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Protein

Ras-related C3 botulinum toxin substrate 3

Gene

Rac3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: UniProtKB
  • cell projection assembly Source: UniProtKB
  • cerebral cortex GABAergic interneuron development Source: MGI
  • homeostasis of number of cells within a tissue Source: MGI
  • neuromuscular process Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • neuron projection development Source: MGI
  • positive regulation of cell adhesion mediated by integrin Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • regulation of cell morphogenesis Source: MGI
  • regulation of neuron maturation Source: MGI
  • small GTPase mediated signal transduction Source: InterPro
  • synaptic transmission, GABAergic Source: MGI
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related C3 botulinum toxin substrate 3
Alternative name(s):
p21-Rac3
Gene namesi
Name:Rac3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2180784. Rac3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related C3 botulinum toxin substrate 3PRO_0000198890Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000281241

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

EPDiP60764.
PaxDbiP60764.
PeptideAtlasiP60764.
PRIDEiP60764.

PTM databases

iPTMnetiP60764.
PhosphoSiteiP60764.

Expressioni

Gene expression databases

BgeeiP60764.
CleanExiMM_RAC3.
ExpressionAtlasiP60764. baseline and differential.
GenevisibleiP60764. MM.

Interactioni

Subunit structurei

Interacts with the GEF protein DOCK7, which promotes the exchange between GDP and GTP, and therefore activates it. Interacts with C1D. Interacts (via C-terminal region) with CIB1; the interaction induces their association with the cytoskeleton upon alpha-IIb/beta3 integrin-mediated adhesion (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ArhgdiaQ99PT13EBI-644949,EBI-494354

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228420. 1 interaction.
IntActiP60764. 4 interactions.
MINTiMINT-4131602.
STRINGi10090.ENSMUSP00000018156.

Structurei

3D structure databases

ProteinModelPortaliP60764.
SMRiP60764. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP60764.
KOiK07861.
OMAiGKKCTMF.
OrthoDBiEOG764747.
PhylomeDBiP60764.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60764-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE
110 120 130 140 150
VRHHCPHTPI LLVGTKLDLR DDKDTIERLR DKKLAPITYP QGLAMAREIG
160 170 180 190
SVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKPGKKCT VF
Length:192
Mass (Da):21,379
Last modified:April 13, 2004 - v1
Checksum:i560BBC26BB7CDF4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040819 mRNA. Translation: BAB40573.1.
AK089930 mRNA. Translation: BAC41001.1.
CCDSiCCDS25754.1.
RefSeqiNP_573486.1. NM_133223.4.
UniGeneiMm.34008.

Genome annotation databases

EnsembliENSMUST00000018156; ENSMUSP00000018156; ENSMUSG00000018012.
GeneIDi170758.
KEGGimmu:170758.
UCSCiuc007mug.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB040819 mRNA. Translation: BAB40573.1.
AK089930 mRNA. Translation: BAC41001.1.
CCDSiCCDS25754.1.
RefSeqiNP_573486.1. NM_133223.4.
UniGeneiMm.34008.

3D structure databases

ProteinModelPortaliP60764.
SMRiP60764. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228420. 1 interaction.
IntActiP60764. 4 interactions.
MINTiMINT-4131602.
STRINGi10090.ENSMUSP00000018156.

PTM databases

iPTMnetiP60764.
PhosphoSiteiP60764.

Proteomic databases

EPDiP60764.
PaxDbiP60764.
PeptideAtlasiP60764.
PRIDEiP60764.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018156; ENSMUSP00000018156; ENSMUSG00000018012.
GeneIDi170758.
KEGGimmu:170758.
UCSCiuc007mug.1. mouse.

Organism-specific databases

CTDi5881.
MGIiMGI:2180784. Rac3.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP60764.
KOiK07861.
OMAiGKKCTMF.
OrthoDBiEOG764747.
PhylomeDBiP60764.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

PROiP60764.
SOURCEiSearch...

Gene expression databases

BgeeiP60764.
CleanExiMM_RAC3.
ExpressionAtlasiP60764. baseline and differential.
GenevisibleiP60764. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse Rac3."
    Koga H., Sumimoto H.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Swiss Webster.
    Tissue: Submandibular gland.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRAC3_MOUSE
AccessioniPrimary (citable) accession number: P60764
Secondary accession number(s): O14658
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.