P63322 (RALA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Ral-A

Gene names

Name:	Rala
Synonyms:	Ral, Ral-a

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

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. The RALA-exocyst complex regulates integrin-dependent membrane raft exocytosis and growth signaling. 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.
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 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 and with CDC42. 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.2
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.
Tissue specificity	Higher levels where found in testes followed by brain, adrenal gland, pituitary gland, ovary, liver and kidney. Low expression was found in muscle. Ref.1
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 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 sequence or structural similarity. Source: UniProtKB regulation of exocytosis Inferred from sequence or structural similarity. 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 Non-traceable author statement Ref.1. Source: RGD 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_0000082695
	Propeptide	204 – 206	3	Removed in mature form By similarity		PRO_0000281346
Regions
	Nucleotide binding	21 – 28	8	GTP By similarity
	Nucleotide binding	68 – 72	5	GTP By similarity
	Nucleotide binding	127 – 130	4	GTP By similarity
	Motif	43 – 51	9	Effector region By similarity
Amino acid modifications
	Modified residue	203	1	Cysteine methyl ester By similarity
	Lipidation	203	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Mutagenesis	49	1	D → N: Loss of RALBP1 binding. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P63322 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 6974341FA08C1874	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

References

[1]	"Isolation of cDNA clones and tissue expression of rat ral A and ral B GTP-binding proteins." Wildey G.M., Viggeswarapu M., Rim S., Denker J.K. Biochem. Biophys. Res. Commun. 194:552-559(1993) [PubMed: 7687439] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases." Cantor S.B., Urano T., Feig L.A. Mol. Cell. Biol. 15:4578-4584(1995) [PubMed: 7623849] [Abstract] Cited for: INTERACTION WITH RALBP1 AND CDC42, MUTAGENESIS OF ASP-49.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19698 mRNA. Translation: AAA42003.1.
IPI	IPI00203575.
PIR	JN0622.
RefSeq	NP_112355.1. NM_031093.2.
UniGene	Rn.100380.
3D structure databases
ProteinModelPortal	P63322.
SMR	P63322. Positions 11-178.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63322. 1 interaction.
STRING	P63322.
Proteomic databases
PRIDE	P63322.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000018190; ENSRNOP00000018190; ENSRNOG00000013454.
GeneID	81757.
KEGG	rno:81757.
UCSC	NM_031093. rat.
Organism-specific databases
CTD	5898.
RGD	619851. Rala.
Phylogenomic databases
eggNOG	roNOG09209.
GeneTree	ENSGT00560000076901.
HOVERGEN	HBG009351.
InParanoid	P63322.
OMA	SAKRREN.
OrthoDB	EOG4HX524.
PhylomeDB	P63322.
Gene expression databases
ArrayExpress	P63322.
Genevestigator	P63322.
GermOnline	ENSRNOG00000013454. Rattus norvegicus.
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	615530.

Entry information

Entry name

RALA_RAT

Accession

Primary (citable) accession number: P63322
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