ARHG9_RAT
ID ARHG9_RAT Reviewed; 493 AA.
AC Q9QX73; Q9ER22;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Rho guanine nucleotide exchange factor 9;
DE AltName: Full=Collybistin;
DE AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 9;
GN Name=Arhgef9;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP GPHN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10607391; DOI=10.1038/71096;
RA Kins S., Betz H., Kirsch J.;
RT "Collybistin, a newly identified brain-specific GEF, induces submembrane
RT clustering of gephyrin.";
RL Nat. Neurosci. 3:22-29(2000).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GPHN, AND MUTAGENESIS OF
RP ARG-107; ASP-108; ARG-111 AND GLU-117.
RX PubMed=11727829; DOI=10.1515/bc.2001.179;
RA Grosskreutz Y., Hermann A., Kins S., Fuhrmann J.C., Betz H., Kneussel M.;
RT "Identification of a gephyrin-binding motif in the GDP/GTP exchange factor
RT collybistin.";
RL Biol. Chem. 382:1455-1462(2001).
RN [3]
RP ALTERNATIVE SPLICING, FUNCTION, INTERACTION WITH GPHN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15215304; DOI=10.1523/jneurosci.1184-04.2004;
RA Harvey K., Duguid I.C., Alldred M.J., Beatty S.E., Ward H., Keep N.H.,
RA Lingenfelter S.E., Pearce B.R., Lundgren J., Owen M.J., Smart T.G.,
RA Luescher B., Rees M.I., Harvey R.J.;
RT "The GDP-GTP exchange factor collybistin: an essential determinant of
RT neuronal gephyrin clustering.";
RL J. Neurosci. 24:5816-5826(2004).
RN [4]
RP MUTAGENESIS OF ARG-297.
RX PubMed=25678704; DOI=10.1074/jbc.m114.633024;
RA Papadopoulos T., Schemm R., Grubmueller H., Brose N.;
RT "Lipid binding defects and perturbed synaptogenic activity of a
RT collybistinR290H mutant that causes epilepsy and intellectual disability.";
RL J. Biol. Chem. 290:8256-8270(2015).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 10-411 IN COMPLEX WITH CDC42, AND
RP MUTAGENESIS OF ARG-107; ASP-108; ARG-111 AND GLU-117.
RX PubMed=16616186; DOI=10.1016/j.jmb.2006.03.019;
RA Xiang S., Kim E.Y., Connelly J.J., Nassar N., Kirsch J., Winking J.,
RA Schwarz G., Schindelin H.;
RT "The crystal structure of Cdc42 in complex with collybistin II, a gephyrin-
RT interacting guanine nucleotide exchange factor.";
RL J. Mol. Biol. 359:35-46(2006).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42.
CC Promotes formation of GPHN clusters. {ECO:0000269|PubMed:10607391,
CC ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:15215304}.
CC -!- SUBUNIT: Interacts with GPHN. {ECO:0000269|PubMed:10607391,
CC ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:15215304,
CC ECO:0000269|PubMed:16616186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10607391,
CC ECO:0000269|PubMed:11727829, ECO:0000269|PubMed:15215304}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q3UTH8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Collybistin I;
CC IsoId=Q9QX73-1; Sequence=Displayed;
CC Name=2; Synonyms=Collybistin II;
CC IsoId=Q9QX73-2; Sequence=VSP_021147, VSP_021148;
CC -!- TISSUE SPECIFICITY: Detected in brain, throughout the gray matter.
CC Detected at low levels in heart and skeletal muscle.
CC {ECO:0000269|PubMed:10607391}.
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DR EMBL; AJ250425; CAB65966.1; -; mRNA.
DR EMBL; AJ302676; CAC16410.1; -; mRNA.
DR RefSeq; NP_076447.1; NM_023957.1. [Q9QX73-1]
DR PDB; 2DFK; X-ray; 2.15 A; A/C=71-463.
DR PDB; 4MT6; X-ray; 5.50 A; A=1-456.
DR PDB; 4MT7; X-ray; 3.50 A; A=10-493.
DR PDBsum; 2DFK; -.
DR PDBsum; 4MT6; -.
DR PDBsum; 4MT7; -.
DR AlphaFoldDB; Q9QX73; -.
DR SMR; Q9QX73; -.
DR PhosphoSitePlus; Q9QX73; -.
DR PaxDb; Q9QX73; -.
DR PRIDE; Q9QX73; -.
DR ABCD; Q9QX73; 2 sequenced antibodies.
DR GeneID; 66013; -.
DR KEGG; rno:66013; -.
DR CTD; 23229; -.
DR RGD; 620719; Arhgef9.
DR InParanoid; Q9QX73; -.
DR OrthoDB; 428887at2759; -.
DR PhylomeDB; Q9QX73; -.
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-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR EvolutionaryTrace; Q9QX73; -.
DR PRO; PR:Q9QX73; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0099572; C:postsynaptic specialization; IDA:SynGO.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; IDA:RGD.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; ISO:RGD.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11975; SH3_ARHGEF9; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID50103; -.
DR InterPro; IPR035728; ARHGEF9_SH3.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
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; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm;
KW Guanine-nucleotide releasing factor; Reference proteome; SH3 domain;
KW Synapse.
FT CHAIN 1..493
FT /note="Rho guanine nucleotide exchange factor 9"
FT /id="PRO_0000253898"
FT DOMAIN 15..74
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 110..294
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 325..432
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 107..117
FT /note="Interaction with GPHN"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 12..71
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10607391"
FT /id="VSP_021147"
FT VAR_SEQ 464..493
FT /note="GRVGEEENQSLELKRACEVLQRLWSPGKKS -> VTQRKWHY (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10607391"
FT /id="VSP_021148"
FT MUTAGEN 107
FT /note="R->A: No effect on formation of GPHN clusters; when
FT associated with A-108 and A-117."
FT /evidence="ECO:0000269|PubMed:11727829,
FT ECO:0000269|PubMed:16616186"
FT MUTAGEN 108
FT /note="D->A: No effect on GPHN clusters; when associated
FT with A-107 and A-117."
FT /evidence="ECO:0000269|PubMed:11727829,
FT ECO:0000269|PubMed:16616186"
FT MUTAGEN 111
FT /note="R->A: Loss of formation of GPHN clusters."
FT /evidence="ECO:0000269|PubMed:11727829,
FT ECO:0000269|PubMed:16616186"
FT MUTAGEN 117
FT /note="E->A: No effect on GPHN clusters; when associated
FT with A-107 and A-108."
FT /evidence="ECO:0000269|PubMed:11727829,
FT ECO:0000269|PubMed:16616186"
FT MUTAGEN 297
FT /note="R->H: Defects in binding to phosphatidylinositol-3-
FT phosphate and in formation of GPHN clusters."
FT /evidence="ECO:0000269|PubMed:25678704"
FT HELIX 107..135
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:2DFK"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 159..176
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2DFK"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 200..218
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 248..265
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 274..299
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 301..310
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4MT7"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 326..337
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 394..407
FT /evidence="ECO:0007829|PDB:2DFK"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 417..440
FT /evidence="ECO:0007829|PDB:2DFK"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:2DFK"
SQ SEQUENCE 493 AA; 58157 MW; 41040671B9398BFA CRC64;
MQWIRGGSGM LITGDSIVSA EAVWDHVTMA NRGVAFKAGD VIKVLDASNK DWWWGQIDDE
EGWFPASFVR LWVNQEDGVE EGPSDVQNGH LDPNSDCLCL GRPLQNRDQM RANVINEIMS
TERHYIKHLK DICEGYLKQC RKRRDMFSDE QLKVIFGNIE DIYRFQMGFV RDLEKQYNND
DPHLSEIGPC FLEHQDGFWI YSEYCNNHLD ACMELSKLMK DSRYQHFFEA CRLLQQMIDI
AIDGFLLTPV QKICKYPLQL AELLKYTAQD HSDYRYVAAA LAVMRNVTQQ INERKRRLEN
IDKIAQWQAS VLDWEGDDIL DRSSELIYTG EMAWIYQPYG RNQQRVFFLF DHQMVLCKKD
LIRRDILYYK GRIDMDKYEV IDIEDGRDDD FNVSMKNAFK LHNKETEEVH LFFAKKLEEK
IRWLRAFREE RKMVQEDEKI GFEISENQKR QAAMTVRKAS KQKGRVGEEE NQSLELKRAC
EVLQRLWSPG KKS
