RHOH_BOVIN
ID RHOH_BOVIN Reviewed; 191 AA.
AC Q2HJG3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Rho-related GTP-binding protein RhoH;
DE Flags: Precursor;
GN Name=RHOH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is
CC resistant to Rho-specific GTPase-activating proteins. Inhibits the
CC activation of NF-kappa-B by TNF and IKKB and the activation of CRK/p38
CC by TNF. Inhibits activities of RAC1, RHOA and CDC42. Negatively
CC regulates leukotriene production in neutrophils. Negative regulator of
CC hematopoietic progenitor cell proliferation, survival and migration.
CC Critical regulator of thymocyte development and T-cell antigen receptor
CC (TCR) signaling by mediating recruitment and activation of ZAP70.
CC Required for phosphorylation of CD3Z, membrane translocation of ZAP70
CC and subsequent activation of the ZAP70-mediated pathways. Essential for
CC efficient beta-selection and positive selection by promoting the ZAP70-
CC dependent phosphorylation of the LAT signalosome during pre-TCR and TCR
CC signaling. Crucial for thymocyte maturation during DN3 to DN4
CC transition and during positive selection. Plays critical roles in mast
CC cell function by facilitating phosphorylation of SYK in Fc epsilon RI-
CC mediated signal transduction. Essential for the phosphorylation of LAT,
CC LCP2, PLCG1 and PLCG2 and for Ca(2+) mobilization in mast cells.
CC -!- SUBUNIT: Interacts with GDI1 and GDI2. Interacts with ZAP70 (via SH2
CC domains) and the interaction is enhanced by its phosphorylation by LCK.
CC Interacts with SYK and the interaction is enhanced by its
CC phosphorylation by FYN (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=Colocalizes together with ZAP70 in the
CC immunological synapse. {ECO:0000250}.
CC -!- DOMAIN: The region involved in interaction with ZAP70 is a non-
CC canonical immunoreceptor tyrosine-based activation motif (ITAM).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine by LCK. Phosphorylated by FYN.
CC Phosphorylation enhances the interactions with ZAP70 and SYK and is
CC critical for its function in thymocyte development (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; BC105439; AAI05440.1; -; mRNA.
DR RefSeq; NP_001071592.1; NM_001078124.2.
DR AlphaFoldDB; Q2HJG3; -.
DR SMR; Q2HJG3; -.
DR STRING; 9913.ENSBTAP00000017893; -.
DR PaxDb; Q2HJG3; -.
DR PRIDE; Q2HJG3; -.
DR GeneID; 768307; -.
DR KEGG; bta:768307; -.
DR CTD; 399; -.
DR eggNOG; KOG0393; Eukaryota.
DR InParanoid; Q2HJG3; -.
DR OrthoDB; 1091615at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Phosphoprotein; Prenylation; Reference proteome.
FT CHAIN 1..188
FT /note="Rho-related GTP-binding protein RhoH"
FT /id="PRO_0000284914"
FT PROPEP 189..191
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000284915"
FT REGION 73..86
FT /note="Interaction with ZAP70"
FT /evidence="ECO:0000250"
FT MOTIF 33..41
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 58..62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 188
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 188
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 21260 MW; 484E0DF021C28A90 CRC64;
MLSSIKCVLV GDSAVGKTSL LVRFTSETFP EAYKPTVYEN TGVDVLMDGI QISLGLWDTA
GNDAFRSIRP LSYQQADVVL MCYSVANHNS FLNLKNKWIG EVRSNLPCTP VLVVATQTDQ
REVGPHRASC VNAIEGKRLA QDVRAKGYLE CSALSNRGVQ QVFECAVRTA VNQARRRNRR
RFFSINECKI L
