GPA1_KLULA
ID GPA1_KLULA Reviewed; 447 AA.
AC Q9Y7B7; Q6CIK5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE AltName: Full=GP1-alpha;
GN Name=GPA1; OrderedLocusNames=KLLA0F25916g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=11114921; DOI=10.1128/jb.183.1.229-234.2001;
RA Savinon-Tejeda A.L., Ongay-Larios L., Valdes-Rodriguez J., Coria R.;
RT "The KlGpa1 gene encodes a G-protein alpha subunit that is a positive
RT control element in the mating pathway of the budding yeast Kluyveromyces
RT lactis.";
RL J. Bacteriol. 183:229-234(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. This protein is involved in the mating response 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. {ECO:0000305}.
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DR EMBL; AF135552; AAD33674.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98942.1; -; Genomic_DNA.
DR RefSeq; XP_456234.1; XM_456234.1.
DR AlphaFoldDB; Q9Y7B7; -.
DR SMR; Q9Y7B7; -.
DR STRING; 28985.XP_456234.1; -.
DR EnsemblFungi; CAG98942; CAG98942; KLLA0_F25916g.
DR GeneID; 2894996; -.
DR KEGG; kla:KLLA0_F25916g; -.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_2_0_1; -.
DR InParanoid; Q9Y7B7; -.
DR OMA; QVIWADA; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:EnsemblFungi.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; IEA:EnsemblFungi.
DR GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0000743; P:nuclear migration involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0071701; P:regulation of MAPK export from nucleus; IEA:EnsemblFungi.
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; Pheromone response; Reference proteome;
KW Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..447
FT /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT /id="PRO_0000203602"
FT DOMAIN 40..447
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 267..275
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 290..299
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 359..366
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 417..422
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:0000250"
FT BINDING 269..275
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 294..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 363..366
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 419
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 271
FT /note="G -> V (in Ref. 1; AAD33674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 50938 MW; 29BADC2166158F98 CRC64;
MGCVASTGNY ENEDDPFIQN KRANDLIEQN LQQERNKNKN EVKLLLLGAG ESGKSTVLKQ
MKLLHQGGFT HRERMQYGQV IWADAIESMR TLILQAGKLG IELDSDLKNA HSGQLVNTEL
HQCKEKIFRA NTLDQIDARM AGGSEFLNEY VLKYNGIGSK KKRQTTLGFK ESNGADPEEE
DETDAFLSEK LAGTSYTGSS ETSELKRIDQ STNEEIAYAI KKLWTQDKGI RQCFNRSSEF
QLEGSASYYF DNIEKFARVD YVCDDMDILK GRIKTTGITE NSFKIGPSTF KVYDAGGQRS
ERRKWIHCFE GITAVVFVIA ISEYDQMLFE DERVNRMHES IVLLDTLLNS RWFANTPFIL
FLNKVDIFQE KVKRSPIRTW FPNYPGKLGD SETGLKYFES LFLSLNRSNK PIYVHRTCAT
DTQSMRFVLG AVTDLVIQQN LKKSGIL
