ARHG1_RAT
ID ARHG1_RAT Reviewed; 919 AA.
AC Q9Z1I6;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Rho guanine nucleotide exchange factor 1;
DE AltName: Full=Lbc's second cousin;
GN Name=Arhgef1; Synonyms=Lsc;
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].
RA Steinbrenner H., Wuensche C., Seissler J.;
RT "Cloning of a rat homologue of lsc, a mouse oncogene with structural
RT similarities to the Dbl family of guanine nucleotide exchange factors.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=20098430; DOI=10.1038/nm.2079;
RA Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M.,
RA Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M.,
RA Offermanns S., Pacaud P., Loirand G.;
RT "The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on
RT vascular tone and blood pressure.";
RL Nat. Med. 16:183-190(2010).
CC -!- FUNCTION: Seems to play a role in the regulation of RhoA GTPase by
CC guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13)
CC subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13,
CC and as guanine nucleotide exchange factor (GEF) for RhoA GTPase.
CC Activated G alpha 13/GNA13 stimulates the RhoGEF activity through
CC interaction with the RGS-like domain. This GEF activity is inhibited by
CC binding to activated GNA12 (By similarity). Mediates angiotensin-2-
CC induced RhoA activation. {ECO:0000250, ECO:0000269|PubMed:20098430}.
CC -!- SUBUNIT: Interacts with RHOA, GNA12 and GNA13. Homooligomerizes through
CC the coiled coil region. Interacts with CTNNAL1. May interact with CCPG1
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}.
CC Note=Translocated to the membrane by activated GNA13 or LPA
CC stimulation. {ECO:0000250}.
CC -!- DOMAIN: The RGSL domain, also known as rgRGS domain, is necessary but
CC not sufficient for full GAP activity. {ECO:0000250}.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKCA. Angiotensin-2 induced Tyr-736
CC phosphorylation is mediated by JAK2. {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; AJ236911; CAA15426.1; -; mRNA.
DR AlphaFoldDB; Q9Z1I6; -.
DR SMR; Q9Z1I6; -.
DR IntAct; Q9Z1I6; 4.
DR STRING; 10116.ENSRNOP00000059325; -.
DR iPTMnet; Q9Z1I6; -.
DR PhosphoSitePlus; Q9Z1I6; -.
DR jPOST; Q9Z1I6; -.
DR PaxDb; Q9Z1I6; -.
DR PRIDE; Q9Z1I6; -.
DR UCSC; RGD:620951; rat.
DR RGD; 620951; Arhgef1.
DR eggNOG; KOG3520; Eukaryota.
DR InParanoid; Q9Z1I6; -.
DR PhylomeDB; Q9Z1I6; -.
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-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR PRO; PR:Q9Z1I6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
DR CDD; cd08755; RGS_p115RhoGEF; 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 InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR037887; p115RhoGEF_RGS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; GTPase activation;
KW Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..919
FT /note="Rho guanine nucleotide exchange factor 1"
FT /id="PRO_0000080908"
FT DOMAIN 39..230
FT /note="RGSL"
FT DOMAIN 414..603
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 645..758
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 247..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 864..893
FT /evidence="ECO:0000255"
FT COMPBIAS 247..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 736
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:Q92888"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61210"
SQ SEQUENCE 919 AA; 102597 MW; CF328CD2587717F8 CRC64;
MGEVAGGAAP GPPRSGLVSI IIGAEDEDFE NELEANPEDQ NSQFQSLEQV KRRPAHLMAL
LQHVALQFEP GPLLCCLHAD MLSSLGPKEA KKAFLDFYHS FLEKTAVLRV PVPPSVAFEL
DRTRPDLISE DVQRRFIQEV VQSQQAAVTR QLEDFRSKRL MGMTPWEQEL SLLEPWIGKD
RGNYEARERH VAERLLSHLE EMQHTISTDE EKSAAVVTAI SLYMRHLGVR TKSGDKKSGR
NFFRKKVMGN RRSDEPPKTK KGLSSILDPA RWNRGEPSAP DCRHLKVEVD EKPGPADRKG
SLGISSRDRT VGTPGQDNPG VSLHPLSVDS LDSREPGVDT PQEPGDTPPQ GPTSLEPLAP
PESTEDNGET ESPEPGDDGE PGRSGLEQEP EEPPGWRELV PSDTLLGLPK NQVKRQEVIS
ELLVTEAAHV RMLRVLHDLF YQPMAEGGFF PLEELQNIFP SLDELIEVHS LFLDRLMKRR
QESGYLIEEI GDVLLARFDG AEGSWFQKIS SRFCSRQSFA LEQLKAKQRK EPRFCAFVQE
AESRPRCRRL QLKDMIPTEM QRLTKYPLLL QSIGQNTEEP AERAKVELAA ECCREILHHV
NQAVRDMEDL LRLKDYQRRL DLTHLRQSND PMLSEFKNLD ITKKKLVHEG PLTWRLTKDK
AVEVHVLLLD DLLLLLQRQD EGCCSSHTSR TLTPTPDGKT MLRPVLRLTS AMTREVATDH
KAFYVIFTWD QEAQIYELVA QTSSERKSWC ALITETAGSL KVPAPASRPK PRPSPSSTRE
PLLSSSENGT GGTEAAPADA RTERILNDLL PFCRPGPEGQ LAATALQKVL SLKQILLSTE
EDSGAGPPRD GDGVPGGGAP GPTHTQEVEE NLLSLEVVIK QLEELEEEFC RLRPFLSQLG
EILSPNLAAP ERSAQTGLS
