ID   ARHG6_RAT               Reviewed;         772 AA.
AC   Q5XXR3;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Rho guanine nucleotide exchange factor 6;
DE   AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 6;
GN   Name=Arhgef6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Node-Langlois R., Jordain-Parisi L., Muller D., Boda B.;
RT   "Cloning of full length rat rac/cdc42 guanine nucleotide exchange factor 6
RT   (ARHGEF6) cDNA.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-640 AND SER-680, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with PAK kinases through the SH3 domain. Interacts
CC       with GIT1. Interacts with PARVB. Component of cytoplasmic complexes,
CC       which also contain PXN, GIT1 and PAK1. Interacts with BIN2. Identified
CC       in a complex with BIN2 and GIT2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium {ECO:0000250}.
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DR   EMBL; AY725848; AAU43636.1; -; mRNA.
DR   RefSeq; NP_001005565.1; NM_001005565.1.
DR   AlphaFoldDB; Q5XXR3; -.
DR   BMRB; Q5XXR3; -.
DR   SMR; Q5XXR3; -.
DR   STRING; 10116.ENSRNOP00000001158; -.
DR   CarbonylDB; Q5XXR3; -.
DR   iPTMnet; Q5XXR3; -.
DR   PhosphoSitePlus; Q5XXR3; -.
DR   jPOST; Q5XXR3; -.
DR   PaxDb; Q5XXR3; -.
DR   PRIDE; Q5XXR3; -.
DR   GeneID; 363509; -.
DR   KEGG; rno:363509; -.
DR   CTD; 9459; -.
DR   RGD; 1359674; Arhgef6.
DR   eggNOG; KOG2070; Eukaryota.
DR   InParanoid; Q5XXR3; -.
DR   OrthoDB; 547556at2759; -.
DR   PhylomeDB; Q5XXR3; -.
DR   Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR   Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR   Reactome; R-RNO-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
DR   Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR   Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR   Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR   PRO; PR:Q5XXR3; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR   CDD; cd00014; CH; 1.
DR   CDD; cd01225; PH_Cool_Pix; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd12060; SH3_alphaPIX; 1.
DR   Gene3D; 1.10.418.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR035788; AlphaPIX_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   Cell projection; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..772
FT                   /note="Rho guanine nucleotide exchange factor 6"
FT                   /id="PRO_0000080919"
FT   DOMAIN          1..111
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          160..219
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          241..421
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          443..548
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          115..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15052"
FT   MOD_RES         133
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15052"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         488
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K4I3"
FT   MOD_RES         640
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   772 AA;  87013 MW;  50FAEB59F70B09AF CRC64;
     MNPEERVVTW LISLGVLESP KKTICDPEEF LKSSLKNGVV LCKLISRLLP GSVEKYCQEP
     QTEADCIDNI NDFLKGCATL QVEVFEPDDL YSGANFSKVL NTLLAVNKAT EDQLSERPCG
     RSSSLSATTS SQTNPQAAVP STTPEQQSEE KAAEMTENGS HQLIVKARFN FKQTNEDELS
     VCKGDIIYVT RVEEGGWWEG TLNGRTGWFP SNYVREIKPS ERPLSPKAVK GFDTAPLTKN
     YYTVVLQNIL DTEKEYAKEL QSLLVTYLRP LQSNNNLSTV EFTCLLGNFE EVCTFQQTLC
     QALEECSKSP ENQHKVGGCL LNLMPHFKSM YLAYCANHPS AVNVLTQHSD DLERFMENQG
     ASSPGILILT TSLSKPFMRL EKYVTLLQEL ERHMEDTHPD HQDILKAIIA FKSLMGQCQD
     LRKRKQLELQ ILSEPIQAWE GDDIKTLGNV IFMSQVVMQH GACEEKEERY FLLFSSVLIM
     LSASPRMSGF MYQGKVPIAG MVVTRLDEIE GNDCTFEITG STVERIVVHC NNNQDFQEWM
     EQLNRLTKGP ASCSSLSKTS SSSCSTHSSF SSTGQPRGPL EPPQIIKPWS LSCLRPAPPL
     RPSAALGYKE RMSYILKESS KSPKTMKKFL HKRKTERKTS EEEYVIRKST AALEEDAQIL
     KVIEAYCTSA SFQQGTRKDS VPQVLLPEEE KLIIEETRSN GQTIIEEKSL VDTVYALKDE
     VKELKQENKK MKQCLEEELK SRKDLEKLVR KLLKQTDESI RAESSSKTSI LQ