GPCRDB: Swiss-Prot entry
ID GNAI2_HUMAN STANDARD; PRT; 354 AA.
AC P04899;
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-2 subunit (Adenylate
DE cyclase-inhibiting G alpha protein).
GN Name=GNAI2;
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.
RX MEDLINE=87105966; PubMed=3100330 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0014-5793(87)81428-X;
RA Didsbury J.R., Ho Y.-S., Snyderman R.;
RT "Human Gi protein alpha-subunit: deduction of amino acid structure
RT from a cloned cDNA.";
RL FEBS Lett. 211:160-164(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
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 [3]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=88068503; PubMed=3120178 [NCBI, ExPASy, EBI, Israel, Japan];
RA Beals C.R., Wilson C.B., Perlmutter R.M.;
RT "A small multigene family encodes Gi signal-transduction proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7886-7890(1987).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 OF 1-38.
RX MEDLINE=88242822; PubMed=2837412 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0014-5793(88)80764-6;
RA Weinstein L.S., Spiegel A.M., Carter A.D.;
RT "Cloning and characterization of the human gene for the alpha-subunit
RT of Gi2, a GTP-binding signal transduction protein.";
RL FEBS Lett. 232:333-340(1988).
RN [7]
RP INTERACTION WITH UNC5B.
RX MEDLINE=22246081; PubMed=12359238 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0006-291X(02)02277-5;
RA Komatsuzaki K., Dalvin S., Kinane T.B.;
RT "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule
RT UNC5H2.";
RL Biochem. Biophys. Res. Commun. 297:898-905(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. Interacts with UNC5B.
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; X04828; CAA28512.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X07854; CAA30703.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20593; AAA35894.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20586; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20587; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20588; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20589; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20590; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20591; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; M20592; AAA35894.1; JOINED; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF493906; AAM12620.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC012138; AAH12138.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; J03004; AAA52556.1; ALT_SEQ; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S02319; RGHUI2.
DR HSSP; P10824; 1AS3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P04899; 4-353.
DR IntAct; P04899; -.
DR Ensembl; ENSG00000114353; Homo_sapiens
DR Genew; HGNC:4385; GNAI2.
DR CleanEx; HGNC:4385; GNAI2.
DR H-InvDB; HIX0003320; -.
DR MIM; 139360; -. [NCBI / EBI]
DR GeneCards; GNAI2.
DR GeneLynx; GNAI2.
DR GenAtlas; GNAI2.
DR SOURCE; GNAI2.
DR GO; GO:0003924; F:GTPase activity; TAS.
DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase ac...; TAS.
DR GO; GO:0007584; P:response to nutrients; TAS.
DR GO; GO:0007165; P:signal transduction; TAS.
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 CMR; P04899.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; P04899.
DR ProtoNet; P04899.
DR ProtoMap; P04899.
DR PRESAGE; P04899.
DR DIP; P04899.
DR ModBase; P04899.
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; 40320 MW; 6E66B102DA0088EB CRC64;
GCTVSAEDKA AAERSKMIDK NLREDGEKAA REVKLLLLGA GESGKSTIVK QMKIIHEDGY
SEEECRQYRA VVYSNTIQSI MAIVKAMGNL QIDFADPSRA DDARQLFALS CTAEEQGVLP
DDLSGVIRRL WADHGVQACF GRSREYQLND SAAYYLNDLE RIAQSDYIPT QQDVLRTRVK
TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSAY DLVLAEDEEM
NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKITH SPLTICFPEY TGANKYDEAA
SYIQSKFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
//