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Rho-related GTP-binding protein RhoJ (Tc10-like GTP-binding protein)

 RHOJ_MOUSE              Reviewed;         214 AA.
Q9ER71; Q3TX76; Q920E4; Q9CQA7;
25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
25-OCT-2002, sequence version 2.
23-MAY-2018, entry version 137.
RecName: Full=Rho-related GTP-binding protein RhoJ;
AltName: Full=Tc10-like GTP-binding protein;
Flags: Precursor;
Name=Rhoj; Synonyms=Arhj, Rhoi, Rhot, Tc10l, Tcl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=10967094; DOI=10.1074/jbc.M003487200;
Vignal E., De Toledo M., Comunale F., Ladopoulou A.,
Gauthier-Rouviere C., Blangy A., Fort P.;
"Characterization of TCL, a new GTPase of the Rho family related to
TC10 and Cdc42.";
J. Biol. Chem. 275:36457-36464(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
Allen M., Halford S., Daniels H., McIntosh B., Kanuga N.,
Greenwood J., Carey A.H., Adamson P.;
"A novel Rho GTPase (RhoI) induces loss of stress-fibers and results
in apical actin reorganization.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Abe T., Endo T.;
"Cdc42 subfamily small GTPases, Tc10 and RhoT.";
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: GTP-binding protein with GTPase activity. Elicits the
formation of F-actin-rich structures in fibroblasts and is
involved in the regulation of cell morphology.
{ECO:0000269|PubMed:10967094}.
-!- SUBUNIT: Interacts with the CRIB domains of proteins such as Pak1
and Was/Wasp. {ECO:0000269|PubMed:10967094}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ER71-1; Sequence=Displayed;
Name=2;
IsoId=Q9ER71-2; Sequence=VSP_005709;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart with moderate levels
in lung and liver. Very low levels detected in brain, spleen,
skeletal muscle, kidney and testis. {ECO:0000269|PubMed:10967094}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
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EMBL; AJ276568; CAC06700.1; -; mRNA.
EMBL; AF309564; AAL09441.1; -; mRNA.
EMBL; AB060651; BAB91069.1; -; mRNA.
EMBL; AK003482; BAB22812.1; -; mRNA.
EMBL; AK003490; BAB22818.1; -; mRNA.
EMBL; AK156619; BAE33778.1; -; mRNA.
EMBL; AK159385; BAE35040.1; -; mRNA.
EMBL; BC043719; AAH43719.1; -; mRNA.
CCDS; CCDS25981.1; -. [Q9ER71-1]
RefSeq; NP_075764.1; NM_023275.2. [Q9ER71-1]
UniGene; Mm.27467; -.
ProteinModelPortal; Q9ER71; -.
SMR; Q9ER71; -.
BioGrid; 219817; 6.
STRING; 10090.ENSMUSP00000059498; -.
iPTMnet; Q9ER71; -.
PhosphoSitePlus; Q9ER71; -.
PaxDb; Q9ER71; -.
PRIDE; Q9ER71; -.
Ensembl; ENSMUST00000055390; ENSMUSP00000059498; ENSMUSG00000046768. [Q9ER71-1]
GeneID; 80837; -.
KEGG; mmu:80837; -.
UCSC; uc007nxc.1; mouse. [Q9ER71-1]
CTD; 57381; -.
MGI; MGI:1931551; Rhoj.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000118978; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; Q9ER71; -.
KO; K07864; -.
OMA; KKRCSEC; -.
OrthoDB; EOG091G0KCM; -.
PhylomeDB; Q9ER71; -.
TreeFam; TF101109; -.
Reactome; R-MMU-194840; Rho GTPase cycle.
PRO; PR:Q9ER71; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000046768; -.
CleanEx; MM_RHOJ; -.
ExpressionAtlas; Q9ER71; baseline and differential.
Genevisible; Q9ER71; MM.
GO; GO:0005622; C:intracellular; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; ISS:MGI.
GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
GO; GO:0061299; P:retina vasculature morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell shape; Complete proteome;
GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
Prenylation; Reference proteome.
CHAIN 1 211 Rho-related GTP-binding protein RhoJ.
/FTId=PRO_0000198870.
PROPEP 212 214 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281221.
NP_BIND 28 35 GTP. {ECO:0000250}.
NP_BIND 75 79 GTP. {ECO:0000250}.
NP_BIND 133 136 GTP. {ECO:0000250}.
MOTIF 50 58 Effector region. {ECO:0000255}.
MOD_RES 211 211 Cysteine methyl ester. {ECO:0000250}.
LIPID 211 211 S-farnesyl cysteine. {ECO:0000250}.
VAR_SEQ 4 13 Missing (in isoform 2).
{ECO:0000303|PubMed:10967094}.
/FTId=VSP_005709.
CONFLICT 166 166 A -> R (in Ref. 2; AAL09441).
{ECO:0000305}.
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


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