GPCRDB: Swiss-Prot entry
ID GNAI1_ORYLA STANDARD; PRT; 353 AA.
AC P87383;
DT 15-DEC-1998 (Rel. 37, Created)
DT 15-DEC-1998 (Rel. 37, 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) (Gi1 alpha subunit) (Gi alpha a).
GN Name=GNAI1;
OS Oryzias latipes (Medaka fish) (Japanese ricefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha;
OC Beloniformes; Adrianichthyidae; Oryziinae; Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Ovary;
RX MEDLINE=98055713; PubMed=9395335 [NCBI, ExPASy, EBI, Israel, Japan];
RA Oba Y., Yoshikuni M., Tanaka M., Mita M., Nagahama Y.;
RT "Inhibitory guanine-nucleotide-binding-regulatory protein alpha
RT subunits in medaka (Oryzias latipes) oocytes -- cDNA cloning and
RT decreased expression of proteins during oocyte maturation.";
RL Eur. J. Biochem. 249:846-853(1997).
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; AB001741; BAA19454.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P87383; 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 SMART; SM00275; G_alpha; 1.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P87383.
DR ProtoNet; P87383.
DR ProtoMap; P87383.
DR PRESAGE; P87383.
DR DIP; P87383.
DR ModBase; P87383.
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 (By similarity).
FT MOD_RES 350 350 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 353 AA; 40150 MW; FBD5A91D0D69DFC0 CRC64;
GCTLSTDDKA AQERSKMIDR NLRDDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEAGY
SEEECKQYKA VVYSNTIQSI IAIIRAMGRL KIDFADQARA DDARQLFILA GSTEEGFMTG
ELAGVIQRLW KDGGVQACFS RSREYQLNDS AAYYLNDLDR ISHASYVPTQ QDVLRTRVKT
TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
GMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKKS LLTICFPEYA GSNTYEEAAA
YVQCQFEDLN KRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKDC GLF
//