P63320 (RALA_SAGOE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Ral-A

Gene names

Name:	RALA
Synonyms:	RAL

Organism

Saguinus oedipus (Cotton-top tamarin)

Taxonomic identifier

9490 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Callitrichinae › Saguinus

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 RALBP1 via its effector domain and with CDC42. Interacts with EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites and compete for RALA binding Interacts with RALGPS1. 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.
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	3D-structure
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 Inferred from direct assay Ref.2. Source: UniProtKB 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_0000082696

Propeptide

204 – 206

3

Removed in mature form By similarity

PRO_0000281347

Regions

Nucleotide binding

21 – 29

9

GTP

Nucleotide binding

127 – 130

4

GTP

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

Secondary structure

1

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206

Helix Strand Turn

Details...

Beta strand

14 – 20

7

Helix

27 – 36

10

Beta strand

51 – 57

7

Beta strand

60 – 68

9

Beta strand

87 – 94

8

Helix

98 – 102

5

Helix

104 – 115

12

Beta strand

122 – 127

6

Helix

129 – 134

6

Helix

139 – 149

11

Beta strand

153 – 155

3

Turn

158 – 160

3

Helix

164 – 176

13

Sequences

	Sequence		Length	Mass (Da)
	P63320 [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]	"The ral gene: a new ras related gene isolated by the use of a synthetic probe." Chardin P., Tavitian A. EMBO J. 5:2203-2208(1986) [PubMed: 3023062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[2]	"Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap." Nicely N.I., Kosak J., de Serrano V., Mattos C. Structure 12:2025-2036(2004) [PubMed: 15530367] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 11-178 IN COMPLEX WITH GTP ANALOG.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04328 mRNA. Translation: CAA27859.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U8Y	X-ray	1.55	A/B	11-178	[»]
1U8Z	X-ray	1.50	A/B	11-178	[»]
1U90	X-ray	2.00	A/B	11-178	[»]

ProteinModelPortal

P63320.

SMR

P63320. Positions 11-178.

ModBase

Search...

Proteomic databases

PRIDE

P63320.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG009351.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR015591. Small_GTPase_Ral.
IPR020849. Small_GTPase_Ras.
[Graphical view]

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...

Entry information

Entry name

RALA_SAGOE

Accession

Primary (citable) accession number: P63320
Secondary accession number(s): P05810

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	October 19, 2011
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program