P48148 (RHO1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-like GTP-binding protein Rho1

Gene names

Name:	Rho1
ORF Names:	CG8416

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a role in regulating actin cytoskeletal organization: required during early development for proper execution of morphogenetic movements of individual cells and groups of cells important for the formation of the embryonic body plan. Plays a role in regulating dorsal closure during embryogenesis. May have a role in eye development. Ref.1 Ref.2 Ref.7
Subunit structure	Interacts with capu. Interacts (via REM repeats) with Pkn (via N-terminus). Ref.2 Ref.7 Ref.8
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cytoplasm › cytoskeleton.
Disruption phenotype	Flies lacking maternal Rho1 exhibit actin cytoskeleton disruption in egg chambers, especially in the ring canals and embryos display patterning defects as a result of improper maintenance of segmentation gene expression. Flies lacking zygotic Rho1 exhibit severe defects in head involution and imperfect dorsal closure. Adults show a severe rough eye phenotype characterized by missing secondary and tertiary pigment cells, a substantial reduction in the number of photoreceptor cells and a grossly abnormal morphology of the rhabdomeres. Ref.1 Ref.2
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane
Ligand	Actin-binding GTP-binding Nucleotide-binding
Molecular function	Developmental protein
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JNK cascade Non-traceable author statement PubMed 10449347. Source: FlyBase Wnt receptor signaling pathway Non-traceable author statement PubMed 12231350. Source: FlyBase actin filament bundle assembly Inferred from mutant phenotype PubMed 12402048. Source: FlyBase border follicle cell migration Inferred from mutant phenotype PubMed 17652348. Source: FlyBase branch fusion, open tracheal system Traceable author statement PubMed 15108810. Source: FlyBase cell elongation involved in imaginal disc-derived wing morphogenesis Inferred from mutant phenotype PubMed 19366729. Source: FlyBase cellularization Inferred from mutant phenotype PubMed 15699213. Source: FlyBase cortical actin cytoskeleton organization Inferred from mutant phenotype PubMed 22648168. Source: FlyBase cytokinesis Inferred from mutant phenotype PubMed 12134082PubMed 14527345PubMed 15380073PubMed 15547975PubMed 16174742. Source: FlyBase dendrite morphogenesis Traceable author statement PubMed 12744843. Source: FlyBase dendrite self-avoidance Inferred from genetic interaction PubMed 21937715. Source: FlyBase determination of left/right symmetry Inferred from mutant phenotype PubMed 18836316. Source: FlyBase dorsal closure, leading edge cell differentiation Inferred from mutant phenotype PubMed 12176336. Source: FlyBase dorsal closure, spreading of leading edge cells Inferred from mutant phenotype PubMed 12176336. Source: FlyBase endocytosis Inferred from mutant phenotype PubMed 15649467. Source: FlyBase epidermal growth factor receptor signaling pathway Inferred from genetic interaction PubMed 16818611. Source: FlyBase establishment of imaginal disc-derived wing hair orientation Traceable author statement PubMed 10449347. Source: FlyBase establishment of protein localization Inferred from mutant phenotype PubMed 16174742. Source: FlyBase germ cell migration Traceable author statement PubMed 15108810. Source: FlyBase germ-band extension Inferred from mutant phenotype PubMed 9428514. Source: FlyBase glial cell migration Inferred from mutant phenotype PubMed 12642488. Source: FlyBase hemocyte migration Inferred from mutant phenotype PubMed 15699212. Source: FlyBase lumen formation, open tracheal system Inferred from mutant phenotype PubMed 11880359. Source: FlyBase maintenance of epithelial cell apical/basal polarity Inferred from mutant phenotype PubMed 18585373. Source: FlyBase melanization defense response Inferred from mutant phenotype PubMed 17356067. Source: FlyBase motor neuron axon guidance Inferred from mutant phenotype PubMed 17568577. Source: FlyBase neuroblast proliferation Inferred from mutant phenotype PubMed 10719887. Source: FlyBase ommatidial rotation Non-traceable author statement PubMed 12000787. Source: FlyBase peripheral nervous system development Inferred from mutant phenotype PubMed 12642488PubMed 12967983. Source: FlyBase positive regulation of protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: UniProtKB posterior midgut invagination Inferred from mutant phenotype PubMed 9428514. Source: FlyBase pseudocleavage involved in syncytial blastoderm formation Inferred from mutant phenotype PubMed 19279137. Source: FlyBase regulation of Malpighian tubule size Inferred from mutant phenotype PubMed 15843408. Source: FlyBase regulation of axonogenesis Inferred from genetic interaction PubMed 15572110. Source: FlyBase regulation of cytoskeleton organization Inferred from direct assay PubMed 19633175. Source: FlyBase regulation of embryonic cell shape Inferred from mutant phenotype PubMed 18585373. Source: FlyBase regulation of tube length, open tracheal system Inferred from mutant phenotype PubMed 19956736. Source: FlyBase response to DNA damage stimulus Inferred from mutant phenotype PubMed 19543366. Source: FlyBase salivary gland morphogenesis Inferred from mutant phenotype PubMed 18585373. Source: FlyBase small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro spiracle morphogenesis, open tracheal system Inferred from mutant phenotype PubMed 17021037. Source: FlyBase ventral furrow formation Inferred from mutant phenotype PubMed 9428514. Source: FlyBase visual perception Inferred from electronic annotation. Source: UniProtKB-KW wound healing Inferred from mutant phenotype PubMed 12402048PubMed 19884309. Source: FlyBase
Cellular_component	cell cortex Inferred from direct assay PubMed 16518391. Source: FlyBase cell hair Inferred from direct assay PubMed 19576201. Source: FlyBase cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence or structural similarity PubMed 14579253. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 189	189	Ras-like GTP-binding protein Rho1		PRO_0000198885
	Propeptide	190 – 192	3	Removed in mature form By similarity		PRO_0000281238
Regions
	Nucleotide binding	12 – 19	8	GTP By similarity
	Nucleotide binding	59 – 63	5	GTP By similarity
	Nucleotide binding	117 – 120	4	GTP By similarity
	Motif	34 – 42	9	Effector region Potential
Amino acid modifications
	Modified residue	189	1	Cysteine methyl ester By similarity
	Lipidation	189	1	S-geranylgeranyl cysteine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P48148 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: B89C7D884E1743CF	FASTA	192	21,723
	10 20 30 40 50 60 MTTIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT 70 80 90 100 110 120 AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 130 140 150 160 170 180 LRNDPNTIRD LAKMKQEPVK PQEGRAMAEK INAFAYLECS AKSKEGVRDV FETATRAALQ 190 VKKRKKTRCL LL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of rho GTPase family homologues in Drosophila melanogaster: overexpressing Rho1 in retinal cells causes a late developmental defect." Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M., Settleman J. EMBO J. 14:292-302(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, DISRUPTION PHENOTYPE.
[2]	"Mutations in the Rho1 small GTPase disrupt morphogenesis and segmentation during early Drosophila development." Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M. Development 126:5353-5364(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH CAPU, DISRUPTION PHENOTYPE.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
[6]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[7]	"The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis." Lu Y., Settleman J. Genes Dev. 13:1168-1180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PKN.
[8]	"A rho-binding protein kinase C-like activity is required for the function of protein kinase N in Drosophila development." Betson M., Settleman J. Genetics 176:2201-2212(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PKN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L38311 mRNA. Translation: AAA67042.1. AF177871 Genomic DNA. Translation: AAF01183.1. AF177872 mRNA. Translation: AAF01184.1. AF177873 mRNA. Translation: AAF01185.1. AF177874 mRNA. Translation: AAF01186.1. AE013599 Genomic DNA. Translation: AAM70944.1. AY119536 mRNA. Translation: AAM50190.1. BT010085 mRNA. Translation: AAQ22554.1.
PIR	S54294.
RefSeq	NP_477098.1. NM_057750.3. NP_599135.1. NM_134308.2. NP_599136.1. NM_134309.1. NP_725524.1. NM_166139.2. NP_995849.1. NM_206127.1. NP_995850.1. NM_206128.1. NP_995851.1. NM_206129.1.
UniGene	Dm.644.
3D structure databases
ProteinModelPortal	P48148.
SMR	P48148. Positions 4-180.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-22676N.
IntAct	P48148. 1 interaction.
MINT	MINT-312636.
Proteomic databases
PaxDb	P48148.
PRIDE	P48148.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087211; FBpp0086353; FBgn0014020. FBtr0087212; FBpp0086354; FBgn0014020. FBtr0087213; FBpp0086355; FBgn0014020. FBtr0087214; FBpp0086356; FBgn0014020. FBtr0087215; FBpp0089128; FBgn0014020. FBtr0087216; FBpp0089129; FBgn0014020. FBtr0087217; FBpp0089130; FBgn0014020.
GeneID	36775.
KEGG	dme:Dmel_CG8416.
Organism-specific databases
CTD	36775.
FlyBase	FBgn0014020. Rho1.
Phylogenomic databases
eggNOG	COG1100.
GeneTree	ENSGT00700000104143.
InParanoid	P48148.
KO	K04513.
OMA	NKKRRGC.
OrthoDB	EOG4XPNXX.
PhylomeDB	P48148.
Gene expression databases
Bgee	P48148.
GermOnline	CG8416. Drosophila melanogaster.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003578. Small_GTPase_Rho. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00174. RHO. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51420. RHO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Rho1. drosophila.
GenomeRNAi	36775.
NextBio	800324.

Entry information

Entry name

RHO1_DROME

Accession

Primary (citable) accession number: P48148
Secondary accession number(s): Q0E958, Q9V3J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project