Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00019
Entry Name
UniProt Accession
Theoretical PI
6.66
Molecular Weight
23552.77
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Ral-A
Protein Synonyms/Alias
Gene Name
Rala
Gene Synonyms/Alias
Ral; Ral-a;
Created Date
11-OCT-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
203
Canonical
AKRIRERCCIL****
[1]
S-Palmitoylation
204
Canonical
KRIRERCCIL*****
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Multifunctional 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.
Sequence Annotation
Nucleotide-binding: 21 28 GTP.
Nucleotide-binding: 68 72 GTP.
Nucleotide-binding: 127 130 GTP.
Motif: 43 51 Effector region.
Modified residue: 203 203 Cysteine methyl ester.
Protein Length
206 AA.
Protein Sequence
(Canonical)
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE  60
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV  120
PFLLVGNKSD LEDKRQVSVE EAKNRADQWN VNYVETSAKT RANVDKVFFD LMREIRARKM  180
EDSKEKNGKK KRKSLAKRIR ERCCIL                                       206
FASTA
(Canonical)
>LipidDB-10090-00019|P63321
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGE
EVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENV
PFLLVGNKSDLEDKRQVSVEEAKNRADQWNVNYVETSAKTRANVDKVFFDLMREIRARKM
EDSKEKNGKKKRKSLAKRIRERCCIL
Gene Ontology
GO:0032154; C:cleavage furrow; ISS:UniProtKB
GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome
GO:0030139; C:endocytic vesicle; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005886; C:plasma membrane; ISS:UniProtKB
GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; ISS:UniProtKB
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0031532; P:actin cytoskeleton reorganization; IEA:Ensembl
GO:0000910; P:cytokinesis; ISS:UniProtKB
GO:0006887; P:exocytosis; IEA:UniProtKB-KW
GO:0051665; P:membrane raft localization; IDA:UniProtKB
GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl
GO:0007265; P:Ras protein signal transduction; IEA:InterPro
GO:0017157; P:regulation of exocytosis; IDA:UniProtKB
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR028412; Ral
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00173; RAS;
PROSITE
PROSITE; PS51421; RAS;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;