GNAZ_RAT
ID GNAZ_RAT Reviewed; 355 AA.
AC P19627;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2456569; DOI=10.1073/pnas.85.15.5384;
RA Matsuoka M., Itoh H., Kozasa T., Kaziro Y.;
RT "Sequence analysis of cDNA and genomic DNA for a putative pertussis toxin-
RT insensitive guanine nucleotide-binding regulatory protein alpha subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5384-5388(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chang P.-Y., Poncz M., Zhang H., Brass L.F., Manning D.R.;
RT "Rat alpha-z gene.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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; J03773; AAA41304.1; -; mRNA.
DR EMBL; U77485; AAD09877.1; -; Genomic_DNA.
DR EMBL; U77484; AAD09877.1; JOINED; Genomic_DNA.
DR PIR; A31316; RGRTGX.
DR RefSeq; NP_037321.1; NM_013189.2.
DR RefSeq; XP_008771088.1; XM_008772866.2.
DR RefSeq; XP_008771089.1; XM_008772867.2.
DR RefSeq; XP_017457054.1; XM_017601565.1.
DR AlphaFoldDB; P19627; -.
DR SMR; P19627; -.
DR BioGRID; 247768; 2.
DR IntAct; P19627; 1.
DR MINT; P19627; -.
DR STRING; 10116.ENSRNOP00000001779; -.
DR iPTMnet; P19627; -.
DR PhosphoSitePlus; P19627; -.
DR SwissPalm; P19627; -.
DR PaxDb; P19627; -.
DR PRIDE; P19627; -.
DR Ensembl; ENSRNOT00000001779; ENSRNOP00000001779; ENSRNOG00000001313.
DR GeneID; 25740; -.
DR KEGG; rno:25740; -.
DR UCSC; RGD:2717; rat.
DR CTD; 2781; -.
DR RGD; 2717; Gnaz.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000160353; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P19627; -.
DR OMA; TMGCRQS; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P19627; -.
DR TreeFam; TF300673; -.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR PRO; PR:P19627; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000001313; Expressed in frontal cortex and 14 other tissues.
DR Genevisible; P19627; RN.
DR GO; GO:0044297; C:cell body; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IPI:RGD.
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; IMP:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; ISO:RGD.
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 2: Evidence at transcript 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_0000203698"
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"
SQ SEQUENCE 355 AA; 40880 MW; 0C268D8A3DDF8136 CRC64;
MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG
FNLEACKEYK PLIIYNAIDS LTRIIRALAA LKIDFHNPDR AYDAVQLFAL TGPAESKGEI
TPELLGVMRR LWADPGAQAC FGRSSEYHLE DNAAYYLNDL ERIAAPDYIP TVEDILRSRD
MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ
TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLSEKIR RIPLSVCFPE YKGQNTYEEA
AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC
