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Q8CFN2 (CDC42_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Cell division control protein 42 homolog
Gene names
Name:Cdc42
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase. Plays a role in the extension and maintenance of the formation of thin, actin-rich surface projections called filopodia. Mediates CDC42-dependent cell migration By similarity.

Enzyme regulation

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase By similarity.

Subunit structure

Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4, CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-dependent manner). Interacts with activated CSPG4 and with BAIAP2. Interacts with Zizimin1/DOCK9 and Zizimin2/DOCK11, which activate it by exchanging GDP for GTP. Interacts with NET1 and ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and PRKCI or PRKCZ. The GTP-bound form interacts with CCPG1 By similarity. Interacts with USP6 By similarity. Interacts with NEK6 By similarity. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas By similarity.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasmcytoskeletoncentrosome By similarity. Midbody By similarity. Note: Localizes to spindle during prometaphase cells. Moves to the central spindle as cells progressed through anaphase to telophase. Localizes at the end of cytokinesis in the intercellular bridge formed between two daughter cells. Its localization is regulated by the activities of guanine nucleotide exchange factor ECT2 and GTPase activating protein RACGAP1. Colocalizes with NEK6 in the centrosome By similarity.

Sequence similarities

Belongs to the small GTPase superfamily. Rho family. CDC42 subfamily.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processestablishment of cell polarity

Traceable author statement. Source: RGD

positive regulation of DNA replication

Inferred from mutant phenotype. Source: RGD

positive regulation of JNK cascade

Inferred from direct assay. Source: RGD

positive regulation of cell cycle cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of attachment of spindle microtubules to kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of exocytosis

Traceable author statement. Source: UniProtKB

regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

response to glucose stimulus

Traceable author statement. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi membrane

Inferred from direct assay. Source: RGD

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from sequence or structural similarity. Source: UniProtKB

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: UniProtKB

secretory granule

Inferred from direct assay. Source: UniProtKB

spindle midzone

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionGTP binding

Traceable author statement. Source: UniProtKB

GTPase activity

Traceable author statement. Source: RGD

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CFN2-1)

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: Q8CFN2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     182-191: PKKSRRCVLL → TQPKRKCCIF

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 188188Cell division control protein 42 homolog
PRO_0000270829
Propeptide189 – 1913Removed in mature form By similarity
PRO_0000270830

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue1351N6-acetyllysine By similarity
Modified residue1441N6-acetyllysine By similarity
Modified residue1881Cysteine methyl ester By similarity
Lipidation1881S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence182 – 19110PKKSRRCVLL → TQPKRKCCIF in isoform 2.
VSP_022241

Experimental info

Sequence conflict1591A → P in AAF15538. Ref.1
Sequence conflict1591A → P in AAN63806. Ref.2
Sequence conflict1631K → R in AAF15538. Ref.1

Sequences

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

Last modified January 9, 2007. Version 2.
Checksum: 51A437E22A4D8FFF

FASTA19121,259
        10         20         30         40         50         60 
MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR 

       130        140        150        160        170        180 
DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP 

       190 
EPKKSRRCVL L 

« Hide

Isoform 2 [UniParc].

Checksum: 34B44F923D7D996B
Show »

FASTA19121,283

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of rat Cdc42 GTPase cDNA."
Han J.-S., Kim J.-H., Kim J.G., Park J.-B., Noh D.-Y., Lee K.-H.
Exp. Mol. Med. 32:115-119(2000) [PubMed: 11048641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"The cdc42 plays a protective role in the brain ischemia."
Chen D., Manabu M., Lan J., Jin J., Simon R.P.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pituitary.
[4]Lubec G., Afjehi-Sadat L., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 6-16; 108-120 AND 167-183, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF205635 mRNA. Translation: AAF15538.1.
AF491841 mRNA. Translation: AAN63806.1.
BC060535 mRNA. Translation: AAH60535.1.
IPIIPI00285606.
IPI00388289.
RefSeqNP_741991.3. NM_171994.4.
UniGeneRn.60067.

3D structure databases

HSSPHSSP built from PDB template 1AM4 based on UniProtKB P60953.
ProteinModelPortalQ8CFN2.
SMRQ8CFN2. Positions 1-191.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-3381856.
STRINGQ8CFN2.

PTM databases

PhosphoSiteQ8CFN2.

Proteomic databases

PRIDEQ8CFN2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000018118; ENSRNOP00000018118; ENSRNOG00000013536.
ENSRNOT00000029025; ENSRNOP00000030928; ENSRNOG00000013536.
GeneID64465.
KEGGrno:64465.

Organism-specific databases

CTD998.
RGD71043. Cdc42.

Phylogenomic databases

eggNOGroNOG07751.
GeneTreeENSGT00560000076570.
HOVERGENHBG009351.
InParanoidQ8CFN2.
OMAEITHHCQ.
OrthoDBEOG4R23VV.
PhylomeDBQ8CFN2.

Gene expression databases

ArrayExpressQ8CFN2.
GenevestigatorQ8CFN2.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
KOK04393.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613224.

Entry information

Entry nameCDC42_RAT
AccessionPrimary (citable) accession number: Q8CFN2
Secondary accession number(s): Q6P9Y3, Q71TW5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: November 16, 2011
This is version 74 of the entry and version 2 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