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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
 
 
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