Rnd1

Protein-coding gene in the species Homo sapiens
RND1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2CLS, 2REX, 3Q3J

Identifiers
AliasesRND1, ARHS, RHO6, RHOS, Rnd1, Rho family GTPase 1
External IDsOMIM: 609038; MGI: 2444878; HomoloGene: 8706; GeneCards: RND1; OMA:RND1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for RND1
Genomic location for RND1
Band12q13.12Start48,857,145 bp[1]
End48,865,870 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for RND1
Genomic location for RND1
Band15|15 F1Start98,561,302 bp[2]
End98,575,342 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • vena cava

  • right lobe of liver

  • frontal pole

  • prefrontal cortex

  • right frontal lobe

  • middle temporal gyrus

  • dorsolateral prefrontal cortex

  • primary visual cortex

  • Brodmann area 9

  • cingulate gyrus
Top expressed in
  • lumbar subsegment of spinal cord

  • granulocyte

  • primary visual cortex

  • morula

  • ventricular zone

  • cerebellar cortex

  • superior frontal gyrus

  • endothelial cell of lymphatic vessel

  • neural layer of retina

  • dorsomedial hypothalamic nucleus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • signaling receptor binding
  • protein binding
  • GTPase activity
  • protein kinase binding
Cellular component
  • cytoplasm
  • adherens junction
  • cytosol
  • cytoskeleton
  • membrane
  • plasma membrane
  • actin cytoskeleton
  • intracellular membrane-bounded organelle
  • intracellular anatomical structure
  • cell cortex
  • cell division site
Biological process
  • neuron remodeling
  • small GTPase mediated signal transduction
  • negative regulation of cell adhesion
  • actin filament organization
  • Rho protein signal transduction
  • regulation of cell shape
  • regulation of cell migration
  • establishment or maintenance of actin cytoskeleton polarity
  • regulation of actin cytoskeleton organization
  • actin filament bundle assembly
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

27289

223881

Ensembl

ENSG00000172602

ENSMUSG00000054855

UniProt

Q92730

Q8BLR7

RefSeq (mRNA)

NM_014470

NM_172612

RefSeq (protein)

NP_055285

NP_766200

Location (UCSC)Chr 12: 48.86 – 48.87 MbChr 15: 98.56 – 98.58 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rnd1 is a small (~21 kDa) signaling G protein (to be specific, a GTPase), and is a member of the Rnd subgroup of the Rho family of GTPases.[5] It is encoded by the gene RND1.[6]

It contributes to regulating the organization of the actin cytoskeleton in response to extracellular growth factors (Nobes et al., 1998).[supplied by OMIM][6]

Interactions

Rnd1 has been shown to interact with GRB7,[7] PLXNB1,[8] PDE6D,[9][10] ARHGAP5[11] and UBXD5.[12]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172602 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000054855 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Ridley AJ (Oct 2006). "Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking". Trends in Cell Biology. 16 (10): 522–9. doi:10.1016/j.tcb.2006.08.006. PMID 16949823.
  6. ^ a b "Entrez Gene: RND1 Rho family GTPase 1".
  7. ^ Vayssière B, Zalcman G, Mahé Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J (Feb 2000). "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family". FEBS Letters. 467 (1): 91–6. doi:10.1016/S0014-5793(99)01530-6. PMID 10664463. S2CID 4901644.
  8. ^ Oinuma I, Katoh H, Harada A, Negishi M (Jul 2003). "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells". The Journal of Biological Chemistry. 278 (28): 25671–7. doi:10.1074/jbc.M303047200. PMID 12730235.
  9. ^ Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
  10. ^ Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
  11. ^ Wennerberg K, Forget MA, Ellerbroek SM, Arthur WT, Burridge K, Settleman J, Der CJ, Hansen SH (Jul 2003). "Rnd proteins function as RhoA antagonists by activating p190 RhoGAP". Current Biology. 13 (13): 1106–15. Bibcode:2003CBio...13.1106W. doi:10.1016/S0960-9822(03)00418-4. PMC 6918695. PMID 12842009.
  12. ^ Katoh H, Harada A, Mori K, Negishi M (May 2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Molecular and Cellular Biology. 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.

Further reading

  • Nobes CD, Lauritzen I, Mattei MG, Paris S, Hall A, Chardin P (Apr 1998). "A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion". The Journal of Cell Biology. 141 (1): 187–97. doi:10.1083/jcb.141.1.187. PMC 2132722. PMID 9531558.
  • Vayssière B, Zalcman G, Mahé Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J (Feb 2000). "Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family". FEBS Letters. 467 (1): 91–6. doi:10.1016/S0014-5793(99)01530-6. PMID 10664463. S2CID 4901644.
  • Aoki J, Katoh H, Mori K, Negishi M (Nov 2000). "Rnd1, a novel rho family GTPase, induces the formation of neuritic processes in PC12 cells". Biochemical and Biophysical Research Communications. 278 (3): 604–8. doi:10.1006/bbrc.2000.3842. PMID 11095956.
  • Rohm B, Rahim B, Kleiber B, Hovatta I, Püschel AW (Dec 2000). "The semaphorin 3A receptor may directly regulate the activity of small GTPases". FEBS Letters. 486 (1): 68–72. doi:10.1016/S0014-5793(00)02240-7. PMID 11108845. S2CID 7914214.
  • Nancy V, Callebaut I, El Marjou A, de Gunzburg J (Apr 2002). "The delta subunit of retinal rod cGMP phosphodiesterase regulates the membrane association of Ras and Rap GTPases". The Journal of Biological Chemistry. 277 (17): 15076–84. doi:10.1074/jbc.M109983200. PMID 11786539.
  • Katoh H, Harada A, Mori K, Negishi M (May 2002). "Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers". Molecular and Cellular Biology. 22 (9): 2952–64. doi:10.1128/MCB.22.9.2952-2964.2002. PMC 133765. PMID 11940653.
  • Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC (May 2002). "The complex of Arl2-GTP and PDE delta: from structure to function". The EMBO Journal. 21 (9): 2095–106. doi:10.1093/emboj/21.9.2095. PMC 125981. PMID 11980706.
  • Oinuma I, Katoh H, Harada A, Negishi M (Jul 2003). "Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells". The Journal of Biological Chemistry. 278 (28): 25671–7. doi:10.1074/jbc.M303047200. PMID 12730235.
  • Oinuma I, Ishikawa Y, Katoh H, Negishi M (Aug 2004). "The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras". Science. 305 (5685): 862–5. Bibcode:2004Sci...305..862O. doi:10.1126/science.1097545. PMID 15297673. S2CID 39544623.
  • Harada A, Katoh H, Negishi M (May 2005). "Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells". The Journal of Biological Chemistry. 280 (18): 18418–24. doi:10.1074/jbc.M411356200. PMID 15738000.
  • Kim YS, Hori M, Yasuda K, Ozaki H (Dec 2005). "Differences in the gestational pattern of mRNA expression of the Rnd family in rat and human myometria". Comparative Biochemistry and Physiology A. 142 (4): 410–5. doi:10.1016/j.cbpa.2005.08.028. PMID 16311049.
  • v
  • t
  • e
  • 2cls: THE CRYSTAL STRUCTURE OF THE HUMAN RND1 GTPASE IN THE ACTIVE GTP BOUND STATE
    2cls: THE CRYSTAL STRUCTURE OF THE HUMAN RND1 GTPASE IN THE ACTIVE GTP BOUND STATE
  • v
  • t
  • e
3.6.1
3.6.2
3.6.3-4: ATPase
3.6.3
Cu++ (3.6.3.4)
Ca+ (3.6.3.8)
Na+/K+ (3.6.3.9)
H+/K+ (3.6.3.10)
  • ATP4A
Other P-type ATPase
3.6.4
3.6.5: GTPase
3.6.5.1: Heterotrimeric G protein
3.6.5.2: Small GTPase > Ras superfamily
3.6.5.3: Protein-synthesizing GTPase
3.6.5.5-6: Polymerization motors


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