ID GNAI_PATPE Reviewed; 354 AA. AC P30676; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 111. DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha; DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein; OS Patiria pectinifera (Starfish) (Asterina pectinifera). OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea; OC Valvatacea; Valvatida; Asterinidae; Patiria. OX NCBI_TaxID=7594; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Ovary; RX PubMed=1499560; DOI=10.1111/j.1432-1033.1992.tb17114.x; RA Chiba K., Tadenuma H., Matsumoto M., Takahashi K., Katada T., Hoshi M.; RT "The primary structure of the alpha subunit of a starfish guanosine- RT nucleotide-binding regulatory protein involved in 1-methyladenine-induced RT oocyte maturation."; RL Eur. J. Biochem. 207:833-838(1992). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved CC as modulators or transducers in various transmembrane signaling CC systems. This G protein is involved in 1-methyladenine-induced oocyte CC maturation. 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(i/o/t/z) subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X66378; CAA47019.1; -; mRNA. DR PIR; S24362; S24362. DR AlphaFoldDB; P30676; -. DR SMR; P30676; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:TreeGrafter. DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:TreeGrafter. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro. DR CDD; cd00066; G-alpha; 1. DR FunFam; 3.40.50.300:FF:000563; Guanine nucleotide-binding protein alpha subunit; 1. DR FunFam; 1.10.400.10:FF:000001; Guanine nucleotide-binding protein G(I) subunit alpha; 1. DR FunFam; 3.40.50.300:FF:003559; Guanine nucleotide-binding protein G(i) subunit alpha-1; 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; IPR001408; Gprotein_alpha_I. DR InterPro; IPR001019; Gprotein_alpha_su. DR InterPro; IPR011025; GproteinA_insert. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10218:SF227; G PROTEIN ALPHA I SUBUNIT; 1. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. 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 1: Evidence at protein level; KW Direct protein sequencing; GTP-binding; Lipoprotein; Magnesium; KW Metal-binding; Myristate; Nucleotide-binding; Palmitate; Transducer. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..354 FT /note="Guanine nucleotide-binding protein G(i) subunit FT alpha" FT /id="PRO_0000203685" FT DOMAIN 32..354 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 35..48 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 173..181 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 196..205 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 40..47 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 175..181 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 200..204 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 LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000255" SQ SEQUENCE 354 AA; 40043 MW; E242F5BB911B05E1 CRC64; MGCATSAEDK AAAERSKAID RNLRIDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEEG YSEEDCKQYK PVVYSNTIQS MIAIIRAMGS LKVDFGDGDR TDDARQLFAL AGQAEEGELS PELAAVMKRL WADGGVQGCF SRSREYQLND SASYYLNALD RLAAPGYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSAY DLVLAEDEEM NRMHESMKLF DSICNNKWFT ETSIILFLNK KDLFEEKITK SPLTICFPEY TGSNTYEEAA AYIQMQFEDL NKRKDQKEIY THFTCATDTN NIQFVFDAVT DVIIKNNLKD CGLF //