GPA14_CAEBR
ID GPA14_CAEBR Reviewed; 408 AA.
AC Q4VT38; A8WW16; Q61XD2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Guanine nucleotide-binding protein alpha-14 subunit;
GN Name=gpa-14; ORFNames=CBG04031;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q4VT38-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q4VT38-2; Sequence=VSP_038479, VSP_038480;
CC -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR EMBL; AY634292; AAW02898.1; -; Genomic_DNA.
DR EMBL; HE600906; CAP24825.3; -; Genomic_DNA.
DR RefSeq; XP_002639438.1; XM_002639392.1. [Q4VT38-1]
DR AlphaFoldDB; Q4VT38; -.
DR SMR; Q4VT38; -.
DR STRING; 6238.CBG04031; -.
DR EnsemblMetazoa; CBG04031.1; CBG04031.1; WBGene00026779. [Q4VT38-1]
DR GeneID; 8581431; -.
DR KEGG; cbr:CBG_04031; -.
DR CTD; 8581431; -.
DR WormBase; CBG04031; CBP14855; WBGene00026779; Cbr-gpa-14.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_2_1_1; -.
DR InParanoid; Q4VT38; -.
DR OMA; ACMESVF; -.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; 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 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 Alternative splicing; GTP-binding; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transducer.
FT CHAIN 1..408
FT /note="Guanine nucleotide-binding protein alpha-14 subunit"
FT /id="PRO_0000203652"
FT DOMAIN 70..408
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 73..86
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 214..222
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 237..246
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 321..328
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 378..383
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 38..45
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 78..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 85
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 216..222
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 241..245
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 285..288
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 325..328
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_038479"
FT VAR_SEQ 36..51
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_038480"
SQ SEQUENCE 408 AA; 46387 MW; 3297FD4B7C33973E CRC64;
MFSCFNNLGL DYCYQCMHGP EGCMVPSRQG DGGELYAHSE ELEAKLRGLA KKESLEIEKS
LENDKKTYGS HIKILILGGP SSGKSTIFKQ MQIIHSNGFK TEQELIQYRG LIDTNIRQTY
RQLVSGARVV GISLESLESL VHDINKVYAP MAADEFSIRT IPDVVEPLTA FWNSREIQEV
YKRRYEFELL DSTKYYLENL NRISKSDYLP NEEDIVHSRK ATVSINSIVF QYTGVSLLMV
DVGGQRSERK KWLHLFDDAK VVIFVIDLTG YAKKSEESRT ELSRFPNFFN EIGNDAFDMK
VALKIFNDVA GSHALANAVF LLFFNKVDLF KELLPQVSLQ PCFSKFAEEN SYDNTSKFIC
DKFIRAAKPK KSVFPHFTTA TNTENIKMVF RACMESVFKA NSKATGLS
