GPA2_SCHPO
ID GPA2_SCHPO Reviewed; 354 AA.
AC Q04665;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
DE AltName: Full=GP2-alpha;
GN Name=gpa2; ORFNames=SPAC23H3.13c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-176 AND GLN-202.
RX PubMed=1340462; DOI=10.1101/gad.6.12b.2455;
RA Isshiki T., Mochizuki N., Maeda T., Yamamoto M.;
RT "Characterization of a fission yeast gene, gpa2, that encodes a G alpha
RT subunit involved in the monitoring of nutrition.";
RL Genes Dev. 6:2455-2462(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
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DR EMBL; D13366; BAA02630.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16244.1; -; Genomic_DNA.
DR PIR; A46393; A46393.
DR PIR; T38306; T38306.
DR RefSeq; NP_593803.1; NM_001019232.2.
DR AlphaFoldDB; Q04665; -.
DR SMR; Q04665; -.
DR BioGRID; 278214; 86.
DR STRING; 4896.SPAC23H3.13c.1; -.
DR MaxQB; Q04665; -.
DR PaxDb; Q04665; -.
DR EnsemblFungi; SPAC23H3.13c.1; SPAC23H3.13c.1:pep; SPAC23H3.13c.
DR GeneID; 2541720; -.
DR KEGG; spo:SPAC23H3.13c; -.
DR PomBase; SPAC23H3.13c; gpa2.
DR VEuPathDB; FungiDB:SPAC23H3.13c; -.
DR eggNOG; KOG0082; Eukaryota.
DR HOGENOM; CLU_014184_0_1_1; -.
DR InParanoid; Q04665; -.
DR OMA; AVTYLWN; -.
DR PhylomeDB; Q04665; -.
DR Reactome; R-SPO-112043; PLC beta mediated events.
DR Reactome; R-SPO-202040; G-protein activation.
DR Reactome; R-SPO-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-SPO-399997; Acetylcholine regulates insulin secretion.
DR Reactome; R-SPO-416476; G alpha (q) signalling events.
DR Reactome; R-SPO-416482; G alpha (12/13) signalling events.
DR Reactome; R-SPO-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-SPO-434316; Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
DR Reactome; R-SPO-9013148; CDC42 GTPase cycle.
DR PRO; PR:Q04665; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0010856; F:adenylate cyclase activator activity; IDA:PomBase.
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; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0010515; P:negative regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:PomBase.
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 1: Evidence at protein level;
KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transducer.
FT CHAIN 1..354
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203609"
FT DOMAIN 33..354
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 36..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 171..179
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 194..203
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 265..272
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 324..329
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 41..48
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 173..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198..202
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MUTAGEN 176
FT /note="R->H: Decrease in mating and sporulation
FT efficiency."
FT /evidence="ECO:0000269|PubMed:1340462"
FT MUTAGEN 202
FT /note="Q->L: Decrease in mating and sporulation
FT efficiency."
FT /evidence="ECO:0000269|PubMed:1340462"
SQ SEQUENCE 354 AA; 40523 MW; A0042174C1389B8A CRC64;
MTIFNGLSES GESKKLNSKI EKQIENASKK DKKIYKVLLL GASDSGKSTI SKQIKILNKN
GFSQEEIMTF IPVIRRNLLE SAKTLVKIIV QKGINLDPLG THNCEIIEKF NPTPGELINA
NIGQAITSLW SANSVRSCTY GNDSVLIDSA PYFFSRADEI CSRHYVPTID DILRSRNSTL
GISEISFTLD HLQIRMFDVG GQRTERRKWI YCFENVNSII FCVSLNDYDK KLYERAAPER
NRLVESISLF DSIINSQWFM HSSIILFLNK FDLFRKKLEH VPFQDYFPQY EGKNSVKSIT
RYILWLFVNP SINRAKHNIY PHITTAVDTS NIKVVFSAVK ETILQHSLKE AGMF
