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Rho guanine nucleotide exchange factor 7 (Beta-Pix) (PAK-interacting exchange factor beta) (p85SPR)

 ARHG7_MOUSE             Reviewed;         862 AA.
Q9ES28; O08757; Q3UTS5; Q6XPA5; Q6ZQI5; Q8C750; Q91ZZ6; Q9ES27;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
20-JUN-2018, entry version 169.
RecName: Full=Rho guanine nucleotide exchange factor 7;
AltName: Full=Beta-Pix;
AltName: Full=PAK-interacting exchange factor beta;
AltName: Full=p85SPR;
Name=Arhgef7; Synonyms=Kiaa0142, Pak3bp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G AND H).
STRAIN=ICR; TISSUE=Brain;
PubMed=15120616; DOI=10.1016/j.bbrc.2004.04.039;
Rhee S., Yang S.J., Lee S.J., Park D.;
"betaPix-b(L), a novel isoform of betaPix, is generated by alternative
translation.";
Biochem. Biophys. Res. Commun. 318:415-421(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 59-862 (ISOFORM B), NUCLEOTIDE SEQUENCE
[MRNA] OF 150-862 (ISOFORM C), AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=10860822; DOI=10.1006/bbrc.2000.2845;
Kim S., Kim T., Lee D., Park S.-H., Kim H., Park D.;
"Molecular cloning of neuronally expressed mouse betaPix isoforms.";
Biochem. Biophys. Res. Commun. 272:721-725(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 63-862 (ISOFORM E), AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=11266127;
Kim T., Park D.;
"Molecular cloning and characterization of a novel mouse betaPix
isoform.";
Mol. Cells 11:89-94(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 126-862 (ISOFORM A).
TISSUE=Thymus;
PubMed=9207241; DOI=10.1006/bbrc.1997.6875;
Oh W.K., Yoo J.C., Jo D., Song Y.H., Kim M.G., Park D.;
"Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and
its localization in focal adhesion.";
Biochem. Biophys. Res. Commun. 235:794-798(1997).
[8]
INTERACTION WITH GIT1.
PubMed=10428811; DOI=10.1074/jbc.274.32.22393;
Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T.,
Taylor S.J., Cerione R.A.;
"A tyrosine-phosphorylated protein that binds to an important
regulatory region on the cool family of p21-activated kinase-binding
proteins.";
J. Biol. Chem. 274:22393-22400(1999).
[9]
INTERACTION WITH GIT1 AND TGFB1I1.
PubMed=12153727; DOI=10.1093/oxfordjournals.jbchem.a003222;
Nishiya N., Shirai T., Suzuki W., Nose K.;
"Hic-5 interacts with GIT1 with a different binding mode from
paxillin.";
J. Biochem. 132:279-289(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[11]
FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
PTK2/FAK1.
PubMed=17093062; DOI=10.1091/mbc.E06-03-0207;
Chang F., Lemmon C.A., Park D., Romer L.H.;
"FAK potentiates Rac1 activation and localization to matrix adhesion
sites: a role for betaPIX.";
Mol. Biol. Cell 18:253-264(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-497, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH PARVB.
PubMed=18325335; DOI=10.1016/j.febslet.2008.01.064;
Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H.,
Nishino I., Hayashi Y.K.;
"Affixin activates Rac1 via betaPIX in C2C12 myoblast.";
FEBS Lett. 582:1189-1196(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-155; SER-164;
SER-497; SER-673 AND SER-776, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 164-220.
PubMed=16307729; DOI=10.1016/j.bbrc.2005.10.212;
Li X., Liu X., Sun F., Gao J., Zhou H., Gao G.F., Bartlam M., Rao Z.;
"Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-
activated kinase-interacting exchange factor.";
Biochem. Biophys. Res. Commun. 339:407-414(2006).
-!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF)
and can induce membrane ruffling. May function as a positive
regulator of apoptosis. Functions in cell migration, attachment
and cell spreading. Promotes targeting of RAC1 to focal adhesions.
Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade,
promotes the formation of spines and synapses in hippocampal
neurons (By similarity). {ECO:0000250,
ECO:0000269|PubMed:17093062}.
-!- SUBUNIT: Interacts with PAK kinases through the SH3 domain.
Interacts with unphosphorylated PAK1. Interacts with ITCH.
Interacts with SCRIB; interaction is direct and may play a role in
regulation of apoptosis (By similarity). Interacts with GIT1 and
TGFB1I1. Interacts with FRMPD4 (via N-terminus). Interacts with
CaMK1. Interacts with BIN2 (By similarity). Interacts with
PTK2/FAK1 and RAC1. Interacts with PARVB. {ECO:0000250,
ECO:0000269|PubMed:10428811, ECO:0000269|PubMed:12153727,
ECO:0000269|PubMed:17093062, ECO:0000269|PubMed:18325335}.
-!- INTERACTION:
Q68FF6:Git1; NbExp=2; IntAct=EBI-642580, EBI-645933;
Q9Z272:Git1 (xeno); NbExp=2; IntAct=EBI-642580, EBI-3842379;
Q14161:GIT2 (xeno); NbExp=2; IntAct=EBI-642580, EBI-1046878;
Q9JLQ2:Git2; NbExp=6; IntAct=EBI-642580, EBI-642860;
Q9HBI1:PARVB (xeno); NbExp=10; IntAct=EBI-642580, EBI-1047679;
Q9ES46:Parvb; NbExp=2; IntAct=EBI-642580, EBI-6914996;
Q9WV48:Shank1 (xeno); NbExp=6; IntAct=EBI-8620514, EBI-80909;
Q9QX74:Shank2 (xeno); NbExp=4; IntAct=EBI-8620514, EBI-397902;
Q9JLU4:Shank3 (xeno); NbExp=2; IntAct=EBI-8620514, EBI-6271152;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
projection, ruffle. Cytoplasm, cell cortex. Cell projection,
lamellipodium. Note=Detected at cell adhesions. A small proportion
is detected at focal adhesions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Name=B;
IsoId=Q9ES28-1; Sequence=Displayed;
Name=A;
IsoId=Q9ES28-2; Sequence=VSP_001817;
Name=C;
IsoId=Q9ES28-3; Sequence=VSP_001816;
Name=D;
IsoId=Q9ES28-4; Sequence=VSP_023052, VSP_023053, VSP_001817;
Name=E; Synonyms=d;
IsoId=Q9ES28-5; Sequence=VSP_023055, VSP_023057;
Name=F;
IsoId=Q9ES28-6; Sequence=VSP_023052, VSP_023053, VSP_023054,
VSP_023056;
Name=G; Synonyms=b(L);
IsoId=Q9ES28-7; Sequence=VSP_023052, VSP_023053;
Name=H; Synonyms=b;
IsoId=Q9ES28-8; Sequence=VSP_023051;
Note=Produced by alternative initiation at Met-158 of isoform
G.;
-!- TISSUE SPECIFICITY: Seems to be expressed in the central nervous
system. Isoform B, isoform C and isoform E are expressed with
highest levels in brain and testis. {ECO:0000269|PubMed:10860822,
ECO:0000269|PubMed:11266127}.
-!- PTM: Phosphorylated on Ser-673 by CaMK1; enhancement of GEF
activity and downstream activation of RAC1 (By similarity).
Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1.
{ECO:0000250, ECO:0000269|PubMed:17093062}.
-!- SEQUENCE CAUTION:
Sequence=AAB57691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG18017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAG18018.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH44838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAK97363.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC35033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAC97874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE23905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK129064; BAC97874.1; ALT_INIT; mRNA.
EMBL; AY220301; AAO65479.1; -; mRNA.
EMBL; AK052545; BAC35033.1; ALT_INIT; mRNA.
EMBL; AK139156; BAE23905.1; ALT_INIT; mRNA.
EMBL; BC044838; AAH44838.1; ALT_INIT; mRNA.
EMBL; AF247654; AAG18017.1; ALT_INIT; mRNA.
EMBL; AF247655; AAG18018.1; ALT_INIT; mRNA.
EMBL; AF343877; AAK97363.1; ALT_INIT; mRNA.
EMBL; U96634; AAB57691.1; ALT_INIT; mRNA.
CCDS; CCDS52480.1; -. [Q9ES28-5]
CCDS; CCDS52481.1; -. [Q9ES28-8]
RefSeq; NP_001106989.1; NM_001113517.1. [Q9ES28-5]
RefSeq; NP_001106990.1; NM_001113518.1. [Q9ES28-8]
RefSeq; NP_059098.2; NM_017402.4.
RefSeq; XP_006508904.2; XM_006508841.2. [Q9ES28-1]
RefSeq; XP_006508906.2; XM_006508843.3. [Q9ES28-2]
RefSeq; XP_006508907.2; XM_006508844.2. [Q9ES28-3]
UniGene; Mm.244068; -.
PDB; 2ESW; X-ray; 2.01 A; A/B=164-220.
PDBsum; 2ESW; -.
ProteinModelPortal; Q9ES28; -.
SMR; Q9ES28; -.
BioGrid; 207566; 17.
CORUM; Q9ES28; -.
IntAct; Q9ES28; 22.
MINT; Q9ES28; -.
STRING; 10090.ENSMUSP00000106534; -.
iPTMnet; Q9ES28; -.
PhosphoSitePlus; Q9ES28; -.
PaxDb; Q9ES28; -.
PeptideAtlas; Q9ES28; -.
PRIDE; Q9ES28; -.
Ensembl; ENSMUST00000098938; ENSMUSP00000096538; ENSMUSG00000031511. [Q9ES28-8]
Ensembl; ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511. [Q9ES28-5]
GeneID; 54126; -.
KEGG; mmu:54126; -.
UCSC; uc009kvu.2; mouse. [Q9ES28-2]
UCSC; uc009kvv.2; mouse. [Q9ES28-5]
UCSC; uc009kvw.2; mouse. [Q9ES28-4]
UCSC; uc009kvx.2; mouse. [Q9ES28-1]
CTD; 8874; -.
MGI; MGI:1860493; Arhgef7.
eggNOG; KOG2070; Eukaryota.
eggNOG; ENOG410XNNP; LUCA.
GeneTree; ENSGT00920000148946; -.
HOVERGEN; HBG050569; -.
InParanoid; Q9ES28; -.
KO; K13710; -.
OMA; SAINKSY; -.
OrthoDB; EOG091G04XA; -.
PhylomeDB; Q9ES28; -.
TreeFam; TF316105; -.
Reactome; R-MMU-182971; EGFR downregulation.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
ChiTaRS; Arhgef7; mouse.
EvolutionaryTrace; Q9ES28; -.
PRO; PR:Q9ES28; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031511; -.
CleanEx; MM_ARHGEF7; -.
ExpressionAtlas; Q9ES28; baseline and differential.
Genevisible; Q9ES28; MM.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0000322; C:storage vacuole; IDA:MGI.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0043615; P:astrocyte cell migration; ISO:MGI.
GO; GO:0007030; P:Golgi organization; ISO:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; IMP:MGI.
GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
GO; GO:1904424; P:regulation of GTP binding; ISO:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:MGI.
CDD; cd00014; CH; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd12061; SH3_betaPIX; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035789; BetaPIX_SH3.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR032409; GEF_CC.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF16523; betaPIX_CC; 1.
Pfam; PF00307; CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00033; CH; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Cell junction; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Guanine-nucleotide releasing factor; Neurogenesis;
Phosphoprotein; Reference proteome; SH3 domain.
CHAIN 1 862 Rho guanine nucleotide exchange factor 7.
/FTId=PRO_0000080922.
DOMAIN 1 112 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 163 222 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 250 430 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 452 557 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
COILED 804 854 {ECO:0000255}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:Q14155}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q14155}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 673 673 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 157 Missing (in isoform H).
{ECO:0000303|PubMed:10860822,
ECO:0000303|PubMed:15120616}.
/FTId=VSP_023051.
VAR_SEQ 1 52 Missing (in isoform D, isoform F and
isoform G). {ECO:0000303|PubMed:15120616,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023052.
VAR_SEQ 53 55 IEK -> MLQ (in isoform D, isoform F and
isoform G). {ECO:0000303|PubMed:15120616,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023053.
VAR_SEQ 576 650 Missing (in isoform C).
{ECO:0000303|PubMed:10860822}.
/FTId=VSP_001816.
VAR_SEQ 712 820 TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSED
SEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEET
KSNGQTVIEEKSLVDTVYALKDEVQEL -> SECRSSPRVG
TDYKQLLHGLAALEREVSGA (in isoform F).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_023054.
VAR_SEQ 712 771 TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSED
SEYDSIWTAHSYRMGSASR -> S (in isoform A
and isoform D).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9207241}.
/FTId=VSP_001817.
VAR_SEQ 772 824 SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYA
LKDEVQELRQDN -> KSCCSYISHQN (in isoform
E). {ECO:0000303|PubMed:11266127,
ECO:0000303|PubMed:14621295,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023055.
VAR_SEQ 821 862 Missing (in isoform F).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_023056.
VAR_SEQ 825 862 Missing (in isoform E).
{ECO:0000303|PubMed:11266127,
ECO:0000303|PubMed:14621295,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_023057.
CONFLICT 485 488 NLLL -> KPSV (in Ref. 2; AAO65479, 5;
AAG18017/AAG18018 and 7; AAB57691).
{ECO:0000305}.
CONFLICT 492 492 A -> P (in Ref. 2; AAO65479, 5; AAG18017/
AAG18018 and 7; AAB57691). {ECO:0000305}.
CONFLICT 616 616 S -> R (in Ref. 2; AAO65479, 5; AAG18017
and 7; AAB57691). {ECO:0000305}.
CONFLICT 624 625 KT -> PH (in Ref. 7; AAB57691).
{ECO:0000305}.
CONFLICT 628 628 P -> A (in Ref. 2; AAO65479 and 7;
AAB57691). {ECO:0000305}.
CONFLICT 630 630 S -> G (in Ref. 7; AAB57691).
{ECO:0000305}.
CONFLICT 633 633 C -> W (in Ref. 2; AAO65479, 5; AAG18017
and 7; AAB57691). {ECO:0000305}.
CONFLICT 635 636 RP -> WT (in Ref. 7; AAB57691).
{ECO:0000305}.
STRAND 167 172 {ECO:0000244|PDB:2ESW}.
STRAND 189 195 {ECO:0000244|PDB:2ESW}.
STRAND 199 205 {ECO:0000244|PDB:2ESW}.
STRAND 208 213 {ECO:0000244|PDB:2ESW}.
HELIX 214 216 {ECO:0000244|PDB:2ESW}.
STRAND 217 219 {ECO:0000244|PDB:2ESW}.
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


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