Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00522
Entry Name
UniProt Accession
Theoretical PI
6.66
Molecular Weight
23566.79
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein Ral-A
Protein Synonyms/Alias
Gene Name
RALA
Gene Synonyms/Alias
RAL;
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
203
Canonical
AKRIRERCCIL****
[2][3]
S-Geranylgeranylation
204
Canonical
KRIRERCCIL*****
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
[2] Kinsella BT, Erdman RA, Maltese WA. Carboxyl-terminal isoprenylation ofras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem.1991 May 25;266(15):9786-94.[PMID:1903399]
[3] Falsetti SC, Wang DA, Peng H, Carrico D, Cox AD, Der CJ, Hamilton AD, SebtiSM. Geranylgeranyltransferase I inhibitors target RalB to inhibitanchorage-dependent growth and induce apoptosis and RalA to inhibitanchorage-independent growth. Mol Cell Biol. 2007 Nov;27(22):8003-14. Epub 2007Sep 17.[PMID:17875936]
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. 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.
Sequence Annotation
Nucleotide-binding: 24 29 GTP.
Nucleotide-binding: 40 46 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 EAKNRAEQWN VNYVETSAKT RANVDKVFFD LMREIRARKM  180
EDSKEKNGKK KRKSLAKRIR ERCCIL                                       206
MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE  60
EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV  120
PFLLVGNKSD LEDKRQVSVE EAKNRAEQWN VNYVETSAKT RANVDKVFFD LMREIRARKM  180
EDSKEKNGKK KRKSLAKRIR ERCCIL                                       206
FASTA
(Canonical)
>LipidDB-9606-00522|P11233
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGE
EVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENV
PFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKM
EDSKEKNGKKKRKSLAKRIRERCCIL
MAANKPKGQNSLALHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGE
EVQIDILDTAGQEDYAAIRDNYFRSGEGFLCVFSITEMESFAATADFREQILRVKEDENV
PFLLVGNKSDLEDKRQVSVEEAKNRAEQWNVNYVETSAKTRANVDKVFFDLMREIRARKM
EDSKEKNGKKKRKSLAKRIRERCCIL
Gene Ontology
GO:0009986; C:cell surface; IDA:UniProtKB
GO:0032154; C:cleavage furrow; IDA:UniProtKB
GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; IDA:UniProtKB
GO:0005525; F:GTP binding; TAS:ProtInc
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0031532; P:actin cytoskeleton reorganization; IDA:BHF-UCL
GO:0006935; P:chemotaxis; TAS:ProtInc
GO:0000910; P:cytokinesis; IDA:UniProtKB
GO:0006887; P:exocytosis; IEA:UniProtKB-KW
GO:0061024; P:membrane organization; TAS:Reactome
GO:0051665; P:membrane raft localization; IDA:UniProtKB
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome
GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL
GO:0007265; P:Ras protein signal transduction; TAS:Reactome
GO:0017157; P:regulation of exocytosis; IDA:UniProtKB
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0016032; P:viral process; IEA:UniProtKB-KW
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;