GPCRDB: Swiss-Prot entry

ID   GNAI2_CHICK    STANDARD;      PRT;   354 AA.
AC   P50147;
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-2 subunit (Adenylate
DE   cyclase-inhibiting G alpha protein).
GN   Name=GNAI2;
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; L24549; AAA65067.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   PIR; I50238; I50238.
DR   HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P50147; 4-353.
DR   Ensembl; ENSGALG00000004639; 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; P50147.
DR   ProtoNet; P50147.
DR   ProtoMap; P50147.
DR   PRESAGE; P50147.
DR   DIP; P50147.
DR   ModBase; P50147.
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     200    204       GTP (By similarity).
FT   NP_BIND     269    272       GTP (By similarity).
FT   MOD_RES     178    178       ADP-ribosylarginine (by cholera toxin).
FT   MOD_RES     351    351       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   354 AA;  40446 MW;  D9645493D9C5CC4F CRC64;
     GCTVSAEDKA AAERSRMIDR NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEDGY
     SEEECRQYKA VVYSNTIQSI MAIIKAMGNL QIDFGDSSRA DDARQLFALA CTAEEQGIMP
     EDLANVIRRL WADHGVQACF NRSREYQLND SAAYYLNDLE RIARADYIPT QQDVLRTRVK
     TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSAY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIVH SPLTICFPEY TGANKYDEAA
     GYIQSKFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
//