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   03-AUG-2022, entry version 102.
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}.
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DR   EMBL; X66378; CAA47019.1; -; mRNA.
DR   PIR; S24362; S24362.
DR   AlphaFoldDB; P30676; -.
DR   SMR; P30676; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; PTHR10218; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
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   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