GPA11_CAEEL
ID GPA11_CAEEL Reviewed; 363 AA.
AC O76584; F0IWT4;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Guanine nucleotide-binding protein alpha-11 subunit;
GN Name=gpa-11; ORFNames=C16A11.1;
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], AND ALTERNATIVE SPLICING.
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 IDENTIFICATION.
RX PubMed=9288111; DOI=10.1038/ng0997-119;
RA Jansen G., Hazendonk E., Thijssen K.L., Plasterk R.H.;
RT "Reverse genetics by chemical mutagenesis in Caenorhabditis elegans.";
RL Nat. Genet. 17:119-121(1997).
RN [4]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [5]
RP FUNCTION.
RX PubMed=15492222; DOI=10.1073/pnas.0403369101;
RA Chao M.Y., Komatsu H., Fukuto H.S., Dionne H.M., Hart A.C.;
RT "Feeding status and serotonin rapidly and reversibly modulate a
RT Caenorhabditis elegans chemosensory circuit.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15512-15517(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17187771; DOI=10.1016/j.ydbio.2006.11.028;
RA Lans H., Jansen G.;
RT "Multiple sensory G proteins in the olfactory, gustatory and nociceptive
RT neurons modulate longevity in Caenorhabditis elegans.";
RL Dev. Biol. 303:474-482(2007).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Mediates the transduction of food and serotonin signals, which
CC modulates the avoidance response to the odorant octanol. Has a role in
CC lifespan to promote longevity. {ECO:0000269|PubMed:15492222,
CC ECO:0000269|PubMed:17187771}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=O76584-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O76584-2; Sequence=VSP_043928;
CC -!- TISSUE SPECIFICITY: Expressed in ADL and ASH neurons.
CC {ECO:0000269|PubMed:10192394}.
CC -!- DISRUPTION PHENOTYPE: Slow to respond to octanol.
CC {ECO:0000269|PubMed:17187771}.
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008133; AAG32086.1; -; mRNA.
DR EMBL; FO080260; CCD62416.1; -; Genomic_DNA.
DR EMBL; FO080260; CCD62417.1; -; Genomic_DNA.
DR RefSeq; NP_001254088.1; NM_001267159.1. [O76584-2]
DR RefSeq; NP_001254089.1; NM_001267160.1. [O76584-1]
DR AlphaFoldDB; O76584; -.
DR SMR; O76584; -.
DR STRING; 6239.C16A11.1b; -.
DR PaxDb; O76584; -.
DR EnsemblMetazoa; C16A11.1a.1; C16A11.1a.1; WBGene00001673. [O76584-1]
DR EnsemblMetazoa; C16A11.1a.2; C16A11.1a.2; WBGene00001673. [O76584-1]
DR EnsemblMetazoa; C16A11.1b.1; C16A11.1b.1; WBGene00001673. [O76584-2]
DR GeneID; 173759; -.
DR KEGG; cel:CELE_C16A11.1; -.
DR UCSC; C16A11.1; c. elegans. [O76584-1]
DR CTD; 173759; -.
DR WormBase; C16A11.1a; CE20515; WBGene00001673; gpa-11. [O76584-1]
DR WormBase; C16A11.1b; CE45827; WBGene00001673; gpa-11. [O76584-2]
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196059; -.
DR HOGENOM; CLU_014184_5_0_1; -.
DR InParanoid; O76584; -.
DR OMA; VVFKISM; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; O76584; -.
DR PRO; PR:O76584; -.
DR Proteomes; UP000001940; Chromosome II.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISS:WormBase.
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; ISS:WormBase.
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:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:WormBase.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..363
FT /note="Guanine nucleotide-binding protein alpha-11 subunit"
FT /id="PRO_0000203647"
FT DOMAIN 26..363
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 29..42
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 170..178
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 193..202
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 272..279
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 333..338
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 172..178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 197..201
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 276..279
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MPRIERDDSSSGDTINSSAMEASTTDNGPLETTTDSNEPRPPPPLTN
FT PTPRAPSVPPPMPPKRDLTPPRTCYDCGCFRNKILAPLNSSTPGASGPAPPANTTSSTN
FT RTVSQQDKLAAGTPGPHSSTHNIESSAFATADITLGFLLCGRLSFTTQVNNRVNVCGGT
FT EM (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_043928"
SQ SEQUENCE 363 AA; 42232 MW; 29A8F0F1F21579F6 CRC64;
MSAADMARKN SLINRQLEKE KIDSKKMLKI LLLGGPECGK STIFKQMKII HMNGFSDLDY
VNFRYLIYSN IMQSMDQLLE AAEFFHFPPD DSPSIRRALN HYKSYKVRYS TSEVELNREL
ADSLSKLYNA EFIKSVLNRK NELKLLDSAV YFLDDIDRIS AHEYKPTEMD VLRARVPTTG
ITEIEFPFKQ ASLRMVDVGG QRSEQRKWIH CFDNVNGVLF IAAISGYNLY DEDEENRKDD
GTPTKTNRLR YSMELFKRIA NHQCFSKKTA MILFLNKIDI FKEKIGKYPL TTCFKNYKGV
NAFEPACKYV TDRFSRLVSG DIQHEKPLYT HITNATDTRN IDRVFDSCMD VIFKISMEKV
GFM
