GPCRDB: Swiss-Prot entry
ID GNAI1_HUMAN STANDARD; PRT; 353 AA.
AC P63096; P04898; P11015; P31871; Q5U074; Q8TAN5; Q9UGA4;
DT 13-AUG-1987 (Rel. 05, 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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX MEDLINE=21154917; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1101/gr.154701;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX MEDLINE=88198230; PubMed=2834384 [NCBI, ExPASy, EBI, Israel, Japan];
RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.;
RT "Presence of three distinct molecular species of Gi protein alpha
RT subunit. Structure of rat cDNAs and human genomic DNAs.";
RL J. Biol. Chem. 263:6656-6664(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-353.
RX MEDLINE=87260939; PubMed=3110783 [NCBI, ExPASy, EBI, Israel, Japan];
RA Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A.,
RA Nirenberg M.;
RT "Human cDNA clones for an alpha subunit of Gi signal-transduction
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987).
RN [8]
RP PROTEIN SEQUENCE OF 90-99 AND 161-175.
RC TISSUE=Adipocyte;
RX PubMed=15242332 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1042/BJ20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at
RT the surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 30-348 IN COMPLEX WITH RGS14.
RX MEDLINE=21973246; PubMed=11976690 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/416878a;
RA Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.;
RT "Structural determinants for GoLoco-induced inhibition of nucleotide
RT release by Galpha subunits.";
RL Nature 416:878-881(2002).
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; AF493905; AAM12619.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF055013; AAC09361.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL049933; CAB43212.2; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BT019775; AAV38580.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC026326; AAH26326.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20596; AAA35893.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20594; AAA35893.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20595; AAA35893.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M17219; AAA52581.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A28318; RGHUI1.
DR PDB; 1KJY; X-ray; A/C=30-353. [ExPASy / RCSB]
DR SMR; P63096; 31-346.
DR Ensembl; ENSG00000127955; Homo_sapiens
DR Genew; HGNC:4384; GNAI1.
DR CleanEx; HGNC:4384; GNAI1.
DR MIM; 139310; -. [NCBI / EBI]
DR GeneCards; GNAI1.
DR GeneLynx; GNAI1.
DR GenAtlas; GNAI1.
DR SOURCE; GNAI1.
DR InterPro; IPR001019; Gprotein_alpha.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00503; G-alpha; 1.
DR Pfam; Graphical view of domain structure.
DR CMR; P63096.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P63096.
DR ProtoNet; P63096.
DR ProtoMap; P63096.
DR PRESAGE; P63096.
DR DIP; P63096.
DR ModBase; P63096.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW 3D-structure; ADP-ribosylation; Direct protein sequencing;
KW GTP-binding; Lipoprotein; Multigene family; Myristate; Palmitate;
KW 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).
FT CONFLICT 137 137 A -> G (in Ref. 3).
FT CONFLICT 218 218 T -> A (in Ref. 5).
FT CONFLICT 243 243 H -> Y (in Ref. 4).
FT CONFLICT 248 248 L -> M (in Ref. 4).
FT CONFLICT 287 287 P -> Q (in Ref. 5).
FT STRAND 32 38
FT TURN 41 42
FT HELIX 45 55
FT HELIX 62 65
FT HELIX 66 68
FT HELIX 69 89
FT TURN 90 91
FT TURN 97 98
FT HELIX 99 112
FT TURN 115 116
FT HELIX 120 131
FT HELIX 133 139
FT TURN 140 141
FT HELIX 142 144
FT TURN 149 150
FT HELIX 151 155
FT TURN 156 157
FT HELIX 158 161
FT TURN 164 165
FT HELIX 170 175
FT STRAND 184 190
FT TURN 191 192
FT STRAND 193 199
FT HELIX 207 214
FT TURN 215 216
FT STRAND 219 225
FT HELIX 226 230
FT TURN 235 236
FT HELIX 241 254
FT HELIX 256 258
FT TURN 259 260
FT STRAND 264 268
FT HELIX 270 276
FT TURN 277 279
FT HELIX 282 284
FT TURN 285 285
FT TURN 287 288
FT HELIX 295 307
FT TURN 308 309
FT TURN 311 315
FT STRAND 319 322
FT TURN 325 326
FT HELIX 328 344
FT TURN 345 345
SQ SEQUENCE 353 AA; 40230 MW; B456C4E189530A6D CRC64;
GCTLSAEDKA AVERSKMIDR NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEAGY
SEEECKQYKA VVYSNTIQSI IAIIRAMGRL KIDFGDSARA DDARQLFVLA GAAEEGFMTA
ELAGVIKRLW KDSGVQACFN RSREYQLNDS AAYYLNDLDR IAQPNYIPTQ QDVLRTRVKT
TGIVETHFTF KDLHFKMFDV GGQRSERKKW IHCFEGVTAI IFCVALSDYD LVLAEDEEMN
RMHESMKLFD SICNNKWFTD TSIILFLNKK DLFEEKIKKS PLTICYPEYA GSNTYEEAAA
YIQCQFEDLN KRKDTKEIYT HFTCATDTKN VQFVFDAVTD VIIKNNLKDC GLF
//