GPA14_CAEEL
ID GPA14_CAEEL Reviewed; 408 AA.
AC Q9BIG2; O01428; Q7Z117;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Guanine nucleotide-binding protein alpha-14 subunit;
GN Name=gpa-14 {ECO:0000312|WormBase:B0207.3b};
GN ORFNames=B0207.3 {ECO:0000312|WormBase:B0207.3b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RA Cuppen E., Jansen G., Plasterk R.H.A.;
RT "Interaction analysis of the complete G-alpha subfamily of heterotrimeric G
RT proteins from Caenorhabditis elegans.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10192394; DOI=10.1038/7753;
RA Jansen G., Thijssen K.L., Werner P., van der Horst M., Hazendonk E.,
RA Plasterk R.H.A.;
RT "The complete family of genes encoding G proteins of Caenorhabditis
RT elegans.";
RL Nat. Genet. 21:414-419(1999).
RN [4]
RP INTERACTION WITH DOP-2.
RX PubMed=22280843; DOI=10.1186/1750-2187-7-3;
RA Pandey P., Harbinder S.;
RT "The Caenorhabditis elegans D2-like dopamine receptor DOP-2 physically
RT interacts with GPA-14, a Galphai subunit.";
RL J. Mol. Signal. 7:3-3(2012).
RN [5]
RP FUNCTION.
RX PubMed=23607404; DOI=10.1186/1744-9081-9-16;
RA Mersha M., Formisano R., McDonald R., Pandey P., Tavernarakis N.,
RA Harbinder S.;
RT "GPA-14, a Galpha(i) subunit mediates dopaminergic behavioral plasticity in
RT C. elegans.";
RL Behav. Brain Funct. 9:16-16(2013).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. In association with the G-protein coupled dopamine receptor
CC dop-2, modulates two types of learning: touch habituation and
CC chemosensory associative conditioning (PubMed:23607404).
CC {ECO:0000269|PubMed:23607404}.
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 the dopamine receptor dop-2 (via C-terminus); the interaction is
CC direct (PubMed:22280843). {ECO:0000269|PubMed:22280843}.
CC -!- INTERACTION:
CC Q9BIG2; E7EM37: dop-2; NbExp=4; IntAct=EBI-2923711, EBI-6082999;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:B0207.3b};
CC IsoId=Q9BIG2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:B0207.3a};
CC IsoId=Q9BIG2-2; Sequence=VSP_020152, VSP_020153;
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008136; AAG32089.1; -; mRNA.
DR EMBL; FO080115; CCD61315.1; -; Genomic_DNA.
DR EMBL; FO080115; CCD61316.1; -; Genomic_DNA.
DR PIR; C87790; C87790.
DR RefSeq; NP_001020965.1; NM_001025794.1.
DR RefSeq; NP_001020966.2; NM_001025795.2. [Q9BIG2-1]
DR AlphaFoldDB; Q9BIG2; -.
DR SMR; Q9BIG2; -.
DR BioGRID; 37723; 1.
DR IntAct; Q9BIG2; 2.
DR STRING; 6239.B0207.3b; -.
DR PaxDb; Q9BIG2; -.
DR EnsemblMetazoa; B0207.3.1; B0207.3.1; WBGene00001676. [Q9BIG2-1]
DR GeneID; 172269; -.
DR KEGG; cel:CELE_B0207.3; -.
DR UCSC; B0207.3b; c. elegans. [Q9BIG2-1]
DR CTD; 172269; -.
DR WormBase; B0207.3a; CE27564; WBGene00001676; gpa-14. [Q9BIG2-2]
DR WormBase; B0207.3b; CE38990; WBGene00001676; gpa-14. [Q9BIG2-1]
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196059; -.
DR HOGENOM; CLU_014184_2_1_1; -.
DR InParanoid; Q9BIG2; -.
DR OMA; ACMESVF; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q9BIG2; -.
DR PRO; PR:Q9BIG2; -.
DR Proteomes; UP000001940; Chromosome I.
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:0007188; P:adenylate cyclase-modulating G protein-coupled 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 1: Evidence at protein level;
KW Alternative splicing; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..408
FT /note="Guanine nucleotide-binding protein alpha-14 subunit"
FT /id="PRO_0000203653"
FT DOMAIN 71..408
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 74..87
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 214..222
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 237..246
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 321..328
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 378..383
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 79..86
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 86
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 216..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 241..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 285..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 325..328
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020152"
FT VAR_SEQ 37..52
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_020153"
SQ SEQUENCE 408 AA; 46734 MW; F5A21AAAF50311E9 CRC64;
MAFSCFDKFS YTYCYQCMHG PDGCMVPSRN GEGTELYAHS EELEAKLREL ARRGHMEIEK
ELALEKKTYG SHIKILILGG PLSGKSTIFK QMQIIHVDGF KTDQELIQYR GLIDNNIRDI
YLQLIAGSRV VGIPLDPIEH ITYEIDEIYA PMSDAFSVRT ISELLEPLTE FWNSKQIQEI
YKRRCEFELL DSTKYYLENL TRIADPTYLP NQEDIVHSRK ATMSINSIVF EYTGVSLLMI
DVGGQRSERK KWLHLFDDAK VVLFVIDLTG YAKRSEESRM ELSRFPKFFR DVGSNAYDMK
VALKIFNEVA AASALANAVF LLFFNKVDLF KEILSQVNLQ PCFSKFDGEN TYEETSKYIC
EKFIRAASSK KSVFPHFTTA TNTENVKLVF RACMESVFKA NAKATGLS
