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Protein

Ras-related protein Ral-a

Gene

Rala

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 258GTPBy similarity
Nucleotide bindingi65 – 695GTPBy similarity
Nucleotide bindingi124 – 1274GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: FlyBase
  • GTP binding Source: UniProtKB-KW
  • PDZ domain binding Source: FlyBase

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • defense response to Gram-negative bacterium Source: FlyBase
  • dorsal closure Source: FlyBase
  • innate immune response Source: FlyBase
  • intracellular protein transport Source: InterPro
  • negative regulation of innate immune response Source: FlyBase
  • negative regulation of JNK cascade Source: FlyBase
  • nucleocytoplasmic transport Source: InterPro
  • R3/R4 cell fate commitment Source: FlyBase
  • Ras protein signal transduction Source: FlyBase
  • regulation of cell morphogenesis Source: FlyBase
  • regulation of Notch signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-1445148. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Ral-a
Gene namesi
Name:Rala
ORF Names:CG2849
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0015286. Rala.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: InterPro
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Ras-related protein Ral-aPRO_0000082697Add
BLAST
Propeptidei199 – 2013Removed in mature formBy similarityPRO_0000281348

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei198 – 1981Cysteine methyl esterBy similarity
Lipidationi198 – 1981S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP48555.
PRIDEiP48555.

Expressioni

Gene expression databases

BgeeiP48555.
ExpressionAtlasiP48555. differential.
GenevisibleiP48555. DM.

Interactioni

GO - Molecular functioni

  • PDZ domain binding Source: FlyBase

Protein-protein interaction databases

BioGridi57853. 18 interactions.
DIPiDIP-19199N.
IntActiP48555. 3 interactions.
STRINGi7227.FBpp0070558.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 177Combined sources
Helixi24 – 329Combined sources
Turni45 – 484Combined sources
Beta strandi49 – 546Combined sources
Beta strandi57 – 659Combined sources
Helixi75 – 806Combined sources
Beta strandi84 – 907Combined sources
Helixi96 – 994Combined sources
Helixi101 – 1099Combined sources
Beta strandi118 – 1236Combined sources
Helixi136 – 1438Combined sources
Helixi144 – 1463Combined sources
Beta strandi150 – 1523Combined sources
Turni155 – 1584Combined sources
Helixi161 – 17717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CM8X-ray2.60B1-201[»]
5CM9X-ray2.60C/D1-201[»]
ProteinModelPortaliP48555.
SMRiP48555. Positions 10-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 489Effector region

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ras family.Curated

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
InParanoidiP48555.
KOiK07834.
OMAiFAATTEF.
OrthoDBiEOG7QVM41.
PhylomeDBiP48555.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKKPTAGPA LHKVIMVGSG GVGKSALTLQ FMYDEFVEDY EPTKADSYRK
60 70 80 90 100
KVVLDGEEVQ IDILDTAGQE DYAAIRDNYF RSGEGFLCVF SITDDESFQA
110 120 130 140 150
TQEFREQILR VKNDESIPFL LVGNKCDLND KRKVPLSECQ LRAQQWAVPY
160 170 180 190 200
VETSAKTREN VDKVFFDLMR EIRSRKTEDS KATSGRAKDR CKKRRLKCTL

L
Length:201
Mass (Da):22,938
Last modified:July 15, 1999 - v2
Checksum:i37F27FD84A813838
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23800 mRNA. Translation: AAC34902.1.
AE014298 Genomic DNA. Translation: AAF45889.1.
AE014298 Genomic DNA. Translation: AAF45890.1.
AY118912 mRNA. Translation: AAM50772.1.
RefSeqiNP_525063.1. NM_080324.4.
NP_726882.1. NM_166986.3.
UniGeneiDm.1689.

Genome annotation databases

EnsemblMetazoaiFBtr0070583; FBpp0070558; FBgn0015286.
FBtr0070584; FBpp0070559; FBgn0015286.
GeneIDi31332.
KEGGidme:Dmel_CG2849.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23800 mRNA. Translation: AAC34902.1.
AE014298 Genomic DNA. Translation: AAF45889.1.
AE014298 Genomic DNA. Translation: AAF45890.1.
AY118912 mRNA. Translation: AAM50772.1.
RefSeqiNP_525063.1. NM_080324.4.
NP_726882.1. NM_166986.3.
UniGeneiDm.1689.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5CM8X-ray2.60B1-201[»]
5CM9X-ray2.60C/D1-201[»]
ProteinModelPortaliP48555.
SMRiP48555. Positions 10-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57853. 18 interactions.
DIPiDIP-19199N.
IntActiP48555. 3 interactions.
STRINGi7227.FBpp0070558.

Proteomic databases

PaxDbiP48555.
PRIDEiP48555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070583; FBpp0070558; FBgn0015286.
FBtr0070584; FBpp0070559; FBgn0015286.
GeneIDi31332.
KEGGidme:Dmel_CG2849.

Organism-specific databases

CTDi5898.
FlyBaseiFBgn0015286. Rala.

Phylogenomic databases

eggNOGiKOG0395. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00780000121849.
InParanoidiP48555.
KOiK07834.
OMAiFAATTEF.
OrthoDBiEOG7QVM41.
PhylomeDBiP48555.

Enzyme and pathway databases

ReactomeiR-DME-1445148. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

GenomeRNAii31332.
PROiP48555.

Gene expression databases

BgeeiP48555.
ExpressionAtlasiP48555. differential.
GenevisibleiP48555. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Winge P., Fleming J.T., Settleman J., Hariharan I.K.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Eye imaginal disk.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "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: Embryo.

Entry informationi

Entry nameiRALA_DROME
AccessioniPrimary (citable) accession number: P48555
Secondary accession number(s): Q540X1, Q9W4Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 15, 1999
Last modified: June 8, 2016
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.