GEM_MOUSE
ID GEM_MOUSE Reviewed; 295 AA.
AC P55041; Q8JZS1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=GTP-binding protein GEM;
DE AltName: Full=GTP-binding mitogen-induced T-cell protein;
DE AltName: Full=RAS-like protein KIR;
GN Name=Gem; Synonyms=Kir;
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].
RX PubMed=7912851; DOI=10.1126/science.7912851;
RA Maguire J., Santoro T., Jensen P., Siebenlist U., Yewdell J., Kelly K.;
RT "Gem: an induced, immediate early protein belonging to the Ras family.";
RL Science 265:241-244(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7809057; DOI=10.1073/pnas.91.26.12448;
RA Cohen L., Mohr R., Chen Y.-Y., Huang M., Kato R., Dorin D., Tamanoi F.,
RA Goga A., Afar D., Rosenberg N., Witte O.;
RT "Transcriptional activation of a ras-like gene (kir) by oncogenic tyrosine
RT kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12448-12452(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH CALMODULIN, AND MUTAGENESIS OF TRP-269.
RX PubMed=8810259; DOI=10.1074/jbc.271.41.25067;
RA Fischer R., Wei Y., Anagli J., Berchtold M.W.;
RT "Calmodulin binds to and inhibits GTP binding of the ras-like GTPase
RT Kir/Gem.";
RL J. Biol. Chem. 271:25067-25070(1996).
CC -!- FUNCTION: Could be a regulatory protein, possibly participating in
CC receptor-mediated signal transduction at the plasma membrane. Has
CC guanine nucleotide-binding activity but undetectable intrinsic GTPase
CC activity.
CC -!- SUBUNIT: Interacts with calmodulin in a Ca(2+)-dependent manner.
CC Calmodulin binding significantly decreases GTP binding. Binds ROCK1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P55041; P31946: YWHAB; Xeno; NbExp=3; IntAct=EBI-7082069, EBI-359815;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side.
CC -!- INDUCTION: By mitogens.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC {ECO:0000305}.
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DR EMBL; U10551; AAA64912.1; -; mRNA.
DR EMBL; U13053; AAC52145.1; -; mRNA.
DR EMBL; BC029668; AAH29668.1; -; mRNA.
DR CCDS; CCDS17971.1; -.
DR PIR; B54575; B54575.
DR PIR; I49117; I49117.
DR RefSeq; NP_034406.2; NM_010276.4.
DR AlphaFoldDB; P55041; -.
DR SMR; P55041; -.
DR BioGRID; 199898; 1.
DR IntAct; P55041; 2.
DR MINT; P55041; -.
DR STRING; 10090.ENSMUSP00000103939; -.
DR iPTMnet; P55041; -.
DR PhosphoSitePlus; P55041; -.
DR EPD; P55041; -.
DR jPOST; P55041; -.
DR PaxDb; P55041; -.
DR PeptideAtlas; P55041; -.
DR PRIDE; P55041; -.
DR ProteomicsDB; 268863; -.
DR Antibodypedia; 12852; 178 antibodies from 34 providers.
DR DNASU; 14579; -.
DR Ensembl; ENSMUST00000029868; ENSMUSP00000029868; ENSMUSG00000028214.
DR Ensembl; ENSMUST00000108304; ENSMUSP00000103939; ENSMUSG00000028214.
DR GeneID; 14579; -.
DR KEGG; mmu:14579; -.
DR UCSC; uc008rzv.2; mouse.
DR CTD; 2669; -.
DR MGI; MGI:99844; Gem.
DR VEuPathDB; HostDB:ENSMUSG00000028214; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000157830; -.
DR HOGENOM; CLU_041217_3_2_1; -.
DR InParanoid; P55041; -.
DR OMA; SNEYNPQ; -.
DR OrthoDB; 679855at2759; -.
DR PhylomeDB; P55041; -.
DR TreeFam; TF314379; -.
DR BioGRID-ORCS; 14579; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Gem; mouse.
DR PRO; PR:P55041; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P55041; protein.
DR Bgee; ENSMUSG00000028214; Expressed in ascending aorta and 154 other tissues.
DR ExpressionAtlas; P55041; baseline and differential.
DR Genevisible; P55041; MM.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; ISO:MGI.
DR GO; GO:0051310; P:metaphase plate congression; ISO:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
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 Cell membrane; GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..295
FT /note="GTP-binding protein GEM"
FT /id="PRO_0000122476"
FT REGION 39..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..284
FT /note="Calmodulin-binding"
FT COMPBIAS 39..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 269
FT /note="W->G: No calmodulin binding."
FT /evidence="ECO:0000269|PubMed:8810259"
FT CONFLICT 23
FT /note="I -> M (in Ref. 1; AAA64912)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> T (in Ref. 1; AAA64912)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="V -> E (in Ref. 1; AAA64912)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="R -> P (in Ref. 1; AAA64912)"
FT /evidence="ECO:0000305"
FT CONFLICT 282..284
FT /note="FKL -> SSS (in Ref. 1; AAA64912)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="V -> W (in Ref. 2; AAC52145)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33725 MW; 4618F225D4FAAFA5 CRC64;
MTLNNVTMRQ GTVGMQPQQR WSIPADARHL MVQKDPHPCN LRNRHSTAPE EHCRRSWSSD
STDSVISSES GNTYYRVVLI GEQGVGKSTL ANIFAGVHDS MDSDCEVLGE DTYERTLVVD
GESATIILLD MWENKGENEW LHDHCMQVGD AYLIVYSITD RASFEKASEL RIQLRRARQT
EDIPIILVGN KSDLVRCREV SVSEGRACAV VFDCKFIETS AAVQHNVKEL FEGIVRQVRL
RRDSKEKNER RLAYQKRRES IPRKARRFWG KIVAKNNKNM AFKLKSKSCH DLSVL
