GPA1_CANAW
ID GPA1_CANAW Reviewed; 429 AA.
AC P28868; C4YS30;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 5.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha;
GN Name=CAG1; ORFNames=CAWG_04888;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=1569935; DOI=10.1128/mcb.12.5.1977-1985.1992;
RA Sadhu C., Hoekstra D., McEachern M.J., Reed S.I., Hicks J.B.;
RT "A G-protein alpha subunit from asexual Candida albicans functions in the
RT mating signal transduction pathway of Saccharomyces cerevisiae and is
RT regulated by the a1-alpha 2 repressor.";
RL Mol. Cell. Biol. 12:1977-1985(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. Involved in the mating pathway.
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. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; M88113; AAA34324.2; -; Genomic_DNA.
DR EMBL; CM000311; EEQ46533.1; -; Genomic_DNA.
DR PIR; A44384; A44384.
DR AlphaFoldDB; P28868; -.
DR SMR; P28868; -.
DR STRING; 5476.P28868; -.
DR PRIDE; P28868; -.
DR EnsemblFungi; EEQ46533; EEQ46533; CAWG_04888.
DR VEuPathDB; FungiDB:CAWG_04888; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR OMA; QVIWADA; -.
DR Proteomes; UP000001429; Chromosome 5.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR002975; Fungi_Gprotein_alpha.
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 PRINTS; PR01241; GPROTEINAFNG.
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; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..429
FT /note="Guanine nucleotide-binding protein subunit alpha"
FT /id="PRO_0000203595"
FT DOMAIN 40..429
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 43..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 125..197
FT /note="Not present in other G-proteins"
FT REGION 249..257
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 272..281
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 341..348
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 399..404
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:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 276..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 345..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 131
FT /note="D -> S (in Ref. 1; AAA34324)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="F -> V (in Ref. 1; AAA34324)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="E -> V (in Ref. 1; AAA34324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 49203 MW; 82EE05F3682CB5F0 CRC64;
MGCGASVPVD DDEIDPFLQD KRINDAIEQS LQLRQQNSKK GVKLLLLGAG ESGKSTVLKQ
LKLLHKGGFT QQERRQYSHV IWCDVIQSMK VLIIQARKLK IKLDCDQPNN SLIPYKQIIL
RSDPLKQIDA DVAGGTDFLN DFVVKYSEEN KNKRRLKSTG TTDIWGKDDD SNINSDAINQ
ALESSLNKDS EQFTRLSIAE AIHKLWKLDS GIKKCFDRSN EFQLEGSADY YFDNVFNFAD
TNYLSTDLDI LKGRIKTTGI TETDFLIKSF QFKVLDAGGQ RSERKKWIHC FEDITAVLFV
LAISEYDQNL FEDERVNRMH ESIVLFDSLC NSKWFANTPF ILFLNKIDIF ENKIKKNPLK
NYFPDYDGKP DDTNEAIKFF ETNFLKINQT NKPIYVHRTC ATDSKSMKFV LSAVTDMIVQ
QNLKKSGIM
