ID   RALA_RAT                Reviewed;         206 AA.
AC   P63322; 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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=93326173; PubMed=7687439; DOI=10.1006/bbrc.1993.1855;
RA   Wildey G.M., Viggeswarapu M., Rim S., Denker J.K.;
RT   "Isolation of cDNA clones and tissue expression of rat ral A and ral B
RT   GTP-binding proteins.";
RL   Biochem. Biophys. Res. Commun. 194:552-559(1993).
RN   [2]
RP   INTERACTION WITH RALBP1 AND CDC42, AND MUTAGENESIS OF ASP-49.
RX   MEDLINE=95349625; PubMed=7623849;
RA   Cantor S.B., Urano T., Feig L.A.;
RT   "Identification and characterization of Ral-binding protein 1, a
RT   potential downstream target of Ral GTPases.";
RL   Mol. Cell. Biol. 15:4578-4584(1995).
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. The RALA-exocyst complex regulates integrin-
CC       dependent membrane raft exocytosis and growth signaling. Key
CC       regulator of LPAR1 signaling and competes with ADRBK1 for binding
CC       to LPAR1 thus affecting the signaling properties of the receptor.
CC       Required for anchorage-independent proliferation of transformed
CC       cells (By similarity).
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 EXOC8 and EXOC2. EXOC2 and EXOC8 have
CC       overlapping binding sites and compete for RALA binding (By
CC       similarity). Interacts with RALGPS1 (By similarity). Interacts
CC       with RALBP1 via its effector domain and with CDC42. Interacts with
CC       LPAR1 and LPAR2. Interacts with ADRBK1 in response to LPAR1
CC       activation. RALA and ADRBK1 mutually inhibit each other's binding
CC       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   -!- TISSUE SPECIFICITY: Higher levels where found in testes followed
CC       by brain, adrenal gland, pituitary gland, ovary, liver and kidney.
CC       Low expression was found in muscle.
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; L19698; AAA42003.1; -; mRNA.
DR   IPI; IPI00203575; -.
DR   PIR; JN0622; JN0622.
DR   RefSeq; NP_112355.1; NM_031093.2.
DR   UniGene; Rn.100380; -.
DR   ProteinModelPortal; P63322; -.
DR   SMR; P63322; 11-178.
DR   IntAct; P63322; 1.
DR   STRING; P63322; -.
DR   PRIDE; P63322; -.
DR   Ensembl; ENSRNOT00000018190; ENSRNOP00000018190; ENSRNOG00000013454.
DR   GeneID; 81757; -.
DR   KEGG; rno:81757; -.
DR   UCSC; NM_031093; rat.
DR   CTD; 5898; -.
DR   RGD; 619851; Rala.
DR   eggNOG; roNOG09209; -.
DR   GeneTree; ENSGT00560000076901; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P63322; -.
DR   OMA; SAKRREN; -.
DR   OrthoDB; EOG4HX524; -.
DR   PhylomeDB; P63322; -.
DR   NextBio; 615530; -.
DR   ArrayExpress; P63322; -.
DR   Genevestigator; P63322; -.
DR   GermOnline; ENSRNOG00000013454; Rattus norvegicus.
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; NAS:RGD.
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; ISS:UniProtKB.
DR   GO; GO:0017157; P:regulation of exocytosis; ISS: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   Exocytosis; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN         1    203       Ras-related protein Ral-A.
FT                                /FTId=PRO_0000082695.
FT   PROPEP      204    206       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281346.
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).
FT   MUTAGEN      49     49       D->N: Loss of RALBP1 binding.
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
//