GPA13_CAEEL
ID GPA13_CAEEL Reviewed; 348 AA.
AC Q9XTB2; Q9BIG3;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Guanine nucleotide-binding protein alpha-13 subunit;
GN Name=gpa-13; ORFNames=F18E2.5;
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. {ECO:0000250}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9XTB2; G5EEM0: nhr-114; NbExp=3; IntAct=EBI-6094254, EBI-315855;
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY008135; AAG32088.1; -; mRNA.
DR EMBL; Z75537; CAA99838.2; -; Genomic_DNA.
DR EMBL; Z75527; CAA99838.2; JOINED; Genomic_DNA.
DR PIR; T19312; T19312.
DR RefSeq; NP_001256450.1; NM_001269521.1.
DR AlphaFoldDB; Q9XTB2; -.
DR SMR; Q9XTB2; -.
DR BioGRID; 44766; 2.
DR IntAct; Q9XTB2; 2.
DR STRING; 6239.F18E2.5b; -.
DR PaxDb; Q9XTB2; -.
DR EnsemblMetazoa; F18E2.5a.1; F18E2.5a.1; WBGene00001675.
DR GeneID; 179746; -.
DR KEGG; cel:CELE_F18E2.5; -.
DR UCSC; F18E2.5; c. elegans.
DR CTD; 179746; -.
DR WormBase; F18E2.5a; CE30659; WBGene00001675; gpa-13.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00970000196172; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q9XTB2; -.
DR PhylomeDB; Q9XTB2; -.
DR PRO; PR:Q9XTB2; -.
DR Proteomes; UP000001940; Chromosome V.
DR ExpressionAtlas; Q9XTB2; baseline and differential.
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:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:WormBase.
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 1: Evidence at protein level;
KW GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..348
FT /note="Guanine nucleotide-binding protein alpha-13 subunit"
FT /id="PRO_0000203651"
FT DOMAIN 34..348
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 37..50
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 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 42..49
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 326
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"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 348 AA; 40067 MW; F0268A48CBC5C4B3 CRC64;
MGCNFSSQSK LQVPEIRASR SITPASQKSE DPYSHIRLLL LGSAESGKTT VLEQVRLLYK
QHFTESEYFH RRAFIYHNIF KSIKALCRAM RMSDIQFADP INMGRAQSII ADEHGHYGLF
SKDLAEKIKH IWNDKSMQKL YARRSQFNLN DSASYFLNNI DKINMVDYKP SERDLIMAYV
PTCGVQNVIF TACNQSFQLF DIGGQKIDRR KWALQYEGID AIFFCIAISE YDQVMSEDMV
TNRLDDALNL LQSISEDPAF ATTPIYLFLN EIDVFCEKLS VIPLSKYKPD FKGGDQDDAI
DFMENLACEA LGKRDRSLYR VYRCIAIDTQ MMAELLSTVF KDIAKRKK
