ID   GNA11_CANLF             Reviewed;         198 AA.
AC   P52206;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-11;
DE            Short=G alpha-11;
DE            Short=G-protein subunit alpha-11;
DE   Flags: Fragment;
GN   Name=GNA11;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8836152; DOI=10.1042/bj3181023;
RA   Johnson G.J., Leis L.A., Dunlop P.C.;
RT   "Specificity of G alpha q and G alpha 11 gene expression in platelets and
RT   erythrocytes. Expressions of cellular differentiation and species
RT   differences.";
RL   Biochem. J. 318:1023-1031(1996).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems. Acts as an activator of phospholipase C (By similarity).
CC       Transduces FFAR4 signaling in response to long-chain fatty acids
CC       (LCFAs) (By similarity). Together with GNAQ, required for heart
CC       development (By similarity). {ECO:0000250|UniProtKB:P21278,
CC       ECO:0000250|UniProtKB:P29992}.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site. Interacts
CC       with RGS22. Interacts with NTSR1. {ECO:0000250|UniProtKB:P29992}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29992};
CC       Lipid-anchor {ECO:0000250|UniProtKB:P29992}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P29992}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L43134; AAB39497.1; -; mRNA.
DR   PIR; S71964; S71964.
DR   AlphaFoldDB; P52206; -.
DR   SMR; P52206; -.
DR   CORUM; P52206; -.
DR   PRIDE; P52206; -.
DR   InParanoid; P52206; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001508; P:action potential; IBA:GO_Central.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; GTP-binding; Lipoprotein; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Palmitate; Reference proteome;
KW   Transducer.
FT   CHAIN           <1..>198
FT                   /note="Guanine nucleotide-binding protein subunit alpha-11"
FT                   /id="PRO_0000203745"
FT   DOMAIN          <1..>198
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          <1..11
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          135..143
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          158..167
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         3..10
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P29992"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         137..140
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27600"
FT   NON_TER         1
FT   NON_TER         198
SQ   SEQUENCE   198 AA;  23133 MW;  BBB0842FD9399873 CRC64;
     LLGTGESGKS TFIKQMRIIH GAGYSEEDKR GFTKLVYQNI FTAMQAMIRA METLKILYKY
     EQNKANALLI REVDVEKVTT FEHRYVHAIK TLWDDPGIQE CYDRRREYQL SDSAKYYLAD
     VDRIATSGYL PTQQDVLRVR VPTTGIIEYP FDLENIIFRM VDVGGQRSER RKWIHCFENV
     TSIMFLVALS EYDHVLVE