GNAZ_MOUSE
ID GNAZ_MOUSE Reviewed; 355 AA.
AC O70443; O70442; Q61637; Q91WM4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Guanine nucleotide-binding protein G(z) subunit alpha;
DE AltName: Full=G(x) alpha chain;
DE AltName: Full=Gz-alpha;
GN Name=Gnaz;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-353.
RC STRAIN=C57BL/6J;
RA Matthaei K.I., Mellick A.M., Hendry I.A.;
RT "Partial genomic sequence of the mouse GTP binding protein Gz alpha.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 207-267.
RC STRAIN=BALB/cJ; TISSUE=Pancreatic islet;
RX PubMed=8013366; DOI=10.1210/endo.135.1.8013366;
RA Zigman J.M., Westermark G.T., LaMendola J., Steiner D.F.;
RT "Expression of cone transducin, Gz alpha, and other G-protein alpha-subunit
RT messenger ribonucleic acids in pancreatic islets.";
RL Endocrinology 135:31-37(1994).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems.
CC -!- SUBUNIT: G-proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. Interacts
CC with ADGRB2 (By similarity). {ECO:0000250|UniProtKB:P19086}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; BC014702; AAH14702.1; -; mRNA.
DR EMBL; AF056973; AAC13569.1; -; Genomic_DNA.
DR EMBL; AF056972; AAC13568.1; -; mRNA.
DR EMBL; L17074; AAC37651.1; -; mRNA.
DR CCDS; CCDS23922.1; -.
DR RefSeq; NP_034441.1; NM_010311.3.
DR RefSeq; XP_006513298.1; XM_006513235.3.
DR RefSeq; XP_006513299.1; XM_006513236.1.
DR RefSeq; XP_006513300.1; XM_006513237.2.
DR AlphaFoldDB; O70443; -.
DR SMR; O70443; -.
DR BioGRID; 199975; 11.
DR IntAct; O70443; 5.
DR MINT; O70443; -.
DR STRING; 10090.ENSMUSP00000036087; -.
DR iPTMnet; O70443; -.
DR PhosphoSitePlus; O70443; -.
DR SwissPalm; O70443; -.
DR EPD; O70443; -.
DR jPOST; O70443; -.
DR PaxDb; O70443; -.
DR PeptideAtlas; O70443; -.
DR PRIDE; O70443; -.
DR ProteomicsDB; 271006; -.
DR Antibodypedia; 222; 340 antibodies from 30 providers.
DR DNASU; 14687; -.
DR Ensembl; ENSMUST00000037813; ENSMUSP00000036087; ENSMUSG00000040009.
DR Ensembl; ENSMUST00000159991; ENSMUSP00000124639; ENSMUSG00000040009.
DR GeneID; 14687; -.
DR KEGG; mmu:14687; -.
DR UCSC; uc007fpt.1; mouse.
DR CTD; 2781; -.
DR MGI; MGI:95780; Gnaz.
DR VEuPathDB; HostDB:ENSMUSG00000040009; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160353; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; O70443; -.
DR OMA; TMGCRQS; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; O70443; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR BioGRID-ORCS; 14687; 0 hits in 72 CRISPR screens.
DR PRO; PR:O70443; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O70443; protein.
DR Bgee; ENSMUSG00000040009; Expressed in ventromedial nucleus of hypothalamus and 184 other tissues.
DR ExpressionAtlas; O70443; baseline and differential.
DR Genevisible; O70443; MM.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; IMP:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001408; Gprotein_alpha_I.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..355
FT /note="Guanine nucleotide-binding protein G(z) subunit
FT alpha"
FT /id="PRO_0000203697"
FT DOMAIN 32..355
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..48
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 210
FT /note="K -> R (in Ref. 3; AAC37651)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 40850 MW; 24590AE5B1FE5D50 CRC64;
MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG
FNLDACKEYK PLIIYNAIDS LTRIIRALAA LKIDFHNPDR AYDAVQLFAL TGPAESKGEI
TPELLGVMRR LWADPGAQAC FGRSSEYHLE DNAAYYLNDL ERIAAPDYIP TVEDILRSRD
MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ
TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLSVCFPE YKGQNTYEEA
AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC
