GBB1_BOVIN
ID GBB1_BOVIN Reviewed; 340 AA.
AC P62871; P04697; P04901; Q3MHF1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3083416; DOI=10.1073/pnas.83.7.2162;
RA Fong H.K.W., Hurley J.B., Hopkins R.S., Miake-Lye R., Johnson M.S.,
RA Doolittle R.F., Simon M.I.;
RT "Repetitive segmental structure of the transducin beta subunit: homology
RT with the CDC4 gene and identification of related mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2162-2166(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2414128; DOI=10.1016/0014-5793(85)80015-6;
RA Sugimoto K., Nukada T., Tanabe T., Takahashi H., Noda M., Minamino N.,
RA Kangawa K., Matsuo H., Hirose T., Inayama S., Numa S.;
RT "Primary structure of the beta-subunit of bovine transducin deduced from
RT the cDNA sequence.";
RL FEBS Lett. 191:235-240(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION AT HIS-266.
RX PubMed=12486123; DOI=10.1074/jbc.m210304200;
RA Cuello F., Schulze R.A., Heemeyer F., Meyer H.E., Lutz S., Jakobs K.H.,
RA Niroomand F., Wieland T.;
RT "Activation of heterotrimeric G proteins by a high energy phosphate
RT transfer via nucleoside diphosphate kinase (NDPK) B and Gbeta subunits.
RT Complex formation of NDPK B with Gbeta gamma dimers and phosphorylation of
RT His-266 IN Gbeta.";
RL J. Biol. Chem. 278:7220-7226(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER.
RX PubMed=8521505; DOI=10.1016/0092-8674(95)90220-1;
RA Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A.,
RA Gilman A.G., Sprang S.R.;
RT "The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2.";
RL Cell 83:1047-1058(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF BETA-GAMMA DIMER.
RX PubMed=8552196; DOI=10.1038/379369a0;
RA Sondek J., Bohm A., Lambright D.G., Hamm H.E., Sigler P.B.;
RT "Crystal structure of a G-protein beta gamma dimer at 2.1-A resolution.";
RL Nature 379:369-374(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH PHOSDUCIN.
RX PubMed=9739091; DOI=10.1016/s0969-2126(98)00102-6;
RA Loew A., Ho Y.K., Blundell T., Bax B.;
RT "Phosducin induces a structural change in transducin beta gamma.";
RL Structure 6:1007-1019(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH GRK2 AND GNG2.
RX PubMed=12764189; DOI=10.1126/science.1082348;
RA Lodowski D.T., Pitcher J.A., Capel W.D., Lefkowitz R.J., Tesmer J.J.;
RT "Keeping G proteins at bay: a complex between G protein-coupled receptor
RT kinase 2 and Gbetagamma.";
RL Science 300:1256-1262(2003).
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
CC (PubMed:8521505). The heterodimer formed by GNB1 and GNG2 interacts
CC with ARHGEF5 (By similarity). The heterodimer formed by GNB1 and GNG2
CC interacts with GRK2 (PubMed:12764189). Interacts with ARHGEF18 and
CC RASD2 (By similarity). {ECO:0000250|UniProtKB:P62873,
CC ECO:0000269|PubMed:12764189, ECO:0000269|PubMed:8521505}.
CC -!- INTERACTION:
CC P62871; P63097: GNAI1; NbExp=3; IntAct=EBI-357141, EBI-8309073;
CC P62871; P63212: GNG2; NbExp=6; IntAct=EBI-357141, EBI-1036424;
CC P62871; Q3T0Q4: NME2; NbExp=3; IntAct=EBI-357141, EBI-8577979;
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:0000269|PubMed:12486123}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; X03073; CAA26875.1; -; mRNA.
DR EMBL; M13236; AAA30792.1; -; mRNA.
DR EMBL; BC105260; AAI05261.1; -; mRNA.
DR PIR; A24225; RGBOB1.
DR RefSeq; NP_786971.2; NM_175777.3.
DR RefSeq; XP_005217074.1; XM_005217017.1.
DR RefSeq; XP_010811610.1; XM_010813308.2.
DR PDB; 1A0R; X-ray; 2.80 A; B=2-340.
DR PDB; 1B9X; X-ray; 3.00 A; A=1-340.
DR PDB; 1B9Y; X-ray; 3.00 A; A=1-340.
DR PDB; 1GG2; X-ray; 2.40 A; B=1-340.
DR PDB; 1GOT; X-ray; 2.00 A; B=1-340.
DR PDB; 1GP2; X-ray; 2.30 A; B=1-340.
DR PDB; 1OMW; X-ray; 2.50 A; B=1-340.
DR PDB; 1TBG; X-ray; 2.10 A; A/B/C/D=1-340.
DR PDB; 1XHM; X-ray; 2.70 A; A=1-340.
DR PDB; 2BCJ; X-ray; 3.06 A; B=2-340.
DR PDB; 2TRC; X-ray; 2.40 A; B=1-340.
DR PDB; 3AH8; X-ray; 2.90 A; B=1-340.
DR PDB; 3CIK; X-ray; 2.75 A; B=1-340.
DR PDB; 3KRW; X-ray; 2.90 A; B=1-340.
DR PDB; 3KRX; X-ray; 3.10 A; B=1-340.
DR PDB; 3PSC; X-ray; 2.67 A; B=1-340.
DR PDB; 3PVU; X-ray; 2.48 A; B=1-340.
DR PDB; 3PVW; X-ray; 2.49 A; B=1-340.
DR PDB; 3UZS; X-ray; 4.52 A; B=1-340.
DR PDB; 3V5W; X-ray; 2.07 A; B=1-340.
DR PDB; 4MK0; X-ray; 2.40 A; B=2-340.
DR PDB; 5KDO; X-ray; 1.90 A; B=1-340.
DR PDB; 5WG3; X-ray; 2.90 A; B=1-340.
DR PDB; 5WG4; X-ray; 2.31 A; B=1-340.
DR PDB; 5WG5; X-ray; 3.10 A; B=1-340.
DR PDB; 6B20; X-ray; 2.34 A; A/B=3-340.
DR PDB; 6C2Y; X-ray; 2.74 A; B=1-340.
DR PDB; 6OY9; EM; 3.90 A; B=1-340.
DR PDB; 6OYA; EM; 3.30 A; B=1-340.
DR PDB; 6PCV; EM; 3.20 A; B=1-340.
DR PDB; 6QNO; EM; 4.38 A; B=1-340.
DR PDB; 6U7C; X-ray; 2.44 A; B=1-340.
DR PDB; 7BZ2; EM; 3.82 A; B=1-340.
DR PDB; 7D68; EM; 3.00 A; B=2-340.
DR PDB; 7DHI; EM; 3.26 A; B=1-340.
DR PDB; 7DHR; EM; 3.80 A; B=1-340.
DR PDB; 7E14; EM; 2.90 A; B=2-340.
DR PDB; 7JJO; EM; 2.60 A; B=2-340.
DR PDB; 7O7F; EM; 3.15 A; B=1-340.
DR PDB; 7PWD; X-ray; 2.60 A; B=1-340.
DR PDB; 7S0F; EM; 2.96 A; B=2-340.
DR PDB; 7S0G; EM; 3.86 A; B=2-340.
DR PDB; 7TD0; EM; 2.83 A; B=1-340.
DR PDB; 7TD1; EM; 3.08 A; B=1-340.
DR PDB; 7TD2; EM; 3.11 A; B=1-340.
DR PDB; 7TD3; EM; 3.00 A; B=1-340.
DR PDB; 7TD4; EM; 2.60 A; B=1-340.
DR PDBsum; 1A0R; -.
DR PDBsum; 1B9X; -.
DR PDBsum; 1B9Y; -.
DR PDBsum; 1GG2; -.
DR PDBsum; 1GOT; -.
DR PDBsum; 1GP2; -.
DR PDBsum; 1OMW; -.
DR PDBsum; 1TBG; -.
DR PDBsum; 1XHM; -.
DR PDBsum; 2BCJ; -.
DR PDBsum; 2TRC; -.
DR PDBsum; 3AH8; -.
DR PDBsum; 3CIK; -.
DR PDBsum; 3KRW; -.
DR PDBsum; 3KRX; -.
DR PDBsum; 3PSC; -.
DR PDBsum; 3PVU; -.
DR PDBsum; 3PVW; -.
DR PDBsum; 3UZS; -.
DR PDBsum; 3V5W; -.
DR PDBsum; 4MK0; -.
DR PDBsum; 5KDO; -.
DR PDBsum; 5WG3; -.
DR PDBsum; 5WG4; -.
DR PDBsum; 5WG5; -.
DR PDBsum; 6B20; -.
DR PDBsum; 6C2Y; -.
DR PDBsum; 6OY9; -.
DR PDBsum; 6OYA; -.
DR PDBsum; 6PCV; -.
DR PDBsum; 6QNO; -.
DR PDBsum; 6U7C; -.
DR PDBsum; 7BZ2; -.
DR PDBsum; 7D68; -.
DR PDBsum; 7DHI; -.
DR PDBsum; 7DHR; -.
DR PDBsum; 7E14; -.
DR PDBsum; 7JJO; -.
DR PDBsum; 7O7F; -.
DR PDBsum; 7PWD; -.
DR PDBsum; 7S0F; -.
DR PDBsum; 7S0G; -.
DR PDBsum; 7TD0; -.
DR PDBsum; 7TD1; -.
DR PDBsum; 7TD2; -.
DR PDBsum; 7TD3; -.
DR PDBsum; 7TD4; -.
DR AlphaFoldDB; P62871; -.
DR SMR; P62871; -.
DR BioGRID; 158560; 6.
DR CORUM; P62871; -.
DR DIP; DIP-29227N; -.
DR IntAct; P62871; 11.
DR MINT; P62871; -.
DR STRING; 9913.ENSBTAP00000042481; -.
DR iPTMnet; P62871; -.
DR PaxDb; P62871; -.
DR PeptideAtlas; P62871; -.
DR PRIDE; P62871; -.
DR ABCD; P62871; 5 sequenced antibodies.
DR Ensembl; ENSBTAT00000000259; ENSBTAP00000000259; ENSBTAG00000000215.
DR Ensembl; ENSBTAT00000045065; ENSBTAP00000042481; ENSBTAG00000000215.
DR GeneID; 281201; -.
DR KEGG; bta:281201; -.
DR CTD; 2782; -.
DR VEuPathDB; HostDB:ENSBTAG00000000215; -.
DR VGNC; VGNC:29457; GNB1.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P62871; -.
DR OMA; PLDSQWV; -.
DR OrthoDB; 704786at2759; -.
DR TreeFam; TF106149; -.
DR EvolutionaryTrace; P62871; -.
DR PRO; PR:P62871; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000000215; Expressed in retina and 102 other tissues.
DR ExpressionAtlas; P62871; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; IDA:BHF-UCL.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Reference proteome; Repeat;
KW Transducer; 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_0000127684"
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:0000269|PubMed:12486123"
FT CONFLICT 71
FT /note="V -> L (in Ref. 2; CAA26875)"
FT /evidence="ECO:0000305"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1GOT"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6PCV"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7DHI"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5KDO"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:5KDO"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2TRC"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:7JJO"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:5KDO"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6OYA"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:5KDO"
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
