GPA10_CAEBR
ID GPA10_CAEBR Reviewed; 362 AA.
AC Q4VT42; A8XUM2; Q60WQ1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Guanine nucleotide-binding protein alpha-10 subunit;
GN Name=gpa-10; ORFNames=CBG19035;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=15856303; DOI=10.1007/s00438-004-1105-6;
RA Jovelin R., Phillips P.C.;
RT "Functional constraint and divergence in the G protein family in
RT Caenorhabditis elegans and Caenorhabditis briggsae.";
RL Mol. Genet. Genomics 273:299-310(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW02894.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY634288; AAW02894.1; ALT_SEQ; Genomic_DNA.
DR EMBL; HE601047; CAP36347.3; -; Genomic_DNA.
DR RefSeq; XP_002637339.1; XM_002637293.1.
DR AlphaFoldDB; Q4VT42; -.
DR SMR; Q4VT42; -.
DR STRING; 6238.CBG19035; -.
DR GeneID; 8579334; -.
DR KEGG; cbr:CBG_19035; -.
DR CTD; 8579334; -.
DR WormBase; CBG19035; CBP39264; WBGene00038318; Cbr-gpa-10.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q4VT42; -.
DR OMA; YMNIVQA; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008549; Chromosome V.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
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: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; 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 3: Inferred from homology;
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..362
FT /note="Guanine nucleotide-binding protein alpha-10 subunit"
FT /id="PRO_0000203645"
FT DOMAIN 35..362
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 38..51
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 182..190
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 205..214
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 274..281
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 333..337
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 43..50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 184..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 209..213
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 278..281
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"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 57..62
FT /note="Missing (in Ref. 1; AAW02894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 41770 MW; 7C3186A7BC8C8563 CRC64;
MGACGSVMQD EALKEQARIH RQIEKSLEKK KSALLEQSVL LIGPGESGKS TVLKQIRSVT
VCRAMCGGYT KHELEEKKLL ILRNLWTFSD MLLEYVIKNY LDMNETDKKK YKVMIEELKF
CVMSGGHMGD ELAETVKVFW LCAPIQEAYE KRNTYHLTES AGYFFENIDR IKMPDFQPTN
QDIVRIRVPT TGVVTADVIL KNIKLSVIDC GGQRQERRKW YHYFDDVHAV LFVAAISEYD
QKLVEDESVN RMDEALNLYH IVFNGKYFTK AACILFLNKI DLFREKVKSV SIKKFHPGFE
GANTAEDGAK YFRRKFRDGM HPDFKKRLYC HETCAISDQV QIIINTVIDT VVQENLKDTG
MI
