REM1_MOUSE
ID REM1_MOUSE Reviewed; 297 AA.
AC O35929;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=GTP-binding protein REM 1;
DE AltName: Full=Rad and Gem-like GTP-binding protein 1;
GN Name=Rem1; Synonyms=Rem;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9268335; DOI=10.1074/jbc.272.35.21982;
RA Finlin B.S., Andres D.A.;
RT "Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding
RT protein family repressed by lipopolysaccharide stimulation.";
RL J. Biol. Chem. 272:21982-21988(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=10441394; DOI=10.1006/abbi.1999.1316;
RA Finlin B.S., Andres D.A.;
RT "Phosphorylation-dependent association of the Ras-related GTP-binding
RT protein Rem with 14-3-3 proteins.";
RL Arch. Biochem. Biophys. 368:401-412(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Promotes endothelial cell sprouting and actin cytoskeletal
CC reorganization (By similarity). May be involved in angiogenesis. May
CC function in Ca(2+) signaling. {ECO:0000250}.
CC -!- SUBUNIT: In vitro, interacts with calmodulin in a calcium-dependent
CC manner (By similarity). Interacts 14-3-3 family members including
CC YWHAE, YWHAH, YWHAQ, YWHAZ in a phosphorylation-dependent manner.
CC {ECO:0000250, ECO:0000269|PubMed:10441394}.
CC -!- TISSUE SPECIFICITY: High expression in cardiac muscle. Moderate
CC expression in lung, skeletal muscle and kidney. Low levels in spleen
CC and brain.
CC -!- INDUCTION: Repressed by lipopolysaccharide stimulation.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC {ECO:0000305}.
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DR EMBL; U91601; AAB71639.1; -; mRNA.
DR EMBL; AK053133; BAC35274.1; -; mRNA.
DR EMBL; AK084460; BAC39190.1; -; mRNA.
DR CCDS; CCDS16895.1; -.
DR RefSeq; NP_033073.1; NM_009047.5.
DR AlphaFoldDB; O35929; -.
DR SMR; O35929; -.
DR MINT; O35929; -.
DR STRING; 10090.ENSMUSP00000000369; -.
DR iPTMnet; O35929; -.
DR PhosphoSitePlus; O35929; -.
DR MaxQB; O35929; -.
DR PaxDb; O35929; -.
DR PRIDE; O35929; -.
DR ProteomicsDB; 253112; -.
DR Antibodypedia; 10156; 108 antibodies from 27 providers.
DR DNASU; 19700; -.
DR Ensembl; ENSMUST00000000369; ENSMUSP00000000369; ENSMUSG00000000359.
DR GeneID; 19700; -.
DR KEGG; mmu:19700; -.
DR UCSC; uc008nfw.1; mouse.
DR CTD; 28954; -.
DR MGI; MGI:1097696; Rem1.
DR VEuPathDB; HostDB:ENSMUSG00000000359; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000160613; -.
DR HOGENOM; CLU_041217_3_2_1; -.
DR InParanoid; O35929; -.
DR OMA; HIGEDTY; -.
DR OrthoDB; 679855at2759; -.
DR PhylomeDB; O35929; -.
DR TreeFam; TF314379; -.
DR BioGRID-ORCS; 19700; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Rem1; mouse.
DR PRO; PR:O35929; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O35929; protein.
DR Bgee; ENSMUSG00000000359; Expressed in renal cortex interstitium and 87 other tissues.
DR ExpressionAtlas; O35929; baseline and differential.
DR Genevisible; O35929; MM.
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: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: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; IPR017358; RGK.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR PIRSF; PIRSF038017; GTP-binding_GEM; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..297
FT /note="GTP-binding protein REM 1"
FT /id="PRO_0000122482"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..286
FT /note="Calmodulin-binding"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 194..197
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 297 AA; 32909 MW; 4DCFFC50132C8262 CRC64;
MTLNTQQEAK TTLRRRASTP LPLSSRGHQP GRLCTAPSAP SQHPRLGQSV SLNPPVRKPS
PAQDGWSSES SDSEGSWEAL YRVVLLGDPG VGKTSLASLF AEKQDRDPHE QLGGVYERTL
SVDGEDTTLV VMDTWEAEKL DESWCQESCL QAGSAYVIVY SIADRSSFES ASELRIQLRR
THQANHVPII LVGNKADLAR CREVSVEEGR ACAVVFDCKF IETSATLQHN VTELFEGVVR
QLRLRRQDNA APETPSPRRR ASLGQRARRF LARLTARSAR RRALKARSKS CHNLAVL
