ID   RALA_MOUSE              Reviewed;         206 AA.
AC   P63321; P05810;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   14-DEC-2011, entry version 73.
DE   RecName: Full=Ras-related protein Ral-A;
DE   Flags: Precursor;
GN   Name=Rala; Synonyms=Ral, Ral-a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RA   Roger T.T.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20480378; PubMed=11025226; DOI=10.1016/S0925-4773(00)00427-5;
RA   Zhao Z., Rivkees S.A.;
RT   "Tissue-specific expression of GTPas RalA and RalB during
RT   embryogenesis and regulation by epithelial-mesenchymal interaction.";
RL   Mech. Dev. 97:201-204(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-16; 28-47; 114-128 AND 167-173, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH RALBP1.
RX   MEDLINE=96112637; PubMed=8570186;
RA   Park S.-H., Weinberg R.A.;
RT   "A putative effector of Ral has homology to Rho/Rac GTPase activating
RT   proteins.";
RL   Oncogene 11:2349-2355(1995).
RN   [6]
RP   FUNCTION.
RX   PubMed=20005108; DOI=10.1016/j.cub.2009.11.016;
RA   Balasubramanian N., Meier J.A., Scott D.W., Norambuena A., White M.A.,
RA   Schwartz M.A.;
RT   "RalA-exocyst complex regulates integrin-dependent membrane raft
RT   exocytosis and growth signaling.";
RL   Curr. Biol. 20:75-79(2010).
CC   -!- FUNCTION: Multifuntional GTPase involved in a variety of cellular
CC       processes including gene expression, cell migration, cell
CC       proliferation, oncogenic transformation and membrane trafficking.
CC       Accomplishes its multiple functions by interacting with distinct
CC       downstream effectors. Acts as a GTP sensor for GTP-dependent
CC       exocytosis of dense core vesicles. Plays a role in the early
CC       stages of cytokinesis and is required to tether the exocyst to the
CC       cytokinetic furrow. Key regulator of LPAR1 signaling and competes
CC       with ADRBK1 for binding to LPAR1 thus affecting the signaling
CC       properties of the receptor. Required for anchorage-independent
CC       proliferation of transformed cells (By similarity). The RALA-
CC       exocyst complex regulates integrin-dependent membrane raft
CC       exocytosis and growth signaling.
CC   -!- ENZYME REGULATION: Alternate between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine
CC       nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC       activating protein (GAP).
CC   -!- SUBUNIT: Interacts with CDC42 (By similarity). Interacts with
CC       EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites
CC       and compete for RALA binding (By similarity). Interacts with
CC       RALGPS1 (By similarity). Interacts with RALBP1 via its effector
CC       domain. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in
CC       response to LPAR1 activation. RALA and ADRBK1 mutually inhibit
CC       each other's binding to LPAR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell surface (By similarity). Cell membrane;
CC       Lipid-anchor; Cytoplasmic side (By similarity). Cleavage furrow.
CC       Midbody (By similarity). Note=Prior to LPA treatment found
CC       predominantly at the cell surface and in the presence of LPA co-
CC       localizes with LPAR1 and LPAR2 in the endocytic vesicles. During
CC       early cytokinesis localizes at the cleavage furrow membrane.
CC       Colocalizes with EXOC2 at the early midbody ring and persists
CC       there till maturation of the midbody (By similarity).
CC   -!- PTM: Prenylation is essential for membrane localization (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR   EMBL; Z48587; CAA88488.1; -; mRNA.
DR   EMBL; AF244951; AAG23136.1; -; mRNA.
DR   EMBL; BC031741; AAH31741.1; -; mRNA.
DR   IPI; IPI00124282; -.
DR   RefSeq; NP_062364.3; NM_019491.5.
DR   UniGene; Mm.27348; -.
DR   ProteinModelPortal; P63321; -.
DR   SMR; P63321; 11-178.
DR   IntAct; P63321; 4.
DR   STRING; P63321; -.
DR   PhosphoSite; P63321; -.
DR   PRIDE; P63321; -.
DR   Ensembl; ENSMUST00000009003; ENSMUSP00000009003; ENSMUSG00000008859.
DR   GeneID; 56044; -.
DR   KEGG; mmu:56044; -.
DR   CTD; 5898; -.
DR   MGI; MGI:1927243; Rala.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P63321; -.
DR   OMA; SAKRREN; -.
DR   OrthoDB; EOG4HX524; -.
DR   PhylomeDB; P63321; -.
DR   NextBio; 311812; -.
DR   ArrayExpress; P63321; -.
DR   Bgee; P63321; -.
DR   Genevestigator; P63321; -.
DR   GermOnline; ENSMUSG00000008859; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0051665; P:membrane raft localization; IDA:UniProtKB.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR015591; Small_GTPase_Ral.
DR   InterPro; IPR020849; Small_GTPase_Ras.
DR   KO; K07834; -.
DR   PANTHER; PTHR24070; PTHR24070; 1.
DR   PANTHER; PTHR24070:SF124; PTHR24070:SF124; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Exocytosis; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Reference proteome.
FT   CHAIN         1    203       Ras-related protein Ral-A.
FT                                /FTId=PRO_0000082694.
FT   PROPEP      204    206       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281345.
FT   NP_BIND      21     28       GTP (By similarity).
FT   NP_BIND      68     72       GTP (By similarity).
FT   NP_BIND     127    130       GTP (By similarity).
FT   MOTIF        43     51       Effector region (By similarity).
FT   MOD_RES     203    203       Cysteine methyl ester (By similarity).
FT   LIPID       203    203       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   206 AA;  23553 MW;  6974341FA08C1874 CRC64;
     MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
     EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV
     PFLLVGNKSD LEDKRQVSVE EAKNRADQWN VNYVETSAKT RANVDKVFFD LMREIRARKM
     EDSKEKNGKK KRKSLAKRIR ERCCIL
//