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Protein

Rho-related GTP-binding protein RhoC

Gene

Rhoc

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

Functioni

Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTPBy similarity
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
  2. signal transducer activity Source: MGI

GO - Biological processi

  1. apical junction assembly Source: UniProtKB
  2. cytokinesis Source: UniProtKB
  3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  4. skeletal muscle satellite cell migration Source: AgBase
  5. small GTPase mediated signal transduction Source: InterPro
  6. wound healing, spreading of cells Source: AgBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.
REACT_299052. G alpha (12/13) signalling events.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho-related GTP-binding protein RhoC
Alternative name(s):
Silica-induced gene 61 protein
Short name:
SIG-61
Gene namesi
Name:Rhoc
Synonyms:Arhc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:106028. Rhoc.

Subcellular locationi

  1. Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated
  2. Cleavage furrow By similarity

  3. Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.By similarity

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: MGI
  4. nucleus Source: MGI
  5. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Rho-related GTP-binding protein RhoCPRO_0000042024Add
BLAST
Propeptidei191 – 1933Removed in mature formBy similarityPRO_0000042025

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901Cysteine methyl esterBy similarity
Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ62159.
PaxDbiQ62159.
PRIDEiQ62159.

PTM databases

PhosphoSiteiQ62159.

Expressioni

Inductioni

Up-regulated in silica-treated macrophages.1 Publication

Gene expression databases

BgeeiQ62159.
CleanExiMM_RHOC.
ExpressionAtlasiQ62159. baseline and differential.
GenevestigatoriQ62159.

Interactioni

Subunit structurei

Interacts with AKAP13, DIAPH1, ROCK1 and ROCK2 (By similarity). Interacts with ARHGDIA (By similarity). Interacts with PKN2 and RTKN.By similarity2 Publications

Protein-protein interaction databases

BioGridi198197. 1 interaction.
IntActiQ62159. 2 interactions.
MINTiMINT-4132345.

Structurei

3D structure databases

ProteinModelPortaliQ62159.
SMRiQ62159. Positions 3-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence Analysis

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ62159.
KOiK07857.
OMAiKKRKGCP.
OrthoDBiEOG73FQPD.
PhylomeDBiQ62159.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 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.

Q62159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR
160 170 180 190
ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC PIL
Length:193
Mass (Da):22,006
Last modified:April 13, 2004 - v2
Checksum:iA193DA581560F131
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021E → Q in CAA56682 (PubMed:7868905).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80638 mRNA. Translation: CAA56682.1.
AK011599 mRNA. Translation: BAB27724.1.
AK152802 mRNA. Translation: BAE31507.1.
AK160650 mRNA. Translation: BAE35941.1.
BC004627 mRNA. Translation: AAH04627.1.
CCDSiCCDS17704.1.
RefSeqiNP_001278788.1. NM_001291859.1.
NP_031510.2. NM_007484.2.
UniGeneiMm.262.

Genome annotation databases

EnsembliENSMUST00000002303; ENSMUSP00000002303; ENSMUSG00000002233.
ENSMUST00000106787; ENSMUSP00000102399; ENSMUSG00000002233.
GeneIDi11853.
KEGGimmu:11853.
UCSCiuc008qul.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X80638 mRNA. Translation: CAA56682.1.
AK011599 mRNA. Translation: BAB27724.1.
AK152802 mRNA. Translation: BAE31507.1.
AK160650 mRNA. Translation: BAE35941.1.
BC004627 mRNA. Translation: AAH04627.1.
CCDSiCCDS17704.1.
RefSeqiNP_001278788.1. NM_001291859.1.
NP_031510.2. NM_007484.2.
UniGeneiMm.262.

3D structure databases

ProteinModelPortaliQ62159.
SMRiQ62159. Positions 3-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198197. 1 interaction.
IntActiQ62159. 2 interactions.
MINTiMINT-4132345.

PTM databases

PhosphoSiteiQ62159.

Proteomic databases

MaxQBiQ62159.
PaxDbiQ62159.
PRIDEiQ62159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000002303; ENSMUSP00000002303; ENSMUSG00000002233.
ENSMUST00000106787; ENSMUSP00000102399; ENSMUSG00000002233.
GeneIDi11853.
KEGGimmu:11853.
UCSCiuc008qul.2. mouse.

Organism-specific databases

CTDi389.
MGIiMGI:106028. Rhoc.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiQ62159.
KOiK07857.
OMAiKKRKGCP.
OrthoDBiEOG73FQPD.
PhylomeDBiQ62159.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiREACT_297947. Rho GTPase cycle.
REACT_299052. G alpha (12/13) signalling events.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.

Miscellaneous databases

NextBioi279829.
PROiQ62159.
SOURCEiSearch...

Gene expression databases

BgeeiQ62159.
CleanExiMM_RHOC.
ExpressionAtlasiQ62159. baseline and differential.
GenevestigatoriQ62159.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 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. "Isolation of nine gene sequences induced by silica in murine macrophages."
    Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.
    J. Immunol. 154:2384-2392(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Tissue: Macrophage.
  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: C57BL/6J.
    Tissue: Bone marrow.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
    Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
    J. Biol. Chem. 271:13556-13560(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RTKN.
  5. "The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
    Wallace S.W., Magalhaes A., Hall A.
    Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN2.

Entry informationi

Entry nameiRHOC_MOUSE
AccessioniPrimary (citable) accession number: Q62159
Secondary accession number(s): Q3TUN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 13, 2004
Last modified: April 1, 2015
This is version 143 of the entry and version 2 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

External Data

Dasty 3

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 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.