ID   GB0_LYMST      STANDARD;      PRT;   353 AA.
AC   P30683;
DT   01-APR-1993 (Rel. 25, Created)
DT   01-OCT-1994 (Rel. 30, Last sequence update)
DT   01-OCT-2000 (Rel. 40, Last annotation update)
DE   GUANINE NUCLEOTIDE-BINDING PROTEIN G(O), ALPHA SUBUNIT.
OS   Lymnaea stagnalis (Great pond snail).
OC   Eukaryota; Metazoa; Mollusca; Gastropoda; Pulmonata; Basommatophora;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=CNS;
RX   MEDLINE=93106153; PubMed=1468550;
RA   Knol J.C., Weidemann W., Planta R.J., Vreugdenhil E.,
RA   van Heerikhuizen H.;
RT   "Molecular cloning of G protein alpha subunits from the central
RT   nervous system of the mollusc Lymnaea stagnalis.";
RL   FEBS Lett. 314:215-219(1992).
CC   -!- FUNCTION: GUANINE NUCLEOTIDE-BINDING PROTEINS (G PROTEINS) ARE
CC       INVOLVED AS MODULATORS OR TRANSDUCERS IN VARIOUS TRANSMEMBRANE
CC       SIGNALING SYSTEMS.
CC   -!- FUNCTION: THE G(O) PROTEIN FUNCTION IS NOT CLEAR.
CC   -!- SUBUNIT: G PROTEINS ARE COMPOSED OF 3 UNITS (ALPHA, BETA & GAMMA).
CC       THE ALPHA CHAIN CONTAINS THE GUANINE NUCLEOTIDE BINDING SITE.
CC   -!- SIMILARITY: BELONGS TO THE G-ALPHA FAMILY. SUBFAMILY 1
CC       (G(I/O/T/Z)).
CC   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC   or send an email to license@isb-sib.ch).
CC   --------------------------------------------------------------------------
DR   EMBL; Z15094; CAA78806.1; -.
DR   PIR; S25589; S25589.
DR   PIR; S27014; S27014.
DR   HSSP; P04896; 1AZT.
DR   INTERPRO; IPR001019; -.
DR   INTERPRO; IPR001408; -.
DR   PFAM; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
KW   GTP-binding; Transducer; Multigene family; ADP-ribosylation;
KW   Myristate; Palmitate; Lipoprotein.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID         2      2       PALMITATE (BY SIMILARITY).
FT   NP_BIND      39     46       GTP (BY SIMILARITY).
FT   NP_BIND     200    203       GTP (BY SIMILARITY).
FT   NP_BIND     269    272       GTP (BY SIMILARITY).
FT   MOD_RES     178    178       ADP-RIBOSYL[1] (BY ACTION OF CTX)
FT                                (BY SIMILARITY).
FT   MOD_RES     350    350       ADP-RIBOSYL[1] (BY ACTION OF IAP)
FT                                (BY SIMILARITY).
SQ   SEQUENCE   353 AA;  40140 MW;  01925758C05F654E CRC64;
     GCTLSAEERA AMERSKAIEK NLKEDGMQAA KDIKLLLLGA GESGKSTIVK QMKIIHEGGF
     TSEDNKQYKP VVYSNTIQSL VAIIRAMGTL SIPFGDNERE SDAKMVLDVI ARMEDTEPFS
     EELLAAMKRL WVDSGVQECL GRANEYQLND SAKYFLDDLD RLGAKDYMPT EQDILRTRVK
     TTGIVEVHFS FKNLNFKLFD VGGQRSERKK WIHCFEDVTA IIFCVAMSEY DQVLHEDETT
     NRMQESLKLF DSICNNKWFT ETSIILFLNK KDLFEEKIKK SPLTICFPEY TGKQMYQEAS
     AYIQAQFEAK NKSSAKEIYC HQTCATDTNN IQFVFDAVTD VIIANNLRGC GLY
//