GBB1_CANLF
ID GBB1_CANLF Reviewed; 340 AA.
AC P62872; P04697; P04901;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
DE AltName: Full=Transducin beta chain 1;
GN Name=GNB1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Labrador;
RX PubMed=9300552; DOI=10.1016/s0034-5288(97)90208-3;
RA Kylma T., Paulin L., Hurwitz M.Y., Hurwitz R.L., Kommonen B.;
RT "Cloning of the cDNA encoding rod photoreceptor cGMP-phosphodiesterase
RT alpha and gamma subunits from the retinal degenerate Labrador retriever
RT dog.";
RL Res. Vet. Sci. 62:293-296(1997).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC ARHGEF5 (By similarity). The heterodimer formed by GNB1 and GNG2
CC interacts with GRK2 (By similarity). Interacts with ARHGEF18 and RASD2
CC (By similarity). {ECO:0000250|UniProtKB:P62871,
CC ECO:0000250|UniProtKB:P62873}.
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer onto
CC GDP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; Z75134; CAA99446.1; -; mRNA.
DR RefSeq; NP_001003236.1; NM_001003236.1.
DR RefSeq; XP_005620396.1; XM_005620339.2.
DR RefSeq; XP_005620397.1; XM_005620340.2.
DR RefSeq; XP_005620398.1; XM_005620341.2.
DR AlphaFoldDB; P62872; -.
DR SMR; P62872; -.
DR STRING; 9612.ENSCAFP00000031020; -.
DR PaxDb; P62872; -.
DR PRIDE; P62872; -.
DR Ensembl; ENSCAFT00030002209; ENSCAFP00030001955; ENSCAFG00030001243.
DR Ensembl; ENSCAFT00040008109; ENSCAFP00040007069; ENSCAFG00040004230.
DR Ensembl; ENSCAFT00845028295; ENSCAFP00845022262; ENSCAFG00845015784.
DR GeneID; 403912; -.
DR KEGG; cfa:403912; -.
DR CTD; 2782; -.
DR VEuPathDB; HostDB:ENSCAFG00845015784; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P62872; -.
DR OMA; PLDSQWV; -.
DR OrthoDB; 704786at2759; -.
DR TreeFam; TF106149; -.
DR Reactome; R-CFA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-CFA-202040; G-protein activation.
DR Reactome; R-CFA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-CFA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-CFA-381753; Olfactory Signaling Pathway.
DR Reactome; R-CFA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-CFA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-CFA-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-CFA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-CFA-4086398; Ca2+ pathway.
DR Reactome; R-CFA-416476; G alpha (q) signalling events.
DR Reactome; R-CFA-416482; G alpha (12/13) signalling events.
DR Reactome; R-CFA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Reactome; R-CFA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-CFA-418594; G alpha (i) signalling events.
DR Reactome; R-CFA-418597; G alpha (z) signalling events.
DR Reactome; R-CFA-420092; Glucagon-type ligand receptors.
DR Reactome; R-CFA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-CFA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-CFA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-CFA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-CFA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-CFA-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-CFA-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-CFA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CFA-9634597; GPER1 signaling.
DR Reactome; R-CFA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-CFA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR Proteomes; UP000002254; Chromosome 5.
DR Bgee; ENSCAFG00000019216; Expressed in prefrontal cortex and 47 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Reference proteome; Repeat; Transducer;
KW WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-1"
FT /id="PRO_0000127685"
FT REPEAT 53..83
FT /note="WD 1"
FT REPEAT 95..125
FT /note="WD 2"
FT REPEAT 141..170
FT /note="WD 3"
FT REPEAT 182..212
FT /note="WD 4"
FT REPEAT 224..254
FT /note="WD 5"
FT REPEAT 268..298
FT /note="WD 6"
FT REPEAT 310..340
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
SQ SEQUENCE 340 AA; 37377 MW; 896CBD32D2686598 CRC64;
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF
TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA
FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
