GPA15_CAEEL
ID GPA15_CAEEL Reviewed; 356 AA.
AC P91907; Q9BIG1;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Guanine nucleotide-binding protein alpha-15 subunit;
GN Name=gpa-15; ORFNames=M04C7.1;
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; AY008137; AAG32090.1; -; mRNA.
DR EMBL; Z83117; CAB05570.2; -; Genomic_DNA.
DR PIR; T23705; T23705.
DR RefSeq; NP_492312.1; NM_059911.1.
DR AlphaFoldDB; P91907; -.
DR SMR; P91907; -.
DR STRING; 6239.M04C7.1.1; -.
DR EPD; P91907; -.
DR PaxDb; P91907; -.
DR EnsemblMetazoa; M04C7.1.1; M04C7.1.1; WBGene00001677.
DR GeneID; 172645; -.
DR KEGG; cel:CELE_M04C7.1; -.
DR UCSC; M04C7.1; c. elegans.
DR CTD; 172645; -.
DR WormBase; M04C7.1; CE28623; WBGene00001677; gpa-15.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000168787; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P91907; -.
DR OMA; KKIYTHV; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P91907; -.
DR PRO; PR:P91907; -.
DR Proteomes; UP000001940; Chromosome I.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
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; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..356
FT /note="Guanine nucleotide-binding protein alpha-15 subunit"
FT /id="PRO_0000203655"
FT DOMAIN 33..356
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 36..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 175..183
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 198..207
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 267..274
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 326..331
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 177..183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 202..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 271..274
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 328
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 5
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 40862 MW; 70F37C61031FA04E CRC64;
MGSTCSTPES KEQKRINSVI DKQIRKDEDD EIGNQKLLLL GTGECGKSTI LKQINILHSS
GFSKADLKNV AGTVYSNIIQ GVATLLKAKD HFYYELSTPE LDADAQHILS LADSSKDAMP
FIPLTFNAIK RLWHDPVVQK TFERRAEFQM MDTLVYFMNE LDRINNADYI PTVDDMLRIR
IPTMGVVQQT IEIKGTKFRI YDVGGQRSER RKWIHLFDNV NATIFISAIN EFNQKLNEDG
QTNRMKESIK LFETICNSRW FVQAAMILFL NKRDLFEQKL KTTSINVLFS TYQGSNDYAE
CVAYIQMRFE RLNKYSDIKK IYTHVTCATD TNQIQLVIDS VVDMVIGRNL RGTGME
