RHOB_RAT
ID RHOB_RAT Reviewed; 196 AA.
AC P62747; P01121; Q9CUV7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Rho-related GTP-binding protein RhoB;
DE Flags: Precursor;
GN Name=Rhob; Synonyms=Arhb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1710770; DOI=10.1128/mcb.11.7.3682-3690.1991;
RA Jaehner D., Hunter T.;
RT "The ras-related gene rhoB is an immediate-early gene inducible by v-Fps,
RT epidermal growth factor, and platelet-derived growth factor in rat
RT fibroblasts.";
RL Mol. Cell. Biol. 11:3682-3690(1991).
RN [2]
RP INTERACTION WITH ROCK1 AND ROCK2.
RX PubMed=8816443; DOI=10.1128/mcb.16.10.5313;
RA Leung T., Chen X.-Q., Manser E., Lim L.;
RT "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and
RT is involved in the reorganization of the cytoskeleton.";
RL Mol. Cell. Biol. 16:5313-5327(1996).
RN [3]
RP INDUCTION.
RX PubMed=13679852; DOI=10.1038/sj.onc.1206638;
RA Malcolm T., Ettehadieh E., Sadowski I.;
RT "Mitogen-responsive expression of RhoB is regulated by RNA stability.";
RL Oncogene 22:6142-6150(2003).
CC -!- FUNCTION: Mediates apoptosis in neoplastically transformed cells after
CC DNA damage. Not essential for development but affects cell adhesion and
CC growth factor signaling in transformed cells. Plays a negative role in
CC tumorigenesis as deletion causes tumor formation. Involved in
CC intracellular protein trafficking of a number of proteins. Targets PKN1
CC to endosomes and is involved in trafficking of the EGF receptor from
CC late endosomes to lysosomes. Also required for stability and nuclear
CC trafficking of AKT1/AKT which promotes endothelial cell survival during
CC vascular development. Serves as a microtubule-dependent signal that is
CC required for the myosin contractile ring formation during cell cycle
CC cytokinesis. Required for genotoxic stress-induced cell death in breast
CC cancer cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds ROCK1 and ROCK2 (PubMed:8816443). Also binds PKN1/PRK1.
CC Interacts with ARGGEF3. Interacts with RTKN. Interacts with AKAP13.
CC Interacts with RIPOR1 (By similarity). {ECO:0000250|UniProtKB:P62745,
CC ECO:0000250|UniProtKB:P62746, ECO:0000269|PubMed:8816443}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Lipid-
CC anchor {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Nucleus {ECO:0000250}. Cleavage furrow {ECO:0000250}.
CC Note=Late endosomal membrane (geranylgeranylated form). Plasma membrane
CC (farnesylated form). Also detected at the nuclear margin and in the
CC nucleus. Translocates to the equatorial region before furrow formation
CC in a ECT2-dependent manner (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Expressed at very low levels in quiescent cells but is
CC transiently induced by serum stimulation with levels increasing to a
CC maximum within 30 minutes and declining over the next hour.
CC {ECO:0000269|PubMed:13679852}.
CC -!- PTM: Prenylation specifies the subcellular location of RHOB. The
CC farnesylated form is localized to the plasma membrane while the
CC geranylgeranylated form is localized to the endosome (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; M74295; AAA42040.1; -; mRNA.
DR PIR; A39727; TVRTRH.
DR RefSeq; NP_071987.1; NM_022542.1.
DR AlphaFoldDB; P62747; -.
DR SMR; P62747; -.
DR BioGRID; 249057; 1.
DR STRING; 10116.ENSRNOP00000008008; -.
DR iPTMnet; P62747; -.
DR PhosphoSitePlus; P62747; -.
DR SwissPalm; P62747; -.
DR jPOST; P62747; -.
DR PaxDb; P62747; -.
DR PRIDE; P62747; -.
DR GeneID; 64373; -.
DR KEGG; rno:64373; -.
DR CTD; 388; -.
DR RGD; 621309; Rhob.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_2_1; -.
DR InParanoid; P62747; -.
DR OMA; WEVFETA; -.
DR OrthoDB; 1166960at2759; -.
DR PhylomeDB; P62747; -.
DR TreeFam; TF300837; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-416482; G alpha (12/13) signalling events.
DR Reactome; R-RNO-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-RNO-5625740; RHO GTPases activate PKNs.
DR Reactome; R-RNO-5625900; RHO GTPases activate CIT.
DR Reactome; R-RNO-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR PRO; PR:P62747; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000021403; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; P62747; RN.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Apoptosis; Cell adhesion; Cell membrane;
KW Developmental protein; Differentiation; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Methylation; Nucleotide-binding; Nucleus; Palmitate;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport; Tumor suppressor.
FT CHAIN 1..193
FT /note="Rho-related GTP-binding protein RhoB"
FT /id="PRO_0000030421"
FT PROPEP 194..196
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000030422"
FT MOTIF 34..42
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 12..19
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 59..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 154
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62746"
FT MOD_RES 193
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 189
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 192
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-farnesyl cysteine; in plasma membrane form"
FT /evidence="ECO:0000250"
FT LIPID 193
FT /note="S-geranylgeranyl cysteine; in endosomal form"
FT /evidence="ECO:0000250"
SQ SEQUENCE 196 AA; 22123 MW; CCE6FD53AE00CD83 CRC64;
MAAIRKKLVV VGDGACGKTC LLIVFSKDEF PEVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWV PEVKHFCPNV PIILVANKKD
LRSDEHVRTE LARMKQEPVR TDDGRAMAVR IQAYDYLECS AKTKEGVREV FETATRAALQ
KRYGSQNGCI NCCKVL
