GNAT_XENLA
ID GNAT_XENLA Reviewed; 350 AA.
AC P38407; Q2T9I4;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha;
DE AltName: Full=Transducin alpha chain;
GN Name=gnat;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Knox B.E., Scalzetti L.C., Batni S., Wang J.Q.;
RT "Molecular cloning of the abundant rhodopsin and transducin from Xenopus
RT laevis.";
RL Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) 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. Transducin is an amplifier and one of the transducers of a
CC visual impulse that performs the coupling between rhodopsin and cGMP-
CC phosphodiesterase.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; L07771; AAA88693.1; -; mRNA.
DR EMBL; BC111509; AAI11510.1; -; mRNA.
DR RefSeq; NP_001084030.1; NM_001090561.1.
DR AlphaFoldDB; P38407; -.
DR SMR; P38407; -.
DR DNASU; 399262; -.
DR GeneID; 399262; -.
DR KEGG; xla:399262; -.
DR CTD; 399262; -.
DR Xenbase; XB-GENE-17343152; gnat1.L.
DR OrthoDB; 754573at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 399262; Expressed in camera-type eye and 8 other tissues.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0009416; P:response to light stimulus; ISS:AgBase.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
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; Metal-binding; Myristate;
KW Nucleotide-binding; Reference proteome; Sensory transduction; Transducer;
KW Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..350
FT /note="Guanine nucleotide-binding protein G(t) subunit
FT alpha"
FT /id="PRO_0000203742"
FT DOMAIN 28..350
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..44
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 169..177
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 192..201
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 261..268
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 320..325
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 171..177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 196..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 265..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 350 AA; 39811 MW; 197ED5A0B5FBCC02 CRC64;
MGAGASAEEK HSRELEKKLK EDADKDARTV KLLLLGAGES GKSTIVKQMK IIHQDGYSVE
ECLEFIAIIY GNTLQSMIAI VKAMNTLNIQ FGDPARQDDA RKLMHLADTI DEGSMPKEMS
DIIGRLWKDT GIQACFDRAS EYQLNDSAGY YLNDLDRLVI PGYVPTEQDV LRSRVKTTGI
IETQFGLKDL NFRMFDVGGQ RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH
ESLHLFNSIC NHRYFATTSI VLFLNKKDVF TEKIKKAHLS ICFPDYDGPN TYEDAGNYIK
TQFLELNMRR DVKEIYSHMT CATDTENVKF VFDAVTDIII KENLKDCGLF
