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Ras-related C3 botulinum toxin substrate 3 (p21-Rac3)

 RAC3_HUMAN              Reviewed;         192 AA.
P60763; O14658; Q5U0M8;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
12-SEP-2018, entry version 150.
RecName: Full=Ras-related C3 botulinum toxin substrate 3;
AltName: Full=p21-Rac3;
Flags: Precursor;
Name=RAC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9252344; DOI=10.1074/jbc.272.33.20384;
Haataja L., Groffen J., Heisterkamp N.;
"Characterization of RAC3, a novel member of the Rho family.";
J. Biol. Chem. 272:20384-20388(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH C1D.
PubMed=9852280;
Haataja L., Groffen J., Heisterkamp N.;
"Identification of a novel Rac3-interacting protein C1D.";
Int. J. Mol. Med. 1:665-670(1998).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NRBP.
PubMed=11956649;
De Langhe S., Haataja L., Senadheera D., Groffen J., Heisterkamp N.;
"Interaction of the small GTPase Rac3 with NRBP, a protein with a
kinase-homology domain.";
Int. J. Mol. Med. 9:451-459(2002).
[7]
FUNCTION, INTERACTION WITH CIB1, AND SUBCELLULAR LOCATION.
PubMed=11756406; DOI=10.1074/jbc.M105363200;
Haataja L., Kaartinen V., Groffen J., Heisterkamp N.;
"The small GTPase Rac3 interacts with the integrin-binding protein CIB
and promotes integrin alpha(IIb)beta(3)-mediated adhesion and
spreading.";
J. Biol. Chem. 277:8321-8328(2002).
[8]
INTERACTION WITH DOCK7.
PubMed=16982419; DOI=10.1016/j.neuron.2006.07.020;
Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.;
"The Rac activator DOCK7 regulates neuronal polarity through local
phosphorylation of stathmin/Op18.";
Neuron 51:727-739(2006).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
GLYCOSYLATION AT TYR-32 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:11756406, ECO:0000269|PubMed:11956649,
ECO:0000269|PubMed:16982419, ECO:0000269|PubMed:9852280}.
-!- INTERACTION:
P03372:ESR1; NbExp=5; IntAct=EBI-767084, EBI-78473;
Q9UHY1:NRBP1; NbExp=3; IntAct=EBI-767084, EBI-749731;
-!- SUBCELLULAR LOCATION: Cytoplasm. Endomembrane system. Cell
projection, lamellipodium. Cytoplasm, perinuclear region. Cell
membrane. Cytoplasm, cytoskeleton. Note=Membrane-associated when
activated. Colocalizes with NRBP to endomembranes and at the cell
periphery in lamellipodia. Colocalized with CIB1 in the
perinuclear area and at the cell periphery.
-!- TISSUE SPECIFICITY: Highest levels in brain, also detected in
heart, placenta and pancreas.
-!- INDUCTION: Expression down-regulated in quiescent fibroblasts and
clearly induced by serum stimulation.
-!- PTM: (Microbial infection) Glycosylated at Tyr-32 by Photorhabdus
asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
inhibits downstream signaling by an impaired interaction with
diverse regulator and effector proteins of Rac and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RAC3ID42022ch17q25.html";
-----------------------------------------------------------------------
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EMBL; AF008591; AAC51667.1; -; mRNA.
EMBL; AF498966; AAM21113.1; -; mRNA.
EMBL; BT019443; AAV38250.1; -; mRNA.
EMBL; BC009605; AAH09605.1; -; mRNA.
EMBL; BC015197; AAH15197.1; -; mRNA.
CCDS; CCDS11798.1; -.
RefSeq; NP_005043.1; NM_005052.2.
UniGene; Hs.45002; -.
PDB; 2C2H; X-ray; 1.85 A; A/B=1-192.
PDB; 2G0N; X-ray; 1.90 A; A/B=1-177.
PDB; 2IC5; X-ray; 1.90 A; A/B=1-178.
PDB; 2OV2; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-177.
PDB; 2QME; X-ray; 1.75 A; A=1-177.
PDBsum; 2C2H; -.
PDBsum; 2G0N; -.
PDBsum; 2IC5; -.
PDBsum; 2OV2; -.
PDBsum; 2QME; -.
ProteinModelPortal; P60763; -.
SMR; P60763; -.
BioGrid; 111819; 17.
DIP; DIP-33881N; -.
IntAct; P60763; 24.
MINT; P60763; -.
STRING; 9606.ENSP00000304283; -.
ChEMBL; CHEMBL6087; -.
iPTMnet; P60763; -.
PhosphoSitePlus; P60763; -.
SwissPalm; P60763; -.
BioMuta; RAC3; -.
DMDM; 46397673; -.
EPD; P60763; -.
MaxQB; P60763; -.
PaxDb; P60763; -.
PeptideAtlas; P60763; -.
PRIDE; P60763; -.
ProteomicsDB; 57225; -.
TopDownProteomics; P60763; -.
DNASU; 5881; -.
Ensembl; ENST00000306897; ENSP00000304283; ENSG00000169750.
GeneID; 5881; -.
KEGG; hsa:5881; -.
UCSC; uc002kdf.4; human.
CTD; 5881; -.
DisGeNET; 5881; -.
EuPathDB; HostDB:ENSG00000169750.8; -.
GeneCards; RAC3; -.
HGNC; HGNC:9803; RAC3.
HPA; HPA047820; -.
MIM; 602050; gene.
neXtProt; NX_P60763; -.
OpenTargets; ENSG00000169750; -.
PharmGKB; PA34164; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P60763; -.
KO; K07861; -.
OMA; GKKCTMF; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; P60763; -.
TreeFam; TF101109; -.
BRENDA; 3.6.5.2; 2681.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-4086400; PCP/CE pathway.
SIGNOR; P60763; -.
EvolutionaryTrace; P60763; -.
GeneWiki; RAC3; -.
GenomeRNAi; 5881; -.
PRO; PR:P60763; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000169750; Expressed in 111 organ(s), highest expression level in cerebellar hemisphere.
CleanEx; HS_RAC3; -.
ExpressionAtlas; P60763; baseline and differential.
Genevisible; P60763; HS.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031941; C:filamentous actin; IDA:MGI.
GO; GO:0030426; C:growth cone; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0030031; P:cell projection assembly; IDA:UniProtKB.
GO; GO:0021894; P:cerebral cortex GABAergic interneuron development; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; TAS:UniProtKB.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0014041; P:regulation of neuron maturation; IEA:Ensembl.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Glycoprotein; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome.
CHAIN 1 189 Ras-related C3 botulinum toxin substrate
3.
/FTId=PRO_0000198889.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281240.
NP_BIND 10 17 GTP. {ECO:0000250}.
NP_BIND 57 61 GTP. {ECO:0000250}.
NP_BIND 115 118 GTP. {ECO:0000250}.
MOTIF 32 40 Effector region. {ECO:0000255}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine. {ECO:0000250}.
CARBOHYD 32 32 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230.
{ECO:0000269|PubMed:24141704}.
STRAND 2 10 {ECO:0000244|PDB:2QME}.
HELIX 16 25 {ECO:0000244|PDB:2QME}.
STRAND 36 46 {ECO:0000244|PDB:2QME}.
STRAND 49 58 {ECO:0000244|PDB:2QME}.
HELIX 62 64 {ECO:0000244|PDB:2QME}.
TURN 65 67 {ECO:0000244|PDB:2QME}.
HELIX 68 71 {ECO:0000244|PDB:2QME}.
STRAND 76 83 {ECO:0000244|PDB:2QME}.
HELIX 87 95 {ECO:0000244|PDB:2QME}.
HELIX 97 104 {ECO:0000244|PDB:2QME}.
STRAND 105 108 {ECO:0000244|PDB:2C2H}.
STRAND 110 115 {ECO:0000244|PDB:2QME}.
HELIX 117 119 {ECO:0000244|PDB:2QME}.
HELIX 123 130 {ECO:0000244|PDB:2QME}.
TURN 131 133 {ECO:0000244|PDB:2QME}.
HELIX 139 148 {ECO:0000244|PDB:2QME}.
STRAND 152 156 {ECO:0000244|PDB:2QME}.
TURN 159 161 {ECO:0000244|PDB:2QME}.
HELIX 165 177 {ECO:0000244|PDB:2QME}.
SEQUENCE 192 AA; 21379 MW; 560BBC26BB7CDF4A CRC64;
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR
DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP
PVKKPGKKCT VF


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