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GBB_DICDI
ID   GBB_DICDI               Reviewed;         347 AA.
AC   P36408; Q54ZV7;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Guanine nucleotide-binding protein subunit beta;
GN   Name=gpbA; ORFNames=DDB_G0277143;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=8099335; DOI=10.1101/gad.7.6.986;
RA   Lilly P., Wu L., Welker D.L., Devreotes P.N.;
RT   "A G-protein beta-subunit is essential for Dictyostelium development.";
RL   Genes Dev. 7:986-995(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10669414; DOI=10.1126/science.287.5455.1034;
RA   Jin T., Zhang N., Long Y., Parent C.A., Devreotes P.N.;
RT   "Localization of the G protein betagamma complex in living cells during
RT   chemotaxis.";
RL   Science 287:1034-1036(2000).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11598203; DOI=10.1091/mbc.12.10.3204;
RA   Zhang N., Long Y., Devreotes P.N.;
RT   "Ggamma in dictyostelium: its role in localization of gbetagamma to the
RT   membrane is required for chemotaxis in shallow gradients.";
RL   Mol. Biol. Cell 12:3204-3213(2001).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14517243; DOI=10.1093/emboj/cdg508;
RA   Blaauw M., Knol J.C., Kortholt A., Roelofs J., Ruchira X., Postma M.,
RA   Visser A.J.W.G., van Haastert P.J.M.;
RT   "Phosducin-like proteins in Dictyostelium discoideum: implications for the
RT   phosducin family of proteins.";
RL   EMBO J. 22:5047-5057(2003).
RN   [7]
RP   INTERACTION WITH GPGA, AND SUBCELLULAR LOCATION.
RX   PubMed=16135826; DOI=10.1128/mcb.25.18.8393-8400.2005;
RA   Knol J.C., Engel R., Blaauw M., Visser A.J.W.G., van Haastert P.J.M.;
RT   "The phosducin-like protein PhLP1 is essential for Gbetagamma dimer
RT   formation in Dictyostelium discoideum.";
RL   Mol. Cell. Biol. 25:8393-8400(2005).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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 (By similarity). Required for normal chemotaxis in response
CC       to cAMP and for aggregation during scorocarp development. {ECO:0000250,
CC       ECO:0000269|PubMed:10669414, ECO:0000269|PubMed:11598203,
CC       ECO:0000269|PubMed:8099335}.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC       Interacts with gpgA, and this requires phlp1.
CC       {ECO:0000269|PubMed:16135826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14517243,
CC       ECO:0000269|PubMed:16135826}. Cell membrane
CC       {ECO:0000269|PubMed:10669414, ECO:0000269|PubMed:11598203,
CC       ECO:0000269|PubMed:14517243, ECO:0000269|PubMed:16135826}.
CC       Note=Membrane-associated protein is concentrated at the anterior of
CC       polarized cells. {ECO:0000269|PubMed:10669414}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development. Expression rises
CC       within 6 hours after the initiation of development and gradually
CC       decreases following the mound stage. Expressed in vegetative cells.
CC       {ECO:0000269|PubMed:11598203, ECO:0000269|PubMed:8099335}.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC       {ECO:0000305}.
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DR   EMBL; X73641; CAA52018.1; -; mRNA.
DR   EMBL; AAFI02000019; EAL68757.1; -; Genomic_DNA.
DR   PIR; A47370; A47370.
DR   RefSeq; XP_642759.1; XM_637667.1.
DR   AlphaFoldDB; P36408; -.
DR   SMR; P36408; -.
DR   IntAct; P36408; 1.
DR   STRING; 44689.DDB0252679; -.
DR   PaxDb; P36408; -.
DR   EnsemblProtists; EAL68757; EAL68757; DDB_G0277143.
DR   GeneID; 8620948; -.
DR   KEGG; ddi:DDB_G0277143; -.
DR   dictyBase; DDB_G0277143; gpbA.
DR   eggNOG; KOG0286; Eukaryota.
DR   HOGENOM; CLU_000288_57_34_1; -.
DR   InParanoid; P36408; -.
DR   OMA; PLDSQWV; -.
DR   PhylomeDB; P36408; -.
DR   Reactome; R-DDI-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-DDI-418594; G alpha (i) signalling events.
DR   Reactome; R-DDI-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   PRO; PR:P36408; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0031982; C:vesicle; IDA:dictyBase.
DR   GO; GO:0008047; F:enzyme activator activity; TAS:dictyBase.
DR   GO; GO:0031682; F:G-protein gamma-subunit binding; IDA:dictyBase.
DR   GO; GO:0019887; F:protein kinase regulator activity; IMP:dictyBase.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR   GO; GO:0140582; P:adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway; IMP:dictyBase.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:dictyBase.
DR   GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IMP:dictyBase.
DR   GO; GO:0043326; P:chemotaxis to folate; IMP:dictyBase.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:dictyBase.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0000165; P:MAPK cascade; IMP:dictyBase.
DR   GO; GO:1903665; P:negative regulation of asexual reproduction; IMP:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; IMP:dictyBase.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:dictyBase.
DR   GO; GO:1903669; P:positive regulation of chemorepellent activity; IMP:dictyBase.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IMP:dictyBase.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:dictyBase.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:dictyBase.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:dictyBase.
DR   GO; GO:1905301; P:regulation of macropinocytosis; IMP:dictyBase.
DR   GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:dictyBase.
DR   GO; GO:1902610; P:response to N-phenylthiourea; IMP:dictyBase.
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   Cell membrane; Chemotaxis; Cytoplasm; Membrane; Reference proteome; Repeat;
KW   Sensory transduction; Transducer; WD repeat.
FT   CHAIN           1..347
FT                   /note="Guanine nucleotide-binding protein subunit beta"
FT                   /id="PRO_0000127714"
FT   REPEAT          60..90
FT                   /note="WD 1"
FT   REPEAT          102..132
FT                   /note="WD 2"
FT   REPEAT          148..177
FT                   /note="WD 3"
FT   REPEAT          189..219
FT                   /note="WD 4"
FT   REPEAT          231..261
FT                   /note="WD 5"
FT   REPEAT          275..305
FT                   /note="WD 6"
FT   REPEAT          317..347
FT                   /note="WD 7"
SQ   SEQUENCE   347 AA;  38623 MW;  22DED34F35516903 CRC64;
     MSSDISEKIQ QARRDAESMK EQIRANRDVM NDTTLKTFTR DLPGLPKMEG KIKVRRNLKG
     HLAKIYAMHW AEDNVHLVSA SQDGKLLVWD GLTTNKVHAI PLRSSWVMTC AYSPTANFVA
     CGGLDNICSI YNLRSREQPI RVCRELNSHT GYLSCCRFLN DRQIVTSSGD MTCILWDVEN
     GTKITEFSDH NGDVMSVSVS PDKNYFISGA CDATAKLWDL RSGKCVQTFT GHEADINAVQ
     YFPNGLSFGT GSDDASCRLF DIRADRELMQ YTHDNILCGI TSVGFSFSGR FLFAGYDDFT
     CNVWDTLKGE RVLSLTGHGN RVSCLGVPTD GMALCTGSWD SLLKIWA
 
 
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