GPCRDB: Swiss-Prot entry

ID   GNAI1_XENLA    STANDARD;      PRT;   353 AA.
AC   P27044;
DT   01-AUG-1992 (Rel. 23, Created)
DT   01-OCT-1994 (Rel. 30, Last sequence update)
DT   10-MAY-2005 (Rel. 47, Last annotation update)
DE   Guanine nucleotide-binding protein G(i), alpha-1 subunit (Adenylate
DE   cyclase-inhibiting G alpha protein).
GN   Name=GNAI1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; 
OC   Xenopodinae; Xenopus; Xenopus. 
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Oocyte;
RX   MEDLINE=90346157; PubMed=2116977 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0014-5793(90)80964-K;
RA   Olate J., Martinez S., Purcell P., Jorquera H., Codina J.,
RA   Birnbaumer L., Allende J.E.;
RT   "Molecular cloning and sequence determination of four different cDNA
RT   species coding for alpha-subunits of G proteins from Xenopus laevis
RT   oocytes.";
RL   FEBS Lett. 268:27-31(1990).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. The G(i) proteins are involved in hormonal
CC       regulation of adenylate cyclase: they inhibit the cyclase in
CC       response to beta-adrenergic stimuli.
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.
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 as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; X56089; CAA39569.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; S11045; RGXLI1.
DR   HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P27044; 4-347.
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   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P27044.
DR   ProtoNet; P27044.
DR   ProtoMap; P27044.
DR   PRESAGE; P27044.
DR   DIP; P27044.
DR   ModBase; P27044.
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     199    203       GTP (By similarity).
FT   NP_BIND     268    271       GTP (By similarity).
FT   MOD_RES     177    177       ADP-ribosylarginine (by cholera toxin).
FT   MOD_RES     350    350       ADP-ribosylcysteine (by pertussis toxin).
FT   LIPID         1      1       N-myristoyl glycine (By similarity).
FT   LIPID         2      2       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   353 AA;  40270 MW;  6B4EE94F841B077D CRC64;
     GCTLSAEDKA AVERSKMIDR NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEAGY
     SEEECKQYKA VVYSNTIQSI IAIIRAMGRL KIDFGDPSRA DDARQLFVLA GAAEEGFMTA
     ELAGVIKRLW KDGGVQACFN RSREYQLNDS AAYYLNDLDR IAQNSYIPTQ QDVLRTRVKT
     TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
     RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYP GSNTYEEAAA
     YIQCQFEDLN KRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKDC GLF
//