ID B7ZR45_XENLA Unreviewed; 379 AA.
AC B7ZR45;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Adenylate cyclase-stimulating G alpha protein {ECO:0000256|ARBA:ARBA00042247};
GN Name=gnas-a {ECO:0000313|EMBL:AAI70038.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI70038.1};
RN [1] {ECO:0000313|EMBL:AAI70038.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000313|EMBL:AAI70038.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000256|ARBA:ARBA00007172}.
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DR EMBL; BC170038; AAI70038.1; -; mRNA.
DR AlphaFoldDB; B7ZR45; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.10.400.10; GI Alpha 1, domain 2-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR000367; Gprotein_alpha_S.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1.
DR PANTHER; PTHR10218:SF365; GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA XL; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00443; GPROTEINAS.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 44514 MW; C3463AC46C8A924E CRC64;
MGCLGNSKTE DQRNEEKAQR EANKKIEKQL QKDKQVYRAT HRLLLLGAGE SGKSTIVKQM
RILHVNGFNA EEKKIKVQDI KNNIKEAIET IVTAMGNLSP PVELVNPENQ FRIDYILNLP
NYKDFEFSPE FYEHTKTLWQ DEGVRACYER SNEYQLIDCA QYFLDKIDIV KQNDYTPSDQ
DLLRCRVLTS GIFETKFQVD KVNFHMFDVG GQRDERRKWI QCFNDVTAII FVVASSSYNM
VIREDNHTNR LQEALNLFKS IWNNRWLRTI SVILFLNKQD LLAEKVNAGK SKIEDYFPEF
ARYTTPDDAT PEVGEDPRVT RAKYFIRDEF LRISTASGDG RHYCYPHFTC AVDTENIRRV
FNDCRDIIQR MHLRQYELL
//
