ARHG7_RAT
ID ARHG7_RAT Reviewed; 646 AA.
AC O55043;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Rho guanine nucleotide exchange factor 7;
DE AltName: Full=Beta-Pix;
DE AltName: Full=PAK-interacting exchange factor beta;
GN Name=Arhgef7; Synonyms=Pak3bp, Pixb;
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].
RX PubMed=9659915; DOI=10.1016/s1097-2765(00)80019-2;
RA Manser E., Loo T.-H., Koh C.-G., Zhao Z.-S., Chen X.-Q., Tan L., Tan I.,
RA Leung T., Lim L.;
RT "PAK kinases are directly coupled to the PIX family of nucleotide exchange
RT factors.";
RL Mol. Cell 1:183-192(1998).
RN [2]
RP INTERACTION WITH GIT1.
RX PubMed=10896954; DOI=10.1074/jbc.275.29.22373;
RA Premont R.T., Claing A., Vitale N., Perry S.J., Lefkowitz R.J.;
RT "The GIT family of ADP-ribosylation factor GTPase-activating proteins.
RT Functional diversity of GIT2 through alternative splicing.";
RL J. Biol. Chem. 275:22373-22380(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-71; SER-79; SER-340;
RP SER-516 AND SER-560, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 5-66.
RX PubMed=16228008; DOI=10.1038/nsmb1000;
RA Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D., Groemping Y.,
RA Dikic I., Rittinger K., Bravo J.;
RT "Cbl promotes clustering of endocytic adaptor proteins.";
RL Nat. Struct. Mol. Biol. 12:972-979(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (0.92 ANGSTROMS) OF 10-63 IN COMPLEX WITH PAK2, AND
RP SUBUNIT.
RX PubMed=16527308; DOI=10.1016/j.jmb.2006.02.027;
RA Hoelz A., Janz J.M., Lawrie S.D., Corwin B., Lee A., Sakmar T.P.;
RT "Crystal structure of the SH3 domain of betaPIX in complex with a high
RT affinity peptide from PAK2.";
RL J. Mol. Biol. 358:509-522(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 10-63 IN COMPLEX WITH ITCH.
RX PubMed=17652093; DOI=10.1074/jbc.m702678200;
RA Janz J.M., Sakmar T.P., Min K.C.;
RT "A novel interaction between atrophin-interacting protein 4 and beta-p21-
RT activated kinase-interactive exchange factor is mediated by an SH3
RT domain.";
RL J. Biol. Chem. 282:28893-28903(2007).
CC -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and
CC can induce membrane ruffling. Functions in cell migration, attachment
CC and cell spreading. Promotes targeting of RAC1 to focal adhesions. May
CC function as a positive regulator of apoptosis. Downstream of NMDA
CC receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of
CC spines and synapses in hippocampal neurons (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SCRIB; interaction is direct and may play a
CC role in regulation of apoptosis (By similarity). Interacts with PAK
CC kinases through the SH3 domain. Interacts with GIT1 and probably
CC TGFB1I1. Interacts with ITCH and PARVB. Interacts with FRMPD4 (via N-
CC terminus). Interacts with CaMK1. Interacts with PTK2/FAK1 and RAC1.
CC Interacts with BIN2 (By similarity). Interacts with YWHAZ (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9ES28}.
CC -!- INTERACTION:
CC O55043; Q13191-1: CBLB; Xeno; NbExp=2; IntAct=EBI-3649585, EBI-15555129;
CC O55043; P41227: NAA10; Xeno; NbExp=3; IntAct=EBI-3649585, EBI-747693;
CC O55043; Q13177: PAK2; Xeno; NbExp=8; IntAct=EBI-3649585, EBI-1045887;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell
CC projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Note=Detected at cell
CC adhesions. A small proportion is detected at focal adhesions.
CC -!- PTM: Phosphorylated on Ser-516 by CaMK1; enhancement of GEF activity
CC and downstream activation of RAC1. Phosphorylated by PTK2/FAK1; this
CC promotes interaction with RAC1 (By similarity). {ECO:0000250}.
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DR EMBL; AF044673; AAC39971.1; -; mRNA.
DR RefSeq; NP_001106994.1; NM_001113522.1.
DR PDB; 2AK5; X-ray; 1.85 A; A/B=5-66.
DR PDB; 2DF6; X-ray; 1.30 A; A/B=10-63.
DR PDB; 2G6F; X-ray; 0.92 A; X=10-63.
DR PDB; 2P4R; X-ray; 2.00 A; A=10-63.
DR PDB; 2W6B; X-ray; 2.80 A; A=588-638.
DR PDB; 3L4F; X-ray; 2.80 A; A/B/C=587-646.
DR PDB; 3QJN; X-ray; 2.71 A; I/J/K/L/M/N/O/P=640-646.
DR PDBsum; 2AK5; -.
DR PDBsum; 2DF6; -.
DR PDBsum; 2G6F; -.
DR PDBsum; 2P4R; -.
DR PDBsum; 2W6B; -.
DR PDBsum; 3L4F; -.
DR PDBsum; 3QJN; -.
DR AlphaFoldDB; O55043; -.
DR SMR; O55043; -.
DR BioGRID; 250377; 2.
DR DIP; DIP-41481N; -.
DR ELM; O55043; -.
DR IntAct; O55043; 9.
DR MINT; O55043; -.
DR STRING; 10116.ENSRNOP00000043761; -.
DR iPTMnet; O55043; -.
DR PhosphoSitePlus; O55043; -.
DR jPOST; O55043; -.
DR PaxDb; O55043; -.
DR PeptideAtlas; O55043; -.
DR PRIDE; O55043; -.
DR GeneID; 114559; -.
DR KEGG; rno:114559; -.
DR UCSC; RGD:620624; rat.
DR CTD; 8874; -.
DR RGD; 620624; Arhgef7.
DR VEuPathDB; HostDB:ENSRNOG00000012934; -.
DR eggNOG; KOG2070; Eukaryota.
DR HOGENOM; CLU_017010_1_1_1; -.
DR InParanoid; O55043; -.
DR OrthoDB; 547556at2759; -.
DR PhylomeDB; O55043; -.
DR Reactome; R-RNO-182971; EGFR downregulation.
DR Reactome; R-RNO-193648; NRAGE signals death through JNK.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013420; RHOU GTPase cycle.
DR Reactome; R-RNO-9013424; RHOV GTPase cycle.
DR EvolutionaryTrace; O55043; -.
DR PRO; PR:O55043; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000012934; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; O55043; baseline and differential.
DR Genevisible; O55043; RN.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0000322; C:storage vacuole; ISO:RGD.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0043615; P:astrocyte cell migration; IMP:RGD.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:1905833; P:negative regulation of microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:0099140; P:presynaptic actin cytoskeleton organization; IDA:SynGO.
DR GO; GO:1904424; P:regulation of GTP binding; ISO:RGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:RGD.
DR CDD; cd01225; PH_Cool_Pix; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd12061; SH3_betaPIX; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035789; BetaPIX_SH3.
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; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 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 3D-structure; Cell junction; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Neurogenesis; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..646
FT /note="Rho guanine nucleotide exchange factor 7"
FT /id="PRO_0000080923"
FT DOMAIN 6..65
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 93..273
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 295..400
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 402..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:2G6F"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2G6F"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:2G6F"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:2G6F"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2G6F"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2G6F"
FT HELIX 588..636
FT /evidence="ECO:0007829|PDB:2W6B"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:3L4F"
SQ SEQUENCE 646 AA; 73140 MW; 17CDE7DD96ADEA53 CRC64;
MTDNANSQLV VRAKFNFQQT NEDELSFSKG DVIHVTRVEE GGWWEGTHNG RTGWFPSNYV
REIKPSEKPV SPKSGTLKSP PKGFDTTAIN KSYYNVVLQN ILETEHEYSK ELQSVLSTYL
WPLQTSEKLS SANTSYLMGN LEEISSFQQV LVQSLEECTK SPEAQQRVGG CFLSLMPQMR
TLYLAYCANH PSAVSVLTEH SEDLGEFMET KGASSPGILV LTTGLSKPFM RLDKYPTLLK
ELERHMEDYH PDRQDIQKSM TAFKNLSAQC QEVRKRKELE LQILTEPIRS WEGDDIKTLG
SVTYMSQVTI QCAGSEEKNE RYLLLFPNLL LMLSASPRMS GFIYQGKLPT TGMTITKLED
SENHRNAFEI SGSMIERILV SCNNQQDLHE WVEHLQRQTK VTSVSNPTIK PHSVPSHTLP
SHPLTPSSKH ADSKPVALTP AYHTLPHPSH HGTPHTTISW GPLEPPKTPK PWSLSCLRPA
PPLRPSAALC YKEDLSRSPK TMKKLLPKRK PERKPSDEEF AVRKSTAALE EDAQILKVIE
AYCTSAKTRQ TLNSSSRKES APQVLLPEEE KIIVEETKSN GQTVIEEKSL VDTVYALKDE
VQELRQDNKK MKKSLEEEQR ARKDLEKLVR KVLKNMNDPA WDETNL
