GPA6_CAEEL
ID GPA6_CAEEL Reviewed; 364 AA.
AC Q93743;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Guanine nucleotide-binding protein alpha-6 subunit;
GN Name=gpa-6; ORFNames=F48C11.1;
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].
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
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; AY008129; AAG32082.1; -; mRNA.
DR EMBL; Z80789; CAB02553.1; -; Genomic_DNA.
DR PIR; T22379; T22379.
DR RefSeq; NP_510189.1; NM_077788.1.
DR AlphaFoldDB; Q93743; -.
DR SMR; Q93743; -.
DR BioGRID; 46345; 1.
DR IntAct; Q93743; 1.
DR STRING; 6239.F48C11.1; -.
DR EPD; Q93743; -.
DR PaxDb; Q93743; -.
DR PRIDE; Q93743; -.
DR EnsemblMetazoa; F48C11.1.1; F48C11.1.1; WBGene00001668.
DR GeneID; 181442; -.
DR KEGG; cel:CELE_F48C11.1; -.
DR UCSC; F48C11.1; c. elegans.
DR CTD; 181442; -.
DR WormBase; F48C11.1; CE20829; WBGene00001668; gpa-6.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196059; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q93743; -.
DR OMA; PEYEDFC; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; Q93743; -.
DR PRO; PR:Q93743; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA: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; 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 2: Evidence at transcript level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..364
FT /note="Guanine nucleotide-binding protein alpha-6 subunit"
FT /id="PRO_0000203639"
FT DOMAIN 40..363
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 184..192
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 207..216
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 276..283
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 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 280..283
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 LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 364 AA; 42058 MW; 14D594208714F63E CRC64;
MGAGATGLRG ARLSPEERAN SSKSRAIDRA LSKDHTDDLN RFKILLLGTA ESGKSTIFKQ
MRVLHLDGYA KEDALEYLSI IHSNCMEALT QLVDACTAFG INHDITVQED VNRFEDFKRK
LRDPEGLVIP VVIGRCMDRV WHSPSLQLCY DTRRFRFALL DSAKYFMDNI VRLTEDNYVP
SIQDIVHCRI STTGINELAF NYKKMDFKMV DVGGQRSERR KWIHCFDNVD MILFIVSMSD
YDQLDPEDNK YNRMKQSYEI FKTIVHSDLF RHASIVLFLN KYDVFVEKLK TSPLRRSFKN
YEGDNSEESA REFIKKLFRR CITDRHKFFV FETTATDTGN IDLVFGSAVA HIVNENLRSA
GLHE
