtlas; Q9ES28; -.
DR PRIDE; Q9ES28; -.
DR ProteomicsDB; 265083; -. [Q9ES28-1]
DR ProteomicsDB; 265084; -. [Q9ES28-2]
DR ProteomicsDB; 265085; -. [Q9ES28-3]
DR ProteomicsDB; 265086; -. [Q9ES28-4]
DR ProteomicsDB; 265087; -. [Q9ES28-5]
DR ProteomicsDB; 265088; -. [Q9ES28-6]
DR ProteomicsDB; 265089; -. [Q9ES28-7]
DR ProteomicsDB; 265090; -. [Q9ES28-8]
DR Antibodypedia; 1486; 301 antibodies from 33 providers.
DR DNASU; 54126; -.
DR Ensembl; ENSMUST00000098938; ENSMUSP00000096538; ENSMUSG00000031511. [Q9ES28-8]
DR Ensembl; ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511. [Q9ES28-5]
DR GeneID; 54126; -.
DR KEGG; mmu:54126; -.
DR UCSC; uc009kvu.2; mouse. [Q9ES28-2]
DR UCSC; uc009kvv.2; mouse. [Q9ES28-5]
DR UCSC; uc009kvw.2; mouse. [Q9ES28-4]
DR UCSC; uc009kvx.2; mouse. [Q9ES28-1]
DR CTD; 8874; -.
DR MGI; MGI:1860493; Arhgef7.
DR VEuPathDB; HostDB:ENSMUSG00000031511; -.
DR eggNOG; KOG2070; Eukaryota.
DR GeneTree; ENSGT00940000155360; -.
DR InParanoid; Q9ES28; -.
DR OMA; TETEYAK; -.
DR OrthoDB; 547556at2759; -.
DR PhylomeDB; Q9ES28; -.
DR TreeFam; TF316105; -.
DR Reactome; R-MMU-182971; EGFR downregulation.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA 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 Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR Reactome; R-MMU-9013424; RHOV GTPase cycle.
DR BioGRID-ORCS; 54126; 21 hits in 73 CRISPR screens.
DR ChiTaRS; Arhgef7; mouse.
DR EvolutionaryTrace; Q9ES28; -.
DR PRO; PR:Q9ES28; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ES28; protein.
DR Bgee; ENSMUSG00000031511; Expressed in cortical plate and 261 other tissues.
DR ExpressionAtlas; Q9ES28; baseline and differential.
DR Genevisible; Q9ES28; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0000322; C:storage vacuole; IDA:MGI.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0043615; P:astrocyte cell migration; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:1905833; P:negative regulation of microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0099140; P:presynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:1904424; P:regulation of GTP binding; ISO:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
DR CDD; cd00014; CH; 1.
DR CDD; cd01225; PH_Cool_Pix; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd12061; SH3_betaPIX; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035789; BetaPIX_SH3.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR032409; GEF6/7_CC.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR046376; PH_Cool_Pix.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF16523; betaPIX_CC; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Cell junction;
KW Cell projection; Coiled coil; Cytoplasm;
KW Guanine-nucleotide releasing factor; Neurogenesis; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..862
FT /note="Rho guanine nucleotide exchange factor 7"
FT /id="PRO_0000080922"
FT DOMAIN 1..112
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 163..222
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 250..430
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 452..557
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 559..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 804..854
FT /evidence="ECO:0000255"
FT COMPBIAS 559..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14155"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14155"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform H)"
FT /evidence="ECO:0000303|PubMed:10860822,
FT ECO:0000303|PubMed:15120616"
FT /id="VSP_023051"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform D, isoform F and isoform G)"
FT /evidence="ECO:0000303|PubMed:15120616,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_023052"
FT VAR_SEQ 53..55
FT /note="IEK -> MLQ (in isoform D, isoform F and isoform G)"
FT /evidence="ECO:0000303|PubMed:15120616,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_023053"
FT VAR_SEQ 576..650
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:10860822"
FT /id="VSP_001816"
FT VAR_SEQ 712..820
FT /note="TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHS
FT YRMGSASRSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQEL
FT -> SECRSSPRVGTDYKQLLHGLAALEREVSGA (in isoform F)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023054"
FT VAR_SEQ 712..771
FT /note="TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSEDSEYDSIWTAHS
FT YRMGSASR -> S (in isoform A and isoform D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9207241"
FT /id="VSP_001817"
FT VAR_SEQ 772..824
FT /note="SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQELRQD
FT N -> KSCCSYISHQN (in isoform E)"
FT /evidence="ECO:0000303|PubMed:11266127,
FT ECO:0000303|PubMed:14621295, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023055"
FT VAR_SEQ 821..862
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023056"
FT VAR_SEQ 825..862
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:11266127,
FT ECO:0000303|PubMed:14621295, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023057"
FT CONFLICT 485..488
FT /note="NLLL -> KPSV (in Ref. 2; AAO65479, 5; AAG18017/
FT AAG18018 and 7; AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> P (in Ref. 2; AAO65479, 5; AAG18017/AAG18018
FT and 7; AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="S -> R (in Ref. 2; AAO65479, 5; AAG18017 and 7;
FT AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 624..625
FT /note="KT -> PH (in Ref. 7; AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="P -> A (in Ref. 2; AAO65479 and 7; AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="S -> G (in Ref. 7; AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 633
FT /note="C -> W (in Ref. 2; AAO65479, 5; AAG18017 and 7;
FT AAB57691)"
FT /evidence="ECO:0000305"
FT CONFLICT 635..636
FT /note="RP -> WT (in Ref. 7; AAB57691)"
FT /evidence="ECO:0000305"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2ESW"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:2ESW"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:2ESW"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2ESW"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2ESW"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2ESW"
FT HELIX 686..698
FT /evidence="ECO:0007829|PDB:6JMT"
SQ SEQUENCE 862 AA; 97056 MW; 46D61B606B8391B4 CRC64;
MNSAEQTVTW LITLGVLESP KKTISDPEVF LQASLKDGVV LCRLLERLLP GTIEKVYPEP
RNESECLSNI REFLRACGAS LRLETFDAND LYQGQNFNKV LSSLVTLNKV TADIGLGSDS
VCARPSSHRI KSFDSLGSQS SHSRTSKLLQ SQYRSLDMTD NTNSQLVVRA KFNFQQTNED
ELSFSKGDVI HVTRVEEGGW WEGTHNGRTG WFPSNYVREI KPSEKPVSPK SGTLKSPPKG
FDTTAINKSY YNVVLQNILE TEHEYSKELQ SVLSTYLRPL QTSDKLSSAN TSYLMGNLEE
ISSFQQVLVQ SLEECTKSPE AQQRVGGCFL SLMPQMRTLY LAYCANHPSA VSVLTEHSED
LGEFMETKGA SSPGILVLTT GLSKPFMRLD KYPTLLKELE RHMEDYHPDR QDIQKSMTAF
KNLSAQCQEV RKRKELELQI LTEPIRSWEG DDIKTLGSVT YMSQVTIQCA GSEEKNERYL
LLFPNLLLML SASPRMSGFI YQGKLPTTGM TITKLEDSEN HRNAFEISGS MIERILVSCT
SQQDLHEWVE HLQKQTKVTS VSNPTIKPHS VPSHTLPSHP LTPSSKHADS KPVALTPAYH
TLPHPSHHGT PHTTISWGPL EPPKTPKPWS LSCLRPAPPL RPSAALCYKE DLSKSPKTMK
KLLPKRKPER KPSDEEFAVR KSTAALEEDA QILKVIEAYC TSAKTRQTLN STWQGTDLMH
NHVLADDDQS SLDSLGRRSS LSRLEPSDLS EDSEYDSIWT AHSYRMGSAS RSRKESAPQV
LLPEEEKIIV EETKSNGQTV IEEKSLVDTV YALKDEVQEL RQDNKKMKKS LEEEQRARKD
LEKLVRKVLK NMNDPAWDET NL
