ID   GEM_PONAB               Reviewed;         296 AA.
AC   Q5R541;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=GTP-binding protein GEM;
GN   Name=GEM;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with calmodulin in a Ca(2+)-dependent manner. Binds
CC       ROCK1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC       {ECO:0000305}.
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DR   EMBL; CR861033; CAH93125.1; -; mRNA.
DR   RefSeq; NP_001126848.1; NM_001133376.1.
DR   AlphaFoldDB; Q5R541; -.
DR   SMR; Q5R541; -.
DR   STRING; 9601.ENSPPYP00000021031; -.
DR   GeneID; 100173856; -.
DR   KEGG; pon:100173856; -.
DR   CTD; 2669; -.
DR   eggNOG; KOG0395; Eukaryota.
DR   InParanoid; Q5R541; -.
DR   OrthoDB; 679855at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell membrane; GTP-binding; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..296
FT                   /note="GTP-binding protein GEM"
FT                   /id="PRO_0000122477"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          266..285
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        37..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         82..89
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         191..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   296 AA;  33980 MW;  A3FE2B7DEC79768F CRC64;
     MTLNNVTMRQ GTVGMQPQQQ RWSIPADGRH LMVQKEPHQY SHRNRHSATP EDHCRRSWSS
     DSTDSVISSE SGNTYYRVVL IGEQGVGKST LANIFAGVHD SMDSDCEVLG EDTYERTLMV
     DGESATIILL DMWENKGENE WLHDHCMQVG DAYLIVYSIT DRASFEKASE LRIQLRRARQ
     TEDIPIILVG NKSDLVRCRE VSVSEGRTCA VVFDCKFIET SAAVQHNVKE LFEGIVRQVR
     LRRDSKEKNE RRLAYQKRKE SMPRKARRFW GKIVAKNNKN MAFKLKSKSC HDLSVL