GPA2_NEUCR
ID GPA2_NEUCR Reviewed; 355 AA.
AC Q05424; Q7S787; Q9URK0; V5ILJ1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Guanine nucleotide-binding protein alpha-2 subunit;
DE AltName: Full=GP2-alpha;
GN Name=gna-2; ORFNames=B11H7.130, NCU06729;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8325859; DOI=10.1016/s0021-9258(18)82405-x;
RA Borkovich K.A., Turner G.E.;
RT "Identification of a G protein alpha subunit from Neurospora crassa that is
RT a member of the Gi family.";
RL J. Biol. Chem. 268:14805-14811(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=9286674; DOI=10.1093/genetics/147.1.137;
RA Baasiri R.A., Lu X., Rowley P.S., Turner G.E., Borkovich K.A.;
RT "Overlapping functions for two G protein alpha subunits in Neurospora
RT crassa.";
RL Genetics 147:137-145(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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 -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC {ECO:0000305}.
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DR EMBL; L11452; AAA02559.1; -; mRNA.
DR EMBL; AF004846; AAD01207.1; -; Genomic_DNA.
DR EMBL; BX294092; CAD71253.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42608.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42609.1; -; Genomic_DNA.
DR PIR; T50479; T50479.
DR RefSeq; XP_011394709.1; XM_011396407.1.
DR RefSeq; XP_011394710.1; XM_011396408.1.
DR AlphaFoldDB; Q05424; -.
DR SMR; Q05424; -.
DR STRING; 5141.EFNCRP00000006662; -.
DR EnsemblFungi; ESA42608; ESA42608; NCU06729.
DR EnsemblFungi; ESA42609; ESA42609; NCU06729.
DR GeneID; 3876804; -.
DR KEGG; ncr:NCU06729; -.
DR VEuPathDB; FungiDB:NCU06729; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; Q05424; -.
DR BRENDA; 3.6.5.1; 3627.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IEA:EnsemblFungi.
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:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0071507; P:pheromone response MAPK cascade; IEA:EnsemblFungi.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; 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; 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 2: Evidence at transcript level;
KW GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transducer.
FT CHAIN 1..355
FT /note="Guanine nucleotide-binding protein alpha-2 subunit"
FT /id="PRO_0000203606"
FT DOMAIN 33..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..49
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 326..331
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 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
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 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 19..20
FT /note="EL -> DV (in Ref. 2; AAD01207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 41361 MW; 61733B89EABB7409 CRC64;
MCFGGRGKDD EAEASRSREL DKQIRADEKR LSKEVKLLLL GAGESGKSTI LKQMKLIYAQ
GFSKNEKLEW RPVIFANILQ SFRLIFDAMN EFNIKLEDED NEKNMVQMMV DYEMRGDEPL
PLEYFEPAKK LWQDSGVRQA IEKGNEFALH DNLQYFCSDL DRLWDRNYVP SDQDLLRSRL
RTTGITETVF DLGQLTYRMF DVGGQRSERK KWIHCFENVN CLLFLVAISG YDQCLVEDKD
GNQMNEALML WESIANSHWF TKSALILFLN KIDLFKEKLP RSPITNHGFT DYHGPPDDSK
QASKYFMDKF RALNRNPDKE IYGHFTNATD TNLLKITMGS VQDMIIQRNL KQLIL
