ARHG3_MOUSE
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 03-AUG-2022, entry version 148.
DE RecName: Full=Rho guanine nucleotide exchange factor 3;
GN Name=Arhgef3;
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] (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., 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 [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 project:
RT 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 Xpln.";
RL Acta Crystallogr. F 68:1455-1459(2012).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for RhoA and
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=AAH07153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 CCDS; CCDS88606.1; -. [Q91X46-1]
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 PDB; 2Z0Q; X-ray; 1.79 A; A=110-448.
DR PDBsum; 2Z0Q; -.
DR AlphaFoldDB; Q91X46; -.
DR SMR; Q91X46; -.
DR BioGRID; 214868; 3.
DR IntAct; Q91X46; 1.
DR STRING; 10090.ENSMUSP00000046486; -.
DR iPTMnet; Q91X46; -.
DR PhosphoSitePlus; Q91X46; -.
DR EPD; Q91X46; -.
DR jPOST; Q91X46; -.
DR MaxQB; Q91X46; -.
DR PaxDb; Q91X46; -.
DR PeptideAtlas; Q91X46; -.
DR PRIDE; Q91X46; -.
DR ProteomicsDB; 273923; -. [Q91X46-1]
DR ProteomicsDB; 273924; -. [Q91X46-2]
DR ProteomicsDB; 273925; -. [Q91X46-3]
DR Antibodypedia; 31503; 189 antibodies from 24 providers.
DR DNASU; 71704; -.
DR Ensembl; ENSMUST00000049206; ENSMUSP00000046486; ENSMUSG00000021895. [Q91X46-2]
DR Ensembl; ENSMUST00000224981; ENSMUSP00000153124; ENSMUSG00000021895. [Q91X46-1]
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 VEuPathDB; HostDB:ENSMUSG00000021895; -.
DR eggNOG; KOG4305; Eukaryota.
DR GeneTree; ENSGT00940000158385; -.
DR HOGENOM; CLU_027428_3_0_1; -.
DR InParanoid; Q91X46; -.
DR OMA; QCVFREM; -.
DR OrthoDB; 849206at2759; -.
DR PhylomeDB; Q91X46; -.
DR TreeFam; TF328974; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR BioGRID-ORCS; 71704; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Arhgef3; mouse.
DR EvolutionaryTrace; Q91X46; -.
DR PRO; PR:Q91X46; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q91X46; protein.
DR Bgee; ENSMUSG00000021895; Expressed in granulocyte and 246 other tissues.
DR ExpressionAtlas; Q91X46; baseline and differential.
DR Genevisible; Q91X46; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR CDD; cd10572; PH_RhoGEF3_XPLN; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR044129; PH_RhoGEF3_XPLN.
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; Cytoplasm;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome.
FT CHAIN 1..524
FT /note="Rho guanine nucleotide exchange factor 3"
FT /id="PRO_0000080913"
FT DOMAIN 121..303
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 290..448
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 461..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NR81"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z628"
FT VAR_SEQ 1..31
FT /note="MVAKDYPFYLTVKRANCSLEAPLGSGVAKDE -> MRSERPMVWCCFFLRAQ
FT RKRKQSSQDEDAVSLCSLDIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011613"
FT VAR_SEQ 1..31
FT /note="MVAKDYPFYLTVKRANCSLEAPLGSGVAKDE -> MFPSPKACNFRGRKRKQ
FT SSQDEDAVSLCSLDIS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011614"
FT CONFLICT 363
FT /note="V -> I (in Ref. 2; AAH05517)"
FT /evidence="ECO:0000305"
FT HELIX 117..146
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 169..186
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 204..208
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 209..227
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 257..274
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 282..315
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 347..365
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 410..417
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:2Z0Q"
FT HELIX 433..447
FT /evidence="ECO:0007829|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
