RHOJ_MOUSE
ID RHOJ_MOUSE Reviewed; 214 AA.
AC Q9ER71; Q3TX76; Q920E4; Q9CQA7;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rho-related GTP-binding protein RhoJ;
DE AltName: Full=Tc10-like GTP-binding protein {ECO:0000303|PubMed:10967094};
DE Flags: Precursor;
GN Name=Rhoj;
GN Synonyms=Arhj, Rhoi {ECO:0000303|Ref.3}, Rhot, Tc10l,
GN Tcl {ECO:0000303|PubMed:10967094};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=10967094; DOI=10.1074/jbc.m003487200;
RA Vignal E., De Toledo M., Comunale F., Ladopoulou A., Gauthier-Rouviere C.,
RA Blangy A., Fort P.;
RT "Characterization of TCL, a new GTPase of the Rho family related to TC10
RT and Cdc42.";
RL J. Biol. Chem. 275:36457-36464(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=12456725; DOI=10.1242/jcs.00208;
RA Abe T., Kato M., Miki H., Takenawa T., Endo T.;
RT "Small GTPase Tc10 and its homologue RhoT induce N-WASP-mediated long
RT process formation and neurite outgrowth.";
RL J. Cell Sci. 116:155-168(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Allen M., Halford S., Daniels H., McIntosh B., Kanuga N., Greenwood J.,
RA Carey A.H., Adamson P.;
RT "A novel Rho GTPase (RhoI) induces loss of stress-fibers and results in
RT apical actin reorganization.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plasma membrane-associated small GTPase specifically involved
CC in angiogenesis (By similarity). Required for endothelial cell
CC migration during vascular development via its interaction with GLUL (By
CC similarity). Elicits the formation of F-actin-rich structures, thereby
CC regulating endothelial cell migration (PubMed:10967094).
CC {ECO:0000250|UniProtKB:Q9H4E5, ECO:0000269|PubMed:10967094}.
CC -!- SUBUNIT: Interacts with the CRIB domains of proteins such as Pak1 and
CC Was/Wasp (PubMed:10967094). Interacts with GLUL (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4E5, ECO:0000269|PubMed:10967094}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H4E5};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q9H4E5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9H4E5}. Note=Localization to the plasma
CC membrane is regulated by GLUL. {ECO:0000250|UniProtKB:Q9H4E5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ER71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER71-2; Sequence=VSP_005709;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart with moderate levels in
CC lung and liver (PubMed:10967094). Very low levels detected in brain,
CC spleen, skeletal muscle, kidney and testis (PubMed:10967094).
CC {ECO:0000269|PubMed:10967094}.
CC -!- PTM: Palmitoylated; regulates localization to the plasma membrane and
CC may be mediated by GLUL. {ECO:0000250|UniProtKB:Q9H4E5}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AJ276568; CAC06700.1; -; mRNA.
DR EMBL; AB060651; BAB91069.1; -; mRNA.
DR EMBL; AF309564; AAL09441.1; -; mRNA.
DR EMBL; AK003482; BAB22812.1; -; mRNA.
DR EMBL; AK003490; BAB22818.1; -; mRNA.
DR EMBL; AK156619; BAE33778.1; -; mRNA.
DR EMBL; AK159385; BAE35040.1; -; mRNA.
DR EMBL; BC043719; AAH43719.1; -; mRNA.
DR CCDS; CCDS25981.1; -. [Q9ER71-1]
DR RefSeq; NP_075764.1; NM_023275.2. [Q9ER71-1]
DR AlphaFoldDB; Q9ER71; -.
DR SMR; Q9ER71; -.
DR BioGRID; 219817; 6.
DR STRING; 10090.ENSMUSP00000059498; -.
DR iPTMnet; Q9ER71; -.
DR PhosphoSitePlus; Q9ER71; -.
DR jPOST; Q9ER71; -.
DR MaxQB; Q9ER71; -.
DR PaxDb; Q9ER71; -.
DR PRIDE; Q9ER71; -.
DR ProteomicsDB; 253234; -. [Q9ER71-1]
DR ProteomicsDB; 253235; -. [Q9ER71-2]
DR Antibodypedia; 160; 354 antibodies from 26 providers.
DR DNASU; 80837; -.
DR Ensembl; ENSMUST00000055390; ENSMUSP00000059498; ENSMUSG00000046768. [Q9ER71-1]
DR GeneID; 80837; -.
DR KEGG; mmu:80837; -.
DR UCSC; uc007nxc.1; mouse. [Q9ER71-1]
DR CTD; 57381; -.
DR MGI; MGI:1931551; Rhoj.
DR VEuPathDB; HostDB:ENSMUSG00000046768; -.
DR eggNOG; KOG0393; Eukaryota.
DR GeneTree; ENSGT00940000159098; -.
DR HOGENOM; CLU_041217_21_3_1; -.
DR InParanoid; Q9ER71; -.
DR OMA; YILIGTQ; -.
DR OrthoDB; 1091615at2759; -.
DR PhylomeDB; Q9ER71; -.
DR TreeFam; TF101109; -.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 80837; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Rhoj; mouse.
DR PRO; PR:Q9ER71; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9ER71; protein.
DR Bgee; ENSMUSG00000046768; Expressed in semi-lunar valve and 216 other tissues.
DR ExpressionAtlas; Q9ER71; baseline and differential.
DR Genevisible; Q9ER71; MM.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032488; P:Cdc42 protein signal transduction; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
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 Alternative splicing; Angiogenesis; Cell membrane; GTP-binding;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Palmitate;
KW Prenylation; Reference proteome.
FT CHAIN 1..211
FT /note="Rho-related GTP-binding protein RhoJ"
FT /id="PRO_0000198870"
FT PROPEP 212..214
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000281221"
FT MOTIF 50..58
FT /note="Effector region"
FT /evidence="ECO:0000255"
FT BINDING 31..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT BINDING 177..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q92730"
FT MOD_RES 211
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4E5"
FT LIPID 11
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4E5"
FT LIPID 211
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P62745"
FT VAR_SEQ 4..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10967094"
FT /id="VSP_005709"
FT CONFLICT 166
FT /note="A -> R (in Ref. 3; AAL09441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 23766 MW; A8070C73583A8AA3 CRC64;
MSCRERTDSS CGCNGHEENR ILKCVVVGDG AVGKTCLLMS YANDAFPEEY VPTVFDHYAV
TVTVGGKQHL LGLYDTAGQE DYNQLRPLSY PNTDVFLICF SVVNPASYHN VQEEWVPELK
DCMPHVPYVL IGTQIDLRDD PKTLARLLYM KEKPLTYEHG VKLAKAIGAQ CYLECSALTQ
KGLKAVFDEA ILTIFHPKKK KKGCLGCHGC CAII