ID   RAD_RAT                 Reviewed;         306 AA.
AC   P55043;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=GTP-binding protein RAD;
DE   AltName: Full=RAD1;
DE   AltName: Full=Ras associated with diabetes;
GN   Name=Rrad; Synonyms=Rad;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RA   Rishi A.K., Gulamhussein A., Steele M.P.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play an important role in cardiac antiarrhythmia via the
CC       strong suppression of voltage-gated L-type Ca(2+) currents. Regulates
CC       voltage-dependent L-type calcium channel subunit alpha-1C trafficking
CC       to the cell membrane. Inhibits cardiac hypertrophy through the
CC       calmodulin-dependent kinase II (CaMKII) pathway. Inhibits
CC       phosphorylation and activation of CAMK2D (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with Calmodulin preferentially to the inactive, GDP-
CC       form. Interacts with CAMK2D and CACNB2. Interaction with CACNB2
CC       regulates the trafficking of CACNA1C to the cell membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA56719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U12187; AAA56719.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; P55043; -.
DR   SMR; P55043; -.
DR   STRING; 10116.ENSRNOP00000016259; -.
DR   PaxDb; P55043; -.
DR   PRIDE; P55043; -.
DR   UCSC; RGD:69357; rat.
DR   RGD; 69357; Rrad.
DR   eggNOG; KOG0395; Eukaryota.
DR   InParanoid; P55043; -.
DR   PhylomeDB; P55043; -.
DR   PRO; PR:P55043; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
DR   GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR028869; RAD.
DR   InterPro; IPR017358; RGK.
DR   InterPro; IPR001806; Small_GTPase.
DR   PANTHER; PTHR45775:SF3; PTHR45775:SF3; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PIRSF; PIRSF038017; GTP-binding_GEM; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell membrane; GTP-binding; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..306
FT                   /note="GTP-binding protein RAD"
FT                   /id="PRO_0000122480"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..295
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        57..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         97..104
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         23
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O88667"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88667"
SQ   SEQUENCE   306 AA;  33038 MW;  1A900FDD4C23C453 CRC64;
     MTLNGGSGAG GSRSAGRERD RRRGSTPWGP APPLHRRSMP VDERDLQAAL TPGSLAATAA
     GTRTQGQRLD WPEGSSDSLS SGDSGSEDGV YKVHAAGAPG VGKSALARIF GGVEDGPEAE
     AAGHTYDRSI TVDGEEASLM VYDIWEQDGG CWLPGHCMAM GDAYVIVYSI TDKGSFEKAS
     ELRVQLRARR QTDVPIILVG NKSDLVRSRE VSVDEGRACA EVFDCKFIET SAALHHNVQA
     LFEGVVRQIR LRRDSKEDNA RRQAGTRRRE SLGKKAKLFL GRIVARNSRK MAFLAKSKSC
     HDLSVL