[1]	NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. DOI=10.1006/bbrc.1993.1855; PubMed=7687439 [NCBI, ExPASy, EBI, Israel, Japan] Wildey G.M., Viggeswarapu M., Rim S., Denker J.K.; "Isolation of cDNA clones and tissue expression of rat ral A and ral B GTP-binding proteins."; Biochem. Biophys. Res. Commun. 194:552-559(1993).
[2]	INTERACTION WITH RALBP1 AND CDC42, AND MUTAGENESIS OF ASP-49. PubMed=7623849 [NCBI, ExPASy, EBI, Israel, Japan] Cantor S.B., Urano T., Feig L.A.; "Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases."; Mol. Cell. Biol. 15:4578-4584(1995).

Comments

SUBUNIT: 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.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential).
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.
SIMILARITY: Belongs to the small GTPase superfamily. Ras family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L19698; AAA42003.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00203575; -.

JN0622; JN0622.

NP_112355.1; -.

3D structure databases

HSSP

P11233; 1UAD. [HSSP ENTRY / PDB]

SMR

P63322; 11-183.

ModBase

P63322.

Organism-specific databases

RGD

619851; Rala.

Gene expression databases

ArrayExpress

P63322; -.

GermOnline

ENSRNOG00000013454; Rattus norvegicus.

Ontologies

GO:0005622;	Cellular component: intracellular (inferred from electronic annotation from InterPro).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005525;	Molecular function: GTP binding (non-traceable author statement from RGD).
GO:0007264;	Biological process: small GTPase mediated signal transduction (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR003577; GTPase_Ras.
IPR013753; Ras.
IPR001806; Ras_GTPase.
IPR015591; Ras_Ral_related.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.

PANTHER

PTHR11708:SF124; Ras_Ral_related; 1.

Pfam

PF00071; Ras; 1.
Pfam graphical view of domain structure.

PRINTS

PR00449; RASTRNSFRMNG.

SMART

SM00173; RAS; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00231; small_GTP; 1.

PROSITE

PS51421; RAS; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P63322; -.

Genome annotation databases

Ensembl

ENSRNOG00000013454; Rattus norvegicus. [Contig view]

GeneID

81757; -.

KEGG

rno:81757; -.

Phylogenomic databases

HOVERGEN

P63322; -.

OMA

P63322; AKPKGQN.

Other

615530; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 203`	`203`	`Ras-related protein Ral-A.`	`PRO_0000082695`
`PROPEP`	`204 206`	`3`	`Removed in mature form (By similarity).`	`PRO_0000281346`
`NP_BIND`	`21 28`	`8`	`GTP (By similarity).`
`NP_BIND`	`68 72`	`5`	`GTP (By similarity).`
`NP_BIND`	`127 130`	`4`	`GTP (By similarity).`
`MOTIF`	`43 51`	`9`	`Effector region (By similarity).`
`MOD_RES`	`203 203`		`Cysteine methyl ester (By similarity).`
`LIPID`	`203 203`		`S-geranylgeranyl cysteine (By similarity).`
`MUTAGEN`	`49 49`		`D->N: Loss of RALBP1 binding.`

Sequence information

Length: 206 AA [This is the length of the unprocessed precursor]

Molecular weight: 23553 Da [This is the MW of the unprocessed precursor]

CRC64: 6974341FA08C1874 [This is a checksum on the sequence]

        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

P63322 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools