ID ARHG3_MOUSE Reviewed; 524 AA. AC Q91X46; Q8CDM0; Q91VY4; Q99K14; Q9DC31; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-SEP-2015, entry version 106. DE RecName: Full=Rho guanine nucleotide exchange factor 3; GN Name=Arhgef3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Salivary gland; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11839749; DOI=10.1074/jbc.M111108200; RA Schmidt A., Hall A.; RT "The Rho exchange factor Net1 is regulated by nuclear sequestration."; RL J. Biol. Chem. 277:14581-14588(2002). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 110-448. RX PubMed=23192023; DOI=10.1107/S1744309112045265; RA Murayama K., Kato-Murayama M., Akasaka R., Terada T., Yokoyama S., RA Shirouzu M.; RT "Structure of the Rho-specific guanine nucleotide-exchange factor RT Xpln."; RL Acta Crystallogr. F 68:1455-1459(2012). CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CC RhoA and RhoB GTPases. {ECO:0000269|PubMed:11839749}. CC -!- SUBUNIT: Interacts with RHOA and RHOB. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11839749}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q91X46-1; Sequence=Displayed; CC Name=2; CC IsoId=Q91X46-2; Sequence=VSP_011613; CC Name=3; CC IsoId=Q91X46-3; Sequence=VSP_011614; CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00062}. CC -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE- CC ProRule:PRU00145}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH07153.1; 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; AK004600; BAB23401.1; -; mRNA. DR EMBL; AK029872; BAC26652.1; -; mRNA. DR EMBL; BC005517; AAH05517.1; -; mRNA. DR EMBL; BC007153; AAH07153.1; ALT_INIT; mRNA. DR EMBL; BC012262; AAH12262.1; -; mRNA. DR CCDS; CCDS26886.1; -. [Q91X46-2] DR RefSeq; NP_001276615.1; NM_001289686.1. DR RefSeq; NP_001276616.1; NM_001289687.1. [Q91X46-1] DR RefSeq; NP_001276617.1; NM_001289688.1. DR RefSeq; NP_082147.1; NM_027871.2. [Q91X46-2] DR UniGene; Mm.248606; -. DR PDB; 2Z0Q; X-ray; 1.79 A; A=110-448. DR PDBsum; 2Z0Q; -. DR ProteinModelPortal; Q91X46; -. DR SMR; Q91X46; 113-448. DR STRING; 10090.ENSMUSP00000046486; -. DR PhosphoSite; Q91X46; -. DR MaxQB; Q91X46; -. DR PaxDb; Q91X46; -. DR PRIDE; Q91X46; -. DR Ensembl; ENSMUST00000049206; ENSMUSP00000046486; ENSMUSG00000021895. [Q91X46-2] DR GeneID; 71704; -. DR KEGG; mmu:71704; -. DR UCSC; uc007sto.2; mouse. [Q91X46-2] DR UCSC; uc007str.2; mouse. [Q91X46-1] DR CTD; 50650; -. DR MGI; MGI:1918954; Arhgef3. DR eggNOG; COG5422; -. DR GeneTree; ENSGT00760000119193; -. DR HOGENOM; HOG000034044; -. DR HOVERGEN; HBG050567; -. DR InParanoid; Q91X46; -. DR OMA; TKLEQMD; -. DR OrthoDB; EOG7J446D; -. DR PhylomeDB; Q91X46; -. DR TreeFam; TF328974; -. DR Reactome; R-MMU-193648; NRAGE signals death through JNK. DR Reactome; R-MMU-194840; Rho GTPase cycle. DR Reactome; R-MMU-416482; G alpha (12/13) signalling events. DR EvolutionaryTrace; Q91X46; -. DR NextBio; 334275; -. DR PRO; PR:Q91X46; -. DR Proteomes; UP000000589; Chromosome 14. DR Bgee; Q91X46; -. DR CleanEx; MM_ARHGEF3; -. DR Genevisible; Q91X46; MM. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; ISO:MGI. DR GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. DR Gene3D; 1.20.900.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR001331; GDS_CDC24_CS. DR InterPro; IPR011993; PH/PTB_dom. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR015721; RhoGEF-like. DR PANTHER; PTHR22825; PTHR22825; 1. DR Pfam; PF00621; RhoGEF; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00325; RhoGEF; 1. DR SUPFAM; SSF48065; SSF48065; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Guanine-nucleotide releasing factor; Reference proteome. FT CHAIN 1 524 Rho guanine nucleotide exchange factor 3. FT /FTId=PRO_0000080913. FT DOMAIN 121 303 DH. {ECO:0000255|PROSITE- FT ProRule:PRU00062}. FT DOMAIN 290 448 PH. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT VAR_SEQ 1 31 MVAKDYPFYLTVKRANCSLEAPLGSGVAKDE -> MRSERP FT MVWCCFFLRAQRKRKQSSQDEDAVSLCSLDIS (in FT isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_011613. FT VAR_SEQ 1 31 MVAKDYPFYLTVKRANCSLEAPLGSGVAKDE -> MFPSPK FT ACNFRGRKRKQSSQDEDAVSLCSLDIS (in isoform FT 3). {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_011614. FT CONFLICT 363 363 V -> I (in Ref. 2; AAH05517). FT {ECO:0000305}. FT HELIX 117 146 {ECO:0000244|PDB:2Z0Q}. FT HELIX 148 153 {ECO:0000244|PDB:2Z0Q}. FT HELIX 159 166 {ECO:0000244|PDB:2Z0Q}. FT HELIX 169 186 {ECO:0000244|PDB:2Z0Q}. FT HELIX 197 203 {ECO:0000244|PDB:2Z0Q}. FT HELIX 204 208 {ECO:0000244|PDB:2Z0Q}. FT HELIX 209 227 {ECO:0000244|PDB:2Z0Q}. FT HELIX 231 234 {ECO:0000244|PDB:2Z0Q}. FT TURN 251 253 {ECO:0000244|PDB:2Z0Q}. FT HELIX 254 256 {ECO:0000244|PDB:2Z0Q}. FT HELIX 257 274 {ECO:0000244|PDB:2Z0Q}. FT HELIX 282 315 {ECO:0000244|PDB:2Z0Q}. FT HELIX 326 329 {ECO:0000244|PDB:2Z0Q}. FT STRAND 334 342 {ECO:0000244|PDB:2Z0Q}. FT STRAND 347 365 {ECO:0000244|PDB:2Z0Q}. FT STRAND 368 375 {ECO:0000244|PDB:2Z0Q}. FT HELIX 380 382 {ECO:0000244|PDB:2Z0Q}. FT STRAND 384 387 {ECO:0000244|PDB:2Z0Q}. FT TURN 390 392 {ECO:0000244|PDB:2Z0Q}. FT HELIX 405 408 {ECO:0000244|PDB:2Z0Q}. FT STRAND 410 417 {ECO:0000244|PDB:2Z0Q}. FT HELIX 420 422 {ECO:0000244|PDB:2Z0Q}. FT STRAND 424 429 {ECO:0000244|PDB:2Z0Q}. FT HELIX 433 447 {ECO:0000244|PDB:2Z0Q}. SQ SEQUENCE 524 AA; 59526 MW; 579FF96C1F0B0ADA CRC64; MVAKDYPFYL TVKRANCSLE APLGSGVAKD EEPSNKRVKP LSRVTSLANL IPPVKTTPLK RFSQTLQRSI SFRSESRPDI LAPRAWSRNA TSSSTKRRDS KLWSETFDVC VNQVLTAKEI KRQEAIFELS QGEEDLIEDL KLAKKAYHDP MLKLSIMTEQ ELNQIFGTLD SLIPLHEELL SQLRDVRKPD GSTEHVGPIL VGWLPCLSSY DSYCSNQVAA KALLDHKKQD HRVQDFLQRC LESPFSRKLD LWNFLDIPRS RLVKYPLLLR EILRHTPNDN PDQQHLEEAI NIIQGIVAEI NTKTGESECR YYKERLLYLE EGQKDSLIDS SRVLCCHGEL KNNRGVKLHV FLFQEVLVIT RAVTHNEQLC YQLYRQPIPV KDLTLEDLQD GEVRLGGSLR GAFSNNERVK NFFRVSFKNG SQSQTHSLQA NDTFNKQQWL NCIRQAKETV LSAAGQAGLL DSEGLVQGPG TENREPQGET KLEQMDQSDS ESDCSMDTSE VSLECERMEQ TDASCANSRP EESV //