Ras-related protein Ral-A precursor

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P63321 (RALA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ras-related protein Ral-A

Gene names

Name:	Rala
Synonyms:	Ral, Ral-a

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	206 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	Multifuntional GTPase involved in a variety of cellular processes including gene expression, cell migration, cell proliferation, oncogenic transformation and membrane trafficking. Accomplishes its multiple functions by interacting with distinct downstream effectors. Acts as a GTP sensor for GTP-dependent exocytosis of dense core vesicles. Plays a role in the early stages of cytokinesis and is required to tether the exocyst to the cytokinetic furrow. Key regulator of LPAR1 signaling and competes with ADRBK1 for binding to LPAR1 thus affecting the signaling properties of the receptor. Required for anchorage-independent proliferation of transformed cells By similarity. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. Ref.6
Enzyme regulation	Alternate between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP).
Subunit structure	Interacts with CDC42 By similarity. Interacts with EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites and compete for RALA binding By similarity. Interacts with RALGPS1 By similarity. Interacts with RALBP1 via its effector domain. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in response to LPAR1 activation. RALA and ADRBK1 mutually inhibit each other's binding to LPAR1 By similarity. Ref.5
Subcellular location	Cell surface By similarity. Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Cleavage furrow. Midbody By similarity. Note: Prior to LPA treatment found predominantly at the cell surface and in the presence of LPA co-localizes with LPAR1 and LPAR2 in the endocytic vesicles. During early cytokinesis localizes at the cleavage furrow membrane. Colocalizes with EXOC2 at the early midbody ring and persists there till maturation of the midbody By similarity.
Post-translational modification	Prenylation is essential for membrane localization By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Ras family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Exocytosis
Cellular component	Cell membrane Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB exocytosis Inferred from electronic annotation. Source: UniProtKB-KW membrane raft localization Inferred from direct assay Ref.6. Source: UniProtKB regulation of exocytosis Inferred from direct assay Ref.6. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB midbody Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	Edg-2 lysophosphatidic acid receptor binding Inferred from sequence or structural similarity. Source: UniProtKB GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 203

203

Ras-related protein Ral-A

PRO_0000082694

Propeptide

204 – 206

Removed in mature form By similarity

PRO_0000281345

Regions

Nucleotide binding

21 – 28

GTP By similarity

Nucleotide binding

68 – 72

GTP By similarity

Nucleotide binding

127 – 130

GTP By similarity

Motif

43 – 51

Effector region By similarity

Amino acid modifications

Modified residue

203

Cysteine methyl ester By similarity

Lipidation

203

S-geranylgeranyl cysteine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P63321 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6974341FA08C1874
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FASTA

206

23,553

        10         20         30         40         50         60 
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE 

        70         80         90        100        110        120 
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV 

       130        140        150        160        170        180 
PFLLVGNKSD LEDKRQVSVE EAKNRADQWN VNYVETSAKT RANVDKVFFD LMREIRARKM 

       190        200 
EDSKEKNGKK KRKSLAKRIR ERCCIL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Roger T.T. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Spleen.
[2]	"Tissue-specific expression of GTPas RalA and RalB during embryogenesis and regulation by epithelial-mesenchymal interaction." Zhao Z., Rivkees S.A. Mech. Dev. 97:201-204(2000) [PubMed: 11025226] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 8-16; 28-47; 114-128 AND 167-173, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[5]	"A putative effector of Ral has homology to Rho/Rac GTPase activating proteins." Park S.-H., Weinberg R.A. Oncogene 11:2349-2355(1995) [PubMed: 8570186] [Abstract] Cited for: INTERACTION WITH RALBP1.
[6]	"RalA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling." Balasubramanian N., Meier J.A., Scott D.W., Norambuena A., White M.A., Schwartz M.A. Curr. Biol. 20:75-79(2010) [PubMed: 20005108] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z48587 mRNA. Translation: CAA88488.1. AF244951 mRNA. Translation: AAG23136.1. BC031741 mRNA. Translation: AAH31741.1.
IPI	IPI00124282.
RefSeq	NP_062364.3. NM_019491.5.
UniGene	Mm.27348.
3D structure databases
ProteinModelPortal	P63321.
SMR	P63321. Positions 11-178.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63321. 4 interactions.
STRING	P63321.
PTM databases
PhosphoSite	P63321.
Proteomic databases
PRIDE	P63321.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000009003; ENSMUSP00000009003; ENSMUSG00000008859.
GeneID	56044.
KEGG	mmu:56044.
Organism-specific databases
CTD	5898.
MGI	MGI:1927243. Rala.
Phylogenomic databases
HOGENOM	HBG745225.
HOVERGEN	HBG009351.
InParanoid	P63321.
OMA	SAKRREN.
OrthoDB	EOG4HX524.
PhylomeDB	P63321.
Gene expression databases
ArrayExpress	P63321.
Bgee	P63321.
Genevestigator	P63321.
GermOnline	ENSMUSG00000008859. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR015591. Small_GTPase_Ral. IPR020849. Small_GTPase_Ras. [Graphical view]
KO	K07834.
PANTHER	PTHR24070. PTHR24070. 1 hit. PTHR24070:SF124. PTHR24070:SF124. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00173. RAS. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. Small_GTP. 1 hit.
PROSITE	PS51421. RAS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	311812.
SOURCE	Search...

Entry information

Entry name

RALA_MOUSE

Accession

Primary (citable) accession number: P63321
Secondary accession number(s): P05810

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents