GNA14_BOVIN
ID GNA14_BOVIN Reviewed; 355 AA.
AC P38408;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-14;
DE Short=G alpha-14;
DE Short=G-protein subunit alpha-14;
DE AltName: Full=G-protein subunit GL1 alpha;
GN Name=GNA14;
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
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; D90335; BAA14349.1; -; mRNA.
DR PIR; A40891; A40891.
DR RefSeq; NP_776748.1; NM_174323.2.
DR AlphaFoldDB; P38408; -.
DR SMR; P38408; -.
DR STRING; 9913.ENSBTAP00000028151; -.
DR PaxDb; P38408; -.
DR PRIDE; P38408; -.
DR Ensembl; ENSBTAT00000028151; ENSBTAP00000028151; ENSBTAG00000021127.
DR GeneID; 281789; -.
DR KEGG; bta:281789; -.
DR CTD; 9630; -.
DR VEuPathDB; HostDB:ENSBTAG00000021127; -.
DR VGNC; VGNC:29447; GNA14.
DR eggNOG; KOG0085; Eukaryota.
DR GeneTree; ENSGT00940000158510; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P38408; -.
DR OMA; CCVSAED; -.
DR OrthoDB; 754573at2759; -.
DR TreeFam; TF300673; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021127; Expressed in prostate gland and 96 other tissues.
DR ExpressionAtlas; P38408; baseline and differential.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; 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 GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transducer.
FT CHAIN 1..355
FT /note="Guanine nucleotide-binding protein subunit alpha-14"
FT /id="PRO_0000203751"
FT DOMAIN 34..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 37..50
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 355 AA; 41499 MW; 60888CC6C9B7243B CRC64;
MAGCCCLSAE EKESQRISAE IERQLRRDKK DARRELKLLL LGTGESGKST FIKQMRIIHG
SGYSDEDRKG FTKLVYQNIF TAMQAMIRAM DTLKIQYVCE QNKENAQLIR EVEVDKVSTL
SRDQVEAIKQ LWQDPGIQEC YDRRREYQLS DSAKYYLTDI DRIAMPAFVP TQQDVLRVRV
PTTGIIEYPF DLENIIFRMV DVGGQRSERR KWIHCFESVT SIIFLVALSE YDQVLAECDN
ENRMEESKAL FKTIITYPWF LNSSVILFLN KKDLLEEKIM YSHLISYFPE YTGPKQDVKA
ARDFILKLYQ DQNPDKEKVI YSHFTCATDT ENIRFVFAAV KDTILQLNLR EFNLV
