ID   GNA14_XENLA             Reviewed;         354 AA.
AC   O73819;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Guanine nucleotide-binding protein subunit alpha-14;
DE            Short=G alpha-14;
DE            Short=G-protein subunit alpha-14;
GN   Name=gna14;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9677362; DOI=10.1074/jbc.273.31.19431;
RA   Shapira H., Amit I., Revach M., Oron Y., Battey J.F.;
RT   "Galpha14 and Galphaq mediate the response to trypsin in Xenopus oocytes.";
RL   J. Biol. Chem. 273:19431-19436(1998).
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. Mediates responses to
CC       trypsin.
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}.
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DR   EMBL; AF059182; AAC41382.1; -; mRNA.
DR   RefSeq; NP_001083750.2; NM_001090281.2.
DR   AlphaFoldDB; O73819; -.
DR   SMR; O73819; -.
DR   PRIDE; O73819; -.
DR   DNASU; 399096; -.
DR   GeneID; 399096; -.
DR   KEGG; xla:399096; -.
DR   CTD; 399096; -.
DR   Xenbase; XB-GENE-6254627; gna14.L.
DR   OMA; CCVSAED; -.
DR   OrthoDB; 754573at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 399096; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
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..354
FT                   /note="Guanine nucleotide-binding protein subunit alpha-14"
FT                   /id="PRO_0000203754"
FT   DOMAIN          33..354
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          36..49
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          173..181
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          196..205
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          265..272
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          324..329
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         41..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         175..181
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         200..204
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         269..272
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  41595 MW;  C7105026B037600E CRC64;
     MAGCCLSAEE KESQRINAEI EKQLRRDKRD ARRELKLLLL GTGESGKSTF IKQMRIIHGS
     GYTDEDRKGF TKLVYQNIFT SMQSMIRAMD TLRIQYTSEQ NMENALVIRE VEVDKVSSLE
     RKHVEAIKKL WEDEGIQECY DRRREYQLSD STKYYLSDID RISNPGFIPT QQDVLRVRVP
     TTGIIEYPFD LENIIFRMVD VGGQRSERRK WIHCFENVTS IIFLVALSEY DQVLAECDNE
     NRMEESKALF KTIITYPWFQ NSSVILFLNK KDLLQEKIMY SHLIDYFPEF TGPKQDSQAA
     RDFILKLYQD QNPDKEKVIY SHFTCATDTE NIRFVFAAVK DTILQLNLRE FNLV