ARHGB_RAT
ID ARHGB_RAT Reviewed; 1527 AA.
AC Q9ES67;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Rho guanine nucleotide exchange factor 11;
DE AltName: Full=RhoGEF glutamate transport modulator GTRAP48;
GN Name=Arhgef11;
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], FUNCTION, AND INTERACTION WITH RHOA; GNA13 AND
RP SLC1A6.
RX PubMed=11242047; DOI=10.1038/35065091;
RA Jackson M., Song W., Liu M.-Y., Jin L., Dykes-Hoberg M., Lin C.-L.G.,
RA Bowers W.J., Federoff H.J., Sternweis P.C., Rothstein J.D.;
RT "Modulation of the neuronal glutamate transporter EAAT4 by two interacting
RT proteins.";
RL Nature 410:89-93(2001).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-51; SER-268; SER-272;
RP SER-288; THR-676; THR-680; SER-1462; SER-1463 AND SER-1485, 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: May play a role in the regulation of RhoA GTPase by guanine
CC nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as
CC guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as
CC GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in
CC neurotrophin-induced neurite outgrowth (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11242047}.
CC -!- SUBUNIT: Interacts with RHOA, GNA13 and SLC1A6. Interacts with GNA12,
CC PLXNB1 and PLXNB2 (By similarity). Interacts (via DH domain) with GCSAM
CC (via C-terminus) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9ES67; P27601: Gna13; Xeno; NbExp=3; IntAct=EBI-15735216, EBI-2255627;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Translocated to the membrane upon stimulation. {ECO:0000250}.
CC -!- PTM: Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or
CC MAPK14). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex when
CC previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13
CC and/or MAPK14), leading to its degradation, thereby restricting RhoA
CC activity and facilitating growth cone spreading and neurite outgrowth.
CC {ECO:0000250}.
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; AF225961; AAG28597.1; -; mRNA.
DR RefSeq; NP_076472.1; NM_023982.1.
DR PDB; 3CX6; X-ray; 2.50 A; B=307-508.
DR PDB; 3CX7; X-ray; 2.25 A; B=307-508.
DR PDB; 3CX8; X-ray; 2.00 A; B=307-508.
DR PDBsum; 3CX6; -.
DR PDBsum; 3CX7; -.
DR PDBsum; 3CX8; -.
DR AlphaFoldDB; Q9ES67; -.
DR SMR; Q9ES67; -.
DR DIP; DIP-46242N; -.
DR IntAct; Q9ES67; 1.
DR STRING; 10116.ENSRNOP00000020717; -.
DR iPTMnet; Q9ES67; -.
DR PhosphoSitePlus; Q9ES67; -.
DR SwissPalm; Q9ES67; -.
DR jPOST; Q9ES67; -.
DR PaxDb; Q9ES67; -.
DR PeptideAtlas; Q9ES67; -.
DR PRIDE; Q9ES67; -.
DR GeneID; 78966; -.
DR KEGG; rno:78966; -.
DR UCSC; RGD:619705; rat.
DR CTD; 9826; -.
DR RGD; 619705; Arhgef11.
DR eggNOG; KOG3520; Eukaryota.
DR InParanoid; Q9ES67; -.
DR OrthoDB; 319635at2759; -.
DR PhylomeDB; Q9ES67; -.
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-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR EvolutionaryTrace; Q9ES67; -.
DR PRO; PR:Q9ES67; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; TAS:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR CDD; cd13391; PH_PRG; 1.
DR CDD; cd08753; RGS_PDZRhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR032919; PDZ-RhoGEF.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR037889; PDZRhoGEF_RGS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037803; PRG_PH.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF1; PTHR45872:SF1; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1527
FT /note="Rho guanine nucleotide exchange factor 11"
FT /id="PRO_0000080929"
FT DOMAIN 64..143
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 323..503
FT /note="RGSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 742..931
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 973..1087
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1480..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 461..487
FT /evidence="ECO:0000255"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1243..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 271
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 676
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 680
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 1462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1467
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 1480
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15085"
FT MOD_RES 1485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 338..351
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:3CX8"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 415..441
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 460..473
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:3CX8"
FT HELIX 483..500
FT /evidence="ECO:0007829|PDB:3CX8"
SQ SEQUENCE 1527 AA; 168534 MW; ABAEA20F541A3A9A CRC64;
MSIRLPHSID RSASKKQSHL SSPIASWLSS LSSLGDSTPE RTSPSHHRQP SDTSETTAGL
VQRCVIIQKD QHGFGFTVSG DRIVLVQSVR PGGAAMKAGV KEGDRIIKVN GTMVTNSSHL
EVVKLIKSGA YAALTLLGSS PPSVGVSGLQ QNPSVAGVLR VNPIIPPPPP PPPLPPPQHI
TGPKPLQDPE VQKHATQILW NMLRQEEEEL QDILPPCGET SQRTCEGRLS VDSQEADSGL
DSGTERFPSI SESLMNRNSV LSDPGLDSPQ TSPVILARVA QHHRRQGSDA ALLPLNHQGI
DQSPKPLIIG PEEDYDPGYF NNESDIIFQD LEKLKSHPAY LVVFLRYILS QADPGPLLFY
LCSEVYQQTN PKDSRSLGKD IWNIFLEKNA PLRVKIPEML QAEIDLRLRN NEDPRNVLCE
AQEAVMLEIQ EQINDYRSKR TLGLGSLYGE NDLLGLDGDP LRERQMAEKQ LAALGDILSK
YEEDRSAPMD FAVNTFMSHA GIRLRESRSS CTAEKTQSAP DKDKWLPFFP KTKKQSSNSK
KEKDALEDKK RNPILRYIGK PKSSSQSIKP GNVRNIIQHF ENSHQYDVPE PGTQRLSTGS
FPEDLLESDS SRSEIRLGRS GSLKGREEMK RSRKAENVPR PRSDVDMDAA AEAARLHQSA
SSSASSLSTR SLENPTPPFT PKMGRRSIES PNLGFCTDVI LPHLLEDDLG QLSDLEPEPE
VQNWQHTVGK DVVANLTQRE IDRQEVINEL FVTEASHLRT LRVLDLIFYQ RMRKENLMPR
EELARLFPNL PELIEIHNSW CEAMKKLREE GPIIRDISDP MLARFDGPAR EELQQVAAQF
CSYQSVALEL IRTKQRKESR FQLFMQEAES HPQCRRLQLR DLIVSEMQRL TKYPLLLENI
IKHTEGGTSE HEKLCRARDQ CREILKFVNE AVKQTENRHR LEGYQKRLDA TALERASNPL
AAEFKSLDLT TRKMIHEGPL TWRISKDKTL DLQVLLLEDL VVLLQRQEER LLLKCHSKTA
VGSSDSKQTF SPVLKLNAVL IRSVATDKRA FFIICTSELG PPQIYELVAL TSSDKNIWME
LLEEAVQNAT KHPGAAPIPI HPSPPGSQEP AYQGSTSSRV EINDSEVYHT EKEPKKLPEG
PGPEQRVQDK QLIAQGEPVQ EEDEEELRTL PRAPPSLDGE NRGIRTRDPV LLALTGPLLM
EGLADAALED VENLRHLILW SLLPGHTVKT QAAGEPEDDL TPTPSVVSIT SHPWDPGSPG
QAPTISDSTR LARPEGSQPE GEDVAVSSLA HLPPRTRSSG VWDSPELDRN PAAEAASTEP
AASYKVVRKV SLLPGGGVGA AKVAGSNAIP DSGQSESELS EVEGGAQATG NCFYVSMPAG
PLDSSTEPTG TPPSPSQCHS LPAWPTEPQP YRGVRGGQCS SLVRRDVDVI FHTIEQLTIK
LHRLKDMELA HRELLKSLGG ESSGGTTPVG SFHTEAARWT DYSLSPPAKE ALASDSQNGQ
EQGSCPEEGS DIALEDSATD TAVSPGP
