GNA11_BOVIN
ID GNA11_BOVIN Reviewed; 359 AA.
AC P38409; Q2TA47;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-11;
DE Short=G alpha-11;
DE Short=G-protein subunit alpha-11;
DE AltName: Full=G-protein subunit GL2 alpha;
GN Name=GNA11;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1905731; DOI=10.1016/s0021-9258(18)98952-0;
RA Nakamura F., Ogata K., Shiozaki K., Kameyama K., Ohara K., Haga T.,
RA Nukada T.;
RT "Identification of two novel GTP-binding protein alpha-subunits that lack
RT apparent ADP-ribosylation sites for pertussis toxin.";
RL J. Biol. Chem. 266:12676-12681(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAI11119.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA14350.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D90336; BAA14350.1; ALT_INIT; mRNA.
DR EMBL; BC111118; AAI11119.2; ALT_INIT; mRNA.
DR PIR; B40891; B40891.
DR RefSeq; NP_776747.1; NM_174322.3.
DR AlphaFoldDB; P38409; -.
DR SMR; P38409; -.
DR BioGRID; 159102; 1.
DR STRING; 9913.ENSBTAP00000050620; -.
DR PaxDb; P38409; -.
DR PRIDE; P38409; -.
DR Ensembl; ENSBTAT00000085254; ENSBTAP00000074164; ENSBTAG00000012181.
DR GeneID; 281788; -.
DR KEGG; bta:281788; -.
DR CTD; 2767; -.
DR VEuPathDB; HostDB:ENSBTAG00000012181; -.
DR VGNC; VGNC:29444; GNA11.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000161033; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P38409; -.
DR OMA; CAYMESK; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000012181; Expressed in jejunum and 106 other tissues.
DR ExpressionAtlas; P38409; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
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:0009649; P:entrainment of circadian clock; ISS:AgBase.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; ISS:AgBase.
DR GO; GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007603; P:phototransduction, visible light; ISS:AgBase.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000654; Gprotein_alpha_Q.
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 PRINTS; PR00442; GPROTEINAQ.
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..359
FT /note="Guanine nucleotide-binding protein subunit alpha-11"
FT /id="PRO_0000203744"
FT DOMAIN 38..359
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 41..54
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 178..186
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 201..210
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 270..277
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 329..334
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 46..53
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P29992"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 180..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 274..277
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P27600"
FT LIPID 9
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P29992"
FT LIPID 10
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P29992"
SQ SEQUENCE 359 AA; 42070 MW; B0BAC4FBF5AAE8D5 CRC64;
MTLESMMACC LSDEVKESKR INAEIEKQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
IIHGAGYSEE DKRGFTKLVY QNIFTAMQAM IRAMETLKIL YKYEQNKANA LLIREVDVEK
VTTFEHRYVS AIKTLWNDPG IQECYDRRRE YQLSDSAKYY LTDVDRIATS GYLPTQQDVL
RVRVPTTGII EYPFDLENII FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
ESDNENRMEE SKALFRTIVT YPWFQNSSVI LFLNKKDLLE DKILHSHLVD YFPEFDGPQR
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
