GPA2_KLULA
ID GPA2_KLULA Reviewed; 554 AA.
AC P54111; Q6CR89;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
DE AltName: Full=GP2-alpha;
GN Name=GPA2; OrderedLocusNames=KLLA0D10956g;
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 [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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-554.
RC STRAIN=CBS 2359 / IFO 1267 / NRRL Y-1140 / WM37;
RX PubMed=8896279;
RX DOI=10.1002/(sici)1097-0061(19960915)12:11<1125::aid-yea7>3.0.co;2-2;
RA Savinon-Tejeda A., Ongay-Larios L., Ramirez J., Coria R.;
RT "Isolation of a gene encoding a G protein alpha subunit involved in the
RT regulation of cAMP levels in the yeast Kluyveromyces lactis.";
RL Yeast 12:1125-1133(1996).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. This protein may be involved in the determination of the cAMP
CC level according to nutritional conditions, most probably as a regulator
CC of adenylyl cyclase.
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=AAA75112.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR382124; CAH00646.1; -; Genomic_DNA.
DR EMBL; L47105; AAA75112.1; ALT_INIT; Genomic_DNA.
DR PIR; S72195; S72195.
DR RefSeq; XP_453550.1; XM_453550.1.
DR AlphaFoldDB; P54111; -.
DR SMR; P54111; -.
DR STRING; 28985.XP_453550.1; -.
DR EnsemblFungi; CAH00646; CAH00646; KLLA0_D10956g.
DR GeneID; 2893290; -.
DR KEGG; kla:KLLA0_D10956g; -.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_0_0_1; -.
DR InParanoid; P54111; -.
DR OMA; IENCKRM; -.
DR Proteomes; UP000000598; Chromosome D.
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:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IEA:EnsemblFungi.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0010737; P:protein kinase A signaling; IEA:EnsemblFungi.
DR GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..554
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203603"
FT DOMAIN 228..554
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..244
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 374..382
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 398..407
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 467..474
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 524..529
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 26..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236..243
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 376..382
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 471..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 526
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"
SQ SEQUENCE 554 AA; 61459 MW; 5F7064B798B36084 CRC64;
MGLCASKDSR ESTHDGGPRV NRPGANDANR RNDVRKGAGD KKQDKKNKKA KGSIVNAASN
INNSSSGKTK ISTVSEDGTV SNGVGNTAEY DNANNKNNGN NNNSNNNDNN NNNNNNIGNN
INGNNNNDSE NIHDSNNSNI ENKRYFNNIN TGVLNGVNGN STNSDKALSN QFDQSNNSET
HSGTMTGISQ ALALNDSGVN GFDTDLAKRN GTVNASGGQS PGGSETVNAL KVLLLGSGES
GKSTVLQQLK ILHQNGFSRE ELLEYKPFIF DNIIETGKDL AKARRTFNVQ LEEDAEISES
DLDELLSQQY QPTKLPCLPA DLAKTLKILW NLQSTQDLLV SEHRSSFYLM DSASYFYENL
DRISEPKYIP TITDVIRTRK KTSGIFDTMI DLDKNLKLHF FDVGGQRSER KKWIHCFDNV
TLIIFCVSLS EYDQTLLEDN SQNRLEESLI LFDSVVNSRW FARSSVVLFL NKIDIFAEKL
RHVPLEKYFP DYTGGKDINK AAKYILWRFV QLNRANLNIY PHVTQATDTS NIKLVFAAIK
ETILENSLKD SGVL
