GPCRDB: Swiss-Prot entry

ID   GNAI1_CHICK    STANDARD;      PRT;   353 AA.
AC   P50146;
DT   01-OCT-1996 (Rel. 34, Created)
DT   01-OCT-1996 (Rel. 34, 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   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; 
OC   Gallus. 
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=95121926; PubMed=7821803 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0378-1119(94)90449-9;
RA   Kilbourne E.J., Galper J.B.;
RT   "Cloning of cDNAs coding for the G alpha i1 and G alpha i2 G-proteins
RT   from chick brain.";
RL   Gene 150:341-344(1994).
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; L24548; AAA65066.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; I50237; I50237.
DR   HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P50146; 4-347.
DR   Ensembl; ENSGALG00000008382; Gallus_gallus
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; P50146.
DR   ProtoNet; P50146.
DR   ProtoMap; P50146.
DR   PRESAGE; P50146.
DR   DIP; P50146.
DR   ModBase; P50146.
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;  40247 MW;  E1DD0C848140137C CRC64;
     GCTLSAEDKA AVERSKMIDR NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEAGY
     SEEECKQYKA VVYSNTIQSI IAIIRAMGRL KIDFGDPTRA DDARQLFVLA GAAEEGFMTA
     DVAGVIKRLW KDSGVQACFN RSREYQLNDS AAYYLNDLDR IAQTSYIPTQ QDVLRTRVKT
     TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
     RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKRS PLTICYPEYA GSNTYEEAAA
     YIQCQFEDLN KRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKDC GLF
//