Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QX73 (ARHG9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho guanine nucleotide exchange factor 9
Alternative name(s):
Collybistin
Rac/Cdc42 guanine nucleotide exchange factor 9
Gene names
Name:Arhgef9
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters. Ref.1 Ref.2 Ref.3

Subunit structure

Interacts with GPHN. Ref.1 Ref.2 Ref.3

Subcellular location

Cytoplasm Ref.1 Ref.2 Ref.3.

Tissue specificity

Detected in brain, throughout the gray matter. Detected at low levels in heart and skeletal muscle. Ref.1

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainSH3 domain
   Molecular functionGuanine-nucleotide releasing factor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processreceptor clustering

Inferred from direct assay Ref.1. Source: RGD

   Cellular_componentcell cortex

Inferred from direct assay Ref.1. Source: RGD

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9QX73-1)

Also known as: Collybistin I;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9QX73-2)

Also known as: Collybistin II;

The sequence of this isoform differs from the canonical sequence as follows:
     12-71: Missing.
     464-493: GRVGEEENQSLELKRACEVLQRLWSPGKKS → VTQRKWHY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 493493Rho guanine nucleotide exchange factor 9
PRO_0000253898

Regions

Domain15 – 7460SH3
Domain110 – 294185DH
Domain325 – 432108PH
Region107 – 11711Interaction with GPHN

Natural variations

Alternative sequence12 – 7160Missing in isoform 2.
VSP_021147
Alternative sequence464 – 49330GRVGE…PGKKS → VTQRKWHY in isoform 2.
VSP_021148

Experimental info

Mutagenesis1071R → A: No effect on formation of GPHN clusters; when associated with A-108 and A-117. Ref.2 Ref.4
Mutagenesis1081D → A: No effect on GPHN clusters; when associated with A-107 and A-117. Ref.2 Ref.4
Mutagenesis1111R → A: Loss of formation of GPHN clusters. Ref.2 Ref.4
Mutagenesis1171E → A: No effect on GPHN clusters; when associated with A-107 and A-108. Ref.2 Ref.4

Secondary structure

.................................................... 493
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Collybistin I) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 41040671B9398BFA

FASTA49358,157
        10         20         30         40         50         60 
MQWIRGGSGM LITGDSIVSA EAVWDHVTMA NRGVAFKAGD VIKVLDASNK DWWWGQIDDE 

        70         80         90        100        110        120 
EGWFPASFVR LWVNQEDGVE EGPSDVQNGH LDPNSDCLCL GRPLQNRDQM RANVINEIMS 

       130        140        150        160        170        180 
TERHYIKHLK DICEGYLKQC RKRRDMFSDE QLKVIFGNIE DIYRFQMGFV RDLEKQYNND 

       190        200        210        220        230        240 
DPHLSEIGPC FLEHQDGFWI YSEYCNNHLD ACMELSKLMK DSRYQHFFEA CRLLQQMIDI 

       250        260        270        280        290        300 
AIDGFLLTPV QKICKYPLQL AELLKYTAQD HSDYRYVAAA LAVMRNVTQQ INERKRRLEN 

       310        320        330        340        350        360 
IDKIAQWQAS VLDWEGDDIL DRSSELIYTG EMAWIYQPYG RNQQRVFFLF DHQMVLCKKD 

       370        380        390        400        410        420 
LIRRDILYYK GRIDMDKYEV IDIEDGRDDD FNVSMKNAFK LHNKETEEVH LFFAKKLEEK 

       430        440        450        460        470        480 
IRWLRAFREE RKMVQEDEKI GFEISENQKR QAAMTVRKAS KQKGRVGEEE NQSLELKRAC 

       490 
EVLQRLWSPG KKS 

« Hide

Isoform 2 (Collybistin II) [UniParc].

Checksum: 4AFFE36CFEE5A820
Show »

FASTA41149,156

References

[1]"Collybistin, a newly identified brain-specific GEF, induces submembrane clustering of gephyrin."
Kins S., Betz H., Kirsch J.
Nat. Neurosci. 3:22-29(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH GPHN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"Identification of a gephyrin-binding motif in the GDP/GTP exchange factor collybistin."
Grosskreutz Y., Hermann A., Kins S., Fuhrmann J.C., Betz H., Kneussel M.
Biol. Chem. 382:1455-1462(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GPHN, MUTAGENESIS OF ARG-107; ASP-108; ARG-111 AND GLU-117.
[3]"The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering."
Harvey K., Duguid I.C., Alldred M.J., Beatty S.E., Ward H., Keep N.H., Lingenfelter S.E., Pearce B.R., Lundgren J., Owen M.J., Smart T.G., Luescher B., Rees M.I., Harvey R.J.
J. Neurosci. 24:5816-5826(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, FUNCTION, INTERACTION WITH GPHN, SUBCELLULAR LOCATION.
[4]"The crystal structure of Cdc42 in complex with collybistin II, a gephyrin-interacting guanine nucleotide exchange factor."
Xiang S., Kim E.Y., Connelly J.J., Nassar N., Kirsch J., Winking J., Schwarz G., Schindelin H.
J. Mol. Biol. 359:35-46(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 10-411 IN COMPLEX WITH CDC42, MUTAGENESIS OF ARG-107; ASP-108; ARG-111 AND GLU-117.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ250425 mRNA. Translation: CAB65966.1.
AJ302676 mRNA. Translation: CAC16410.1.
RefSeqNP_076447.1. NM_023957.1.
UniGeneRn.163449.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DFKX-ray2.15A/C71-463[»]
ProteinModelPortalQ9QX73.
SMRQ9QX73. Positions 11-461.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9QX73.

Proteomic databases

PaxDbQ9QX73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID66013.
KEGGrno:66013.

Organism-specific databases

CTD23229.
RGD620719. Arhgef9.

Phylogenomic databases

eggNOGCOG5422.
HOGENOMHOG000237363.
HOVERGENHBG050568.
PhylomeDBQ9QX73.

Gene expression databases

GenevestigatorQ9QX73.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR000219. DH-domain.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9QX73.
NextBio614272.

Entry information

Entry nameARHG9_RAT
AccessionPrimary (citable) accession number: Q9QX73
Secondary accession number(s): Q9ER22
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references