GPCRDB: Swiss-Prot entry

ID   GNAO_PATYE     STANDARD;      PRT;   356 AA.
AC   O15976;
DT   15-JUL-1998 (Rel. 36, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Guanine nucleotide-binding protein G(o), alpha subunit.
GN   Name=SCGOA;
OS   Patinopecten yessoensis (Ezo giant scallop) (Yesso scallop).
OC   Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida; 
OC   Pectinoidea; Pectinidae; Mizuhopecten. 
OX   NCBI_TaxID=6573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Eye;
RX   MEDLINE=97435252; PubMed=9287291 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1074/jbc.272.37.22979;
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A.,
RA   Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual
RT   cells.";
RL   J. Biol. Chem. 272:22979-22989(1997).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. The G(o) protein function is not clear.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
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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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; AB006457; BAA22220.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P04896; 1AZT. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; O15976; 4-355.
DR   InterPro; IPR001019; Gprotein_alpha.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF00503; G-alpha; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   ProDom; PD000281; Gprotein_alpha; 1.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR   BLOCKS; O15976.
DR   ProtoNet; O15976.
DR   ProtoMap; O15976.
DR   PRESAGE; O15976.
DR   DIP; O15976.
DR   ModBase; O15976.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   ADP-ribosylation; GTP-binding; Lipoprotein; Multigene family;
KW   Myristate; Palmitate; Transducer.
FT   INIT_MET      0      0       By similarity.
FT   NP_BIND      39     46       GTP (By similarity).
FT   NP_BIND     203    207       GTP (By similarity).
FT   NP_BIND     272    275       GTP (By similarity).
FT   MOD_RES     181    181       ADP-ribosylarginine (by cholera toxin)
FT                                (By similarity).
FT   MOD_RES     353    353       ADP-ribosylcysteine (by pertussis toxin)
FT                                (By similarity).
FT   LIPID         1      1       N-myristoyl glycine (By similarity).
FT   LIPID         2      2       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   356 AA;  40623 MW;  C668F5E5BDEE376E CRC64;
     GCTMSAEDRA AAERSRDIEK KLKEDGIQAA KDIKLLLLGA GESGKSTIVK QMKIIHEGGF
     TSEDNKQYKP VVYSNTIQSL VAIVRAMSTL NIPYGDNERE EIKSDAKIVL DVIARMEDTE
     PFSEELLAAM KRLWTDTGVQ ECFGRSNEYQ LNDSAKYFLD DLDRLGSKDY MPTEQDILRT
     RVKTTGIVEV HFSFKNLNFK LFDVGGQRSE RKKWIHCFED VTAIIFCVAM SEYDQVLHED
     ETTNRMQESL KLFDNICNNK WFTDTSIILF LNKKDLFEEK IKKSSLTICF NEYTGNQTYE
     EAAAYIQAQF EAKNKSSSKE IYCHQTCATD TNNIQFVFDA VTDVIIANNL RGCGLY
//