GPA12_CAEEL
ID GPA12_CAEEL Reviewed; 355 AA.
AC Q19572;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Guanine nucleotide-binding protein alpha-12 subunit;
GN Name=gpa-12; ORFNames=F18G5.3;
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].
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19380113; DOI=10.1016/j.chom.2009.03.006;
RA Ziegler K., Kurz C.L., Cypowyj S., Couillault C., Pophillat M., Pujol N.,
RA Ewbank J.J.;
RT "Antifungal innate immunity in C. elegans: PKCdelta links G protein
RT signaling and a conserved p38 MAPK cascade.";
RL Cell Host Microbe 5:341-352(2009).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLN-205.
RX PubMed=22470487; DOI=10.1371/journal.pone.0033887;
RA Labed S.A., Omi S., Gut M., Ewbank J.J., Pujol N.;
RT "The pseudokinase NIPI-4 is a novel regulator of antimicrobial peptide gene
RT expression.";
RL PLoS ONE 7:E33887-E33887(2012).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (Probable). 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 (PubMed:22470487,
CC PubMed:19380113). Upstream of plc-3, tpa-1 and the p38-like pathway,
CC required for the expression of antimicrobial peptide nlp-29 in the
CC epidermis in response to fungal infection or physical injury
CC (PubMed:19380113). {ECO:0000269|PubMed:19380113,
CC ECO:0000269|PubMed:22470487, ECO:0000305}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- DISRUPTION PHENOTYPE: Up-regulation of nlp-29 is severely impaired in
CC the hyp7 epidermal cell but not in vulva epidermal cells following
CC fungal infection by D.coniospora or physical injury.
CC {ECO:0000269|PubMed:19380113}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008134; AAG32087.1; -; mRNA.
DR EMBL; FO080202; CCD61930.1; -; Genomic_DNA.
DR PIR; D89605; D89605.
DR RefSeq; NP_509557.1; NM_077156.3.
DR AlphaFoldDB; Q19572; -.
DR SMR; Q19572; -.
DR BioGRID; 46073; 1.
DR STRING; 6239.F18G5.3; -.
DR EPD; Q19572; -.
DR PaxDb; Q19572; -.
DR PeptideAtlas; Q19572; -.
DR EnsemblMetazoa; F18G5.3.1; F18G5.3.1; WBGene00001674.
DR EnsemblMetazoa; F18G5.3.2; F18G5.3.2; WBGene00001674.
DR GeneID; 181157; -.
DR KEGG; cel:CELE_F18G5.3; -.
DR UCSC; F18G5.3; c. elegans.
DR CTD; 181157; -.
DR WormBase; F18G5.3; CE20692; WBGene00001674; gpa-12.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000168398; -.
DR HOGENOM; CLU_014184_3_1_1; -.
DR InParanoid; Q19572; -.
DR OMA; MVASNEY; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q19572; -.
DR Reactome; R-CEL-193648; NRAGE signals death through JNK.
DR Reactome; R-CEL-416482; G alpha (12/13) signalling events.
DR Reactome; R-CEL-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-CEL-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-CEL-9013148; CDC42 GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q19572; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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 1: Evidence at protein level;
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_0000203649"
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"
FT MUTAGEN 205
FT /note="Q->L: Probably constitutively active. Constitutive
FT expression of nlp-29, nlp-31, nlp-34, cnc-2, cnc-4 and cnc-
FT 1 in absence of infection."
FT /evidence="ECO:0000269|PubMed:22470487"
SQ SEQUENCE 355 AA; 41974 MW; 40DD3793B8132E69 CRC64;
MVCCFGKKDE RTKTIEKELH KERKIMRRQI NLLLLGSGES GKSTFVKQMH IIHGAGEFTA
DEVRAYRQQI YQNAISAMRV LLDARNKLGI AWEDPKRQVE VEKVMRFSVG DLLKGIDFTT
FVEVAPIISD FWNDAAIRKT YEQRNLFQIS DSCQYFFEHI PRIAMPDFYP TNRDILFCRK
ATRGISEHIF EINKIPFRFI DVGGQRSQRQ KWFQCFTDIT SILFMVASNE YDQVILEDRR
TNRVVESRSV FETIVNNRAF SNVSIILFMN KNDLLQEKVP KSDIRQYFTD FTGDHTLVRD
VQFFLVDKFE ASRRDRARPF FYHFTTAVDT ENIRRVFRDV RESILEQNLK TLMMQ
