REM2_RAT
ID REM2_RAT Reviewed; 341 AA.
AC Q9WTY2; Q5D202;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=GTP-binding protein REM 2;
DE AltName: Full=Rad and Gem-like GTP-binding protein 2;
GN Name=Rem2;
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 STRAIN=Brown Norway; TISSUE=Spinal ganglion;
RX PubMed=16237180; DOI=10.1523/jneurosci.3111-05.2005;
RA Chen H., Puhl H.L., Niu S.L., Mitchell D.C., Ikeda S.R.;
RT "Expression of Rem2, an RGK family small GTPase, reduces N-type calcium
RT current without affecting channel surface density.";
RL J. Neurosci. 25:9762-9772(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-341, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND GTP-BINDING.
RC TISSUE=Brain;
RX PubMed=10727423; DOI=10.1042/bj3470223;
RA Finlin B.S., Shao H., Kadono-Okuda K., Guo N., Andres D.A.;
RT "Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases.";
RL Biochem. J. 347:223-231(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-296, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Binds GTP saturably and exhibits a low intrinsic rate of GTP
CC hydrolysis. {ECO:0000269|PubMed:10727423}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10727423}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney.
CC {ECO:0000269|PubMed:10727423}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34238.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY916790; AAX13958.1; -; mRNA.
DR EMBL; AF084464; AAD34238.1; ALT_FRAME; mRNA.
DR RefSeq; NP_073176.2; NM_022685.2.
DR PDB; 4AII; X-ray; 2.66 A; A/B=113-283.
DR PDBsum; 4AII; -.
DR AlphaFoldDB; Q9WTY2; -.
DR SMR; Q9WTY2; -.
DR BioGRID; 249164; 1.
DR STRING; 10116.ENSRNOP00000016020; -.
DR iPTMnet; Q9WTY2; -.
DR PhosphoSitePlus; Q9WTY2; -.
DR PaxDb; Q9WTY2; -.
DR PRIDE; Q9WTY2; -.
DR ABCD; Q9WTY2; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000016020; ENSRNOP00000016020; ENSRNOG00000011646.
DR GeneID; 64626; -.
DR KEGG; rno:64626; -.
DR UCSC; RGD:69081; rat.
DR CTD; 161253; -.
DR RGD; 69081; Rem2.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160062; -.
DR HOGENOM; CLU_041217_3_1_1; -.
DR InParanoid; Q9WTY2; -.
DR OMA; DIWEQMQ; -.
DR OrthoDB; 679855at2759; -.
DR PhylomeDB; Q9WTY2; -.
DR TreeFam; TF314379; -.
DR PRO; PR:Q9WTY2; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000011646; Expressed in Ammon's horn and 10 other tissues.
DR Genevisible; Q9WTY2; RN.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IDA:RGD.
DR DisProt; DP02429; -.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; GTP-binding; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..341
FT /note="GTP-binding protein REM 2"
FT /id="PRO_0000122485"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT BINDING 230..233
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT BINDING 261..262
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8IYK8"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:4AII"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:4AII"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:4AII"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:4AII"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:4AII"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:4AII"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:4AII"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:4AII"
SQ SEQUENCE 341 AA; 37275 MW; 4CABA88C1925B97B CRC64;
MHTDLDTDMD ADTETVALCS SSSRQASPSG TPTPEADTTL LKQKPEKLLA ELDRGGPPPA
PGVPRRRGSM PVPYKHQLRR AQAVDELDWP PQASSSGSSD SLGSGEAALA QKDGVFKVML
LGESGVGKST LAGTFGGLQG DNAHEMENSE DTYERRIMVD KEEVTLIVYD IWEQGDAGGW
LQDHCLQTGD AFLIVFSVTD RRSFSKVPET LLRLRAGRPH HDLPVILVGN KSDLARSREV
SLEEGRHLAG TLSCKHIETS AALHHNTREL FEGAVRQIRL RRGRGHAGGQ RPEPSSPDGP
APPTRRESLT KKAKRFLANL VPRNAKFFKQ RSRSCHDLSV L
