GPA2_CAEBR
ID GPA2_CAEBR Reviewed; 338 AA.
AC Q4VT35; A8XDE2; Q61GC9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
GN Name=gpa-2; ORFNames=CBG11277;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=15856303; DOI=10.1007/s00438-004-1105-6;
RA Jovelin R., Phillips P.C.;
RT "Functional constraint and divergence in the G protein family in
RT Caenorhabditis elegans and Caenorhabditis briggsae.";
RL Mol. Genet. Genomics 273:299-310(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Involved in behavioral responses to P.aeruginosa by
CC controlling the expression of daf-7, a member of the TGF-beta family,
CC in ASJ sensory neurons. {ECO:0000250|UniProtKB:P22454}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAW02901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY634295; AAW02901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CAAC02000500; CAP30661.4; -; Genomic_DNA.
DR AlphaFoldDB; Q4VT35; -.
DR SMR; Q4VT35; -.
DR STRING; 6238.CBG11277; -.
DR WormBase; CBG11277; CBP42726; WBGene00032418; Cbr-gpa-2.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q4VT35; -.
DR OMA; EYNEVLF; -.
DR OrthoDB; 754573at2759; -.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0007188; P:adenylate cyclase-modulating 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; IPR001408; Gprotein_alpha_I.
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; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 3: Inferred from homology;
KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding; Transducer.
FT CHAIN 1..338
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203630"
FT DOMAIN 14..338
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 17..30
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 158..166
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 181..190
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 250..257
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 308..313
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 22..29
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 160..166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185..189
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254..257
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 39627 MW; 937DCAB684F60EF9 CRC64;
MLILFLLRTH SCNFQNFESF LGAGECGKST VLKQMRLLTS KTYTADELEA QAKLVFTNIV
IEMDHIVKAM PSAHFNFTDP MREHDVHMLT LYIKDMQHKS FHADAAEHVA KLWKDPVIKR
LYAERRERNI RDIGDNTEYF FENLDRIAKP DYSPNSMDTL LLRTKTTGIV EVQFEIKKVK
FRVFDVGGQR SERKKWIHCF EDVNAIIFIA ALSEYNEVLF EDETTNRMIE SMRLFESICN
SRWFHNTNII LFLNKKDLFE DKIKKENITK AFPEYRGAQN YEETVAFIKQ KFEALSNNPK
KTFYVHETCA TDTNQVQKIL DSVISMIIQS NLHKSGLY
