GPA12_CAEBR
ID GPA12_CAEBR Reviewed; 355 AA.
AC Q613V4; A8XNX9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Guanine nucleotide-binding protein alpha-12 subunit;
GN Name=gpa-12; ORFNames=CBG16182;
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. May play a role in resistance to fungal infection in the
CC epidermis by regulating the up-regulation of several antimicrobial
CC peptides of the NLP and CNC families. Upstream of plc-3, egl-8, tpa-1
CC and the p38-like pathway, required for the expression of antimicrobial
CC peptide nlp-29 in the epidermis in response to fungal infection or
CC physical injury. {ECO:0000250|UniProtKB:Q19572}.
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. {ECO:0000305}.
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DR EMBL; AY634290; AAW02896.1; -; Genomic_DNA.
DR EMBL; HE600961; CAP34219.3; -; Genomic_DNA.
DR RefSeq; XP_002643509.1; XM_002643463.1.
DR AlphaFoldDB; Q613V4; -.
DR SMR; Q613V4; -.
DR STRING; 6238.CBG16182; -.
DR GeneID; 8585502; -.
DR KEGG; cbr:CBG_16182; -.
DR CTD; 8585502; -.
DR WormBase; CBG16182; CBP45901; WBGene00036208; Cbr-gpa-12.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_3_1_1; -.
DR InParanoid; Q613V4; -.
DR OMA; MVASNEY; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0031752; F:D5 dopamine receptor binding; 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 GO; GO:0007266; P:Rho protein signal transduction; 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; IPR000469; Gprotein_alpha_12/13.
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; PR00440; GPROTEINA12.
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;
KW Reference proteome; Transducer.
FT CHAIN 1..355
FT /note="Guanine nucleotide-binding protein alpha-12 subunit"
FT /id="PRO_0000203648"
FT DOMAIN 28..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 31..44
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 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 43
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; 42004 MW; 32234E77366AD008 CRC64;
MVCCFGKKDE RTKTIEKELH KERKIMRRQI NLLLLGSGES GKSTFVKQMH IIHGAGEFTA
DEVRAYRQQI YQNAISAMRV LLDARNKLGI AWEDPKRQVE VEKVMRFTVG DLLKGIDFTT
FVEVAPIISD FWNDAAIRKT YEQRNLFQIS DSCQYFFEHI PRIAMPDFYP TNRDILFCRK
ATRGISEHIF EINKIPFRFI DVGGQRSQRQ KWFQCFTDIT SILFMVASNE YDQVILEDRR
TNRVVESRSV FETIVNNRSF SNVSIILFMN KNDLLQEKVP KSDIRQYFTD FTGDHTLVRD
VQFFLVDKFE ASRRDRARPF FYHFTTAVDT ENIRRVFRDV RESILEQNLK TLMMQ
