[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Spleen; Roger T.T.; Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0925-4773(00)00427-5; PubMed=11025226 [NCBI, ExPASy, EBI, Israel, Japan] Zhao Z., Rivkees S.A.; "Tissue-specific expression of GTPas RalA and RalB during embryogenesis and regulation by epithelial-mesenchymal interaction."; Mech. Dev. 97:201-204(2000).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Eye; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	PROTEIN SEQUENCE OF 8-16; 28-47; 114-128 AND 167-173, AND MASS SPECTROMETRY. STRAIN=C57BL/6; TISSUE=Brain; Lubec G., Kang S.U.; Submitted (APR-2007) to UniProtKB.
[5]	INTERACTION WITH RALBP1. PubMed=8570186 [NCBI, ExPASy, EBI, Israel, Japan] Park S.-H., Weinberg R.A.; "A putative effector of Ral has homology to Rho/Rac GTPase activating proteins."; Oncogene 11:2349-2355(1995).

Comments

SUBUNIT: 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.
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side (Potential).
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

Z48587; CAA88488.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF244951; AAG23136.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC031741; AAH31741.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00124282; -.

NP_062364.3; -.

3D structure databases

HSSP

P11233; 1UAD. [HSSP ENTRY / PDB]

P63321; 11-183.

PTM databases

P63321; -.

Organism-specific databases

MGI

MGI:1927243; Rala.

Gene expression databases

ArrayExpress

P63321; -.

Bgee

P63321; -.

GermOnline

ENSMUSG00000008859; Mus musculus.

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 (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
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

P63321; -.

Genome annotation databases

Ensembl

ENSMUSG00000008859; Mus musculus. [Contig view]

GeneID

56044; -.

KEGG

mmu:56044; -.

Phylogenomic databases

HOGENOM

P63321; -.

HOVERGEN

P63321; -.

OMA

P63321; AKPKGQN.

Other

311812; -.

Rala; Mus musculus.

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

Keywords

Cell membrane; Direct protein sequencing; 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_0000082694`
`PROPEP`	`204 206`	`3`	`Removed in mature form (By similarity).`	`PRO_0000281345`
`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).`

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

P63321 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