GBB2_RAT
ID GBB2_RAT Reviewed; 340 AA.
AC P54313; Q71SU9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
DE AltName: Full=G protein subunit beta-2;
DE AltName: Full=Transducin beta chain 2;
GN Name=Gnb2;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Kuroda S., Tokunaga C., Konishi H., Kikkawa U.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10970423; DOI=10.1111/j.1469-7793.2000.00203.x;
RA Arnot M.I., Stotz S.C., Jarvis S.E., Zamponi G.W.;
RT "Differential modulation of N-type 1B and P/Q-type 1A calcium channels by
RT different G protein subunit isoforms.";
RL J. Physiol. (Lond.) 527:203-212(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP PROTEIN SEQUENCE OF 2-15; 69-78 AND 198-209, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 58-78 AND 138-150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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. In
CC this context, interacts with GNAI2 and GNG2 (By similarity). Interacts
CC with ARHGEF18 and RASD2. Interacts with ATXN10. Interacts with SCN8A.
CC {ECO:0000250|UniProtKB:P62879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P62879}. Cell membrane
CC {ECO:0000250|UniProtKB:P62879}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; U34959; AAC72248.1; -; mRNA.
DR EMBL; AF277892; AAF82123.1; -; mRNA.
DR EMBL; BC065579; AAH65579.1; -; mRNA.
DR RefSeq; NP_112299.1; NM_031037.2.
DR AlphaFoldDB; P54313; -.
DR SMR; P54313; -.
DR BioGRID; 249566; 2.
DR DIP; DIP-61095N; -.
DR IntAct; P54313; 10.
DR STRING; 10116.ENSRNOP00000001911; -.
DR iPTMnet; P54313; -.
DR PhosphoSitePlus; P54313; -.
DR World-2DPAGE; 0004:P54313; -.
DR jPOST; P54313; -.
DR PaxDb; P54313; -.
DR PRIDE; P54313; -.
DR Ensembl; ENSRNOT00000001911; ENSRNOP00000001911; ENSRNOG00000001409.
DR GeneID; 81667; -.
DR KEGG; rno:81667; -.
DR UCSC; RGD:69319; rat.
DR CTD; 2783; -.
DR RGD; 69319; Gnb2.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR HOGENOM; CLU_000288_57_34_1; -.
DR InParanoid; P54313; -.
DR OMA; HVWDTLR; -.
DR OrthoDB; 704786at2759; -.
DR PhylomeDB; P54313; -.
DR TreeFam; TF106149; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-202040; G-protein activation.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-RNO-4086398; Ca2+ pathway.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-418597; G alpha (z) signalling events.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:P54313; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001409; Expressed in ovary and 20 other tissues.
DR Genevisible; P54313; RN.
DR GO; GO:0044297; C:cell body; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; IMP:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
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 Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-2"
FT /id="PRO_0000127697"
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:0000269|Ref.4"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62880"
FT CONFLICT 35
FT /note="A -> D (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="A -> D (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="S -> A (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="A -> V (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="M -> K (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="I -> N (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="RE -> KK (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="G -> D (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="D -> E (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="A -> V (in Ref. 1; AAC72248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37331 MW; 5D08FFA240ADEEE6 CRC64;
MSELEQLRQE AEQLRNQIRD ARKACGDSTL TQITAGLDPV GRIQMRTRRT LRGHLAKIYA
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN FVACGGLDNI
CSIYSLKTRE GNVRVSRELP GHTGYLSCCR FLDDNQIITS SGDTTCALWD IETGQQTVGF
AGHSGDVMSL SLAPDGRTFV SGACDASIKL WDVRDSMCRQ TFIGHESDIN AVAFFPNGYA
FTTGSDDATC RLFDLRADQE LLMYSHDNII CGITSVAFSR SGRLLLAGYD DFNCNIWDAM
KGDRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
