ID V4ACM4_LOTGI Unreviewed; 375 AA.
AC V4ACM4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Adenylate cyclase-stimulating G alpha protein {ECO:0000256|ARBA:ARBA00042247};
GN ORFNames=LOTGIDRAFT_163596 {ECO:0000313|EMBL:ESO91071.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO91071.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO91071.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC {ECO:0000256|ARBA:ARBA00011356}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC {ECO:0000256|ARBA:ARBA00007172}.
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DR EMBL; KB202284; ESO91071.1; -; Genomic_DNA.
DR RefSeq; XP_009058340.1; XM_009060092.1.
DR AlphaFoldDB; V4ACM4; -.
DR STRING; 225164.V4ACM4; -.
DR EnsemblMetazoa; LotgiT163596; LotgiP163596; LotgiG163596.
DR GeneID; 20239462; -.
DR KEGG; lgi:LOTGIDRAFT_163596; -.
DR CTD; 20239462; -.
DR HOGENOM; CLU_014184_3_0_1; -.
DR OMA; DHVAKCW; -.
DR OrthoDB; 2897309at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
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:SF212; G PROTEIN ALPHA S SUBUNIT; 1.
DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 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 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Transducer {ECO:0000256|ARBA:ARBA00023224}.
SQ SEQUENCE 375 AA; 44258 MW; 7B2EB3720105AD7E CRC64;
MGCFRRKEDE DEKVRKEANK RIEKQLQKDK QLYRATHRLL LLGAGESGKS TIVKQMRILH
VNGFGPDERK QKIEDIKRNI KDAILTITGA MSTLNPPATL ENPDNQFRVD YIQDVASQPD
FDYPPEFYEH TEILWKDKGV QGCFERSNEY QLIDCAQYFL DRVHIVKESD YTPTEQDILR
CRVLTSGIFE TRFTVDKVNF HMFDVGGQRD ERRKWIQCFN DVTAIIFVTA CSGYNLVLRE
DPSQNRLRES LDLFRSIWNN RWLRTISVIL FLNKQDLLAQ KVMGGRSRIE DYFPDYVRYQ
TPFDAVSEVG DDPEVVRAKY FIRDEFLRIS TASGEGRHYC YPHFTCAVDT ENIRRVFNDC
RDIIQRMHLR QYELL
//
