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GBLP_DROME
ID   GBLP_DROME              Reviewed;         318 AA.
AC   O18640; Q9VLW5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=Guanine nucleotide-binding protein subunit beta-like protein;
DE   AltName: Full=Receptor of activated protein kinase C homolog;
GN   Name=Rack1; ORFNames=CG7111;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Oregon-R;
RX   PubMed=9296523; DOI=10.1016/s0167-4889(97)00079-7;
RA   Vani K., Yang G., Mohler J.;
RT   "Isolation and cloning of a Drosophila homolog to the mammalian RACK1 gene,
RT   implicated in PKC-mediated signalling.";
RL   Biochim. Biophys. Acta 1358:67-71(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) IN COMPLEX WITH THE 80S
RP   RIBOSOME, AND SUBUNIT.
RX   PubMed=23636399; DOI=10.1038/nature12104;
RA   Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA   Wilson D.N., Beckmann R.;
RT   "Structures of the human and Drosophila 80S ribosome.";
RL   Nature 497:80-85(2013).
CC   -!- FUNCTION: Involved in the recruitment, assembly and/or regulation of a
CC       variety of signaling molecules. Interacts with a wide variety of
CC       proteins and plays a role in many cellular processes (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the 80S ribosome.
CC       {ECO:0000269|PubMed:23636399}.
CC   -!- TISSUE SPECIFICITY: Highest expression in the mesodermal and endodermal
CC       lineages. {ECO:0000269|PubMed:9296523}.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
CC       protein RACK1 subfamily. {ECO:0000305}.
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DR   EMBL; U96491; AAB72148.1; -; mRNA.
DR   EMBL; AE014134; AAF52566.1; -; Genomic_DNA.
DR   EMBL; AY071661; AAL49283.1; -; mRNA.
DR   RefSeq; NP_001260218.1; NM_001273289.1.
DR   RefSeq; NP_001285723.1; NM_001298794.1.
DR   RefSeq; NP_477269.1; NM_057921.4.
DR   PDB; 4V6W; EM; 6.00 A; Ag=1-318.
DR   PDB; 6XU6; EM; 3.50 A; Ag=1-318.
DR   PDB; 6XU7; EM; 4.90 A; Ag=1-318.
DR   PDB; 6XU8; EM; 3.00 A; Ag=1-318.
DR   PDBsum; 4V6W; -.
DR   PDBsum; 6XU6; -.
DR   PDBsum; 6XU7; -.
DR   PDBsum; 6XU8; -.
DR   AlphaFoldDB; O18640; -.
DR   SMR; O18640; -.
DR   BioGRID; 60209; 134.
DR   DIP; DIP-17169N; -.
DR   IntAct; O18640; 29.
DR   STRING; 7227.FBpp0303680; -.
DR   PaxDb; O18640; -.
DR   PRIDE; O18640; -.
DR   EnsemblMetazoa; FBtr0079565; FBpp0079187; FBgn0020618.
DR   EnsemblMetazoa; FBtr0331238; FBpp0303680; FBgn0020618.
DR   EnsemblMetazoa; FBtr0345448; FBpp0311572; FBgn0020618.
DR   GeneID; 34070; -.
DR   KEGG; dme:Dmel_CG7111; -.
DR   CTD; 10399; -.
DR   FlyBase; FBgn0020618; Rack1.
DR   VEuPathDB; VectorBase:FBgn0020618; -.
DR   eggNOG; KOG0279; Eukaryota.
DR   GeneTree; ENSGT00940000154461; -.
DR   HOGENOM; CLU_000288_57_7_1; -.
DR   InParanoid; O18640; -.
DR   OMA; CKAMLWD; -.
DR   OrthoDB; 805365at2759; -.
DR   PhylomeDB; O18640; -.
DR   SignaLink; O18640; -.
DR   BioGRID-ORCS; 34070; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Rack1; fly.
DR   GenomeRNAi; 34070; -.
DR   PRO; PR:O18640; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0020618; Expressed in wing disc and 24 other tissues.
DR   ExpressionAtlas; O18640; baseline and differential.
DR   Genevisible; O18640; DM.
DR   GO; GO:0005776; C:autophagosome; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:FlyBase.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR   GO; GO:0042335; P:cuticle development; IMP:FlyBase.
DR   GO; GO:0075522; P:IRES-dependent viral translational initiation; IMP:FlyBase.
DR   GO; GO:0007626; P:locomotory behavior; IMP:FlyBase.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:FlyBase.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR   GO; GO:0018991; P:oviposition; IMP:FlyBase.
DR   GO; GO:0044829; P:positive regulation by host of viral genome replication; IMP:FlyBase.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:FlyBase.
DR   GO; GO:1903003; P:positive regulation of protein deubiquitination; IDA:FlyBase.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IGI:FlyBase.
DR   GO; GO:0016243; P:regulation of autophagosome size; IMP:FlyBase.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IBA:GO_Central.
DR   GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR045223; Asc1/RACK1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
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; PTHR19868; PTHR19868; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Repeat; Ribonucleoprotein;
KW   Ribosomal protein; WD repeat.
FT   CHAIN           1..318
FT                   /note="Guanine nucleotide-binding protein subunit beta-like
FT                   protein"
FT                   /id="PRO_0000127740"
FT   REPEAT          13..44
FT                   /note="WD 1"
FT   REPEAT          62..92
FT                   /note="WD 2"
FT   REPEAT          104..134
FT                   /note="WD 3"
FT   REPEAT          147..179
FT                   /note="WD 4"
FT   REPEAT          191..221
FT                   /note="WD 5"
FT   REPEAT          232..261
FT                   /note="WD 6"
FT   REPEAT          282..312
FT                   /note="WD 7"
FT   CONFLICT        104
FT                   /note="G -> R (in Ref. 1; AAB72148)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  35618 MW;  202930BE51AEE822 CRC64;
     MSETLQLRGT LIGHNGWVTQ IATNPKDPDT IISASRDKTL IVWKLTRDED TNYGYPQKRL
     YGHSHFISDV VLSSDGNYAL SGSWDQTLRL WDLAAGKTTR RFEGHTKDVL SVAFSADNRQ
     IVSGSRDKTI KLWNTLAECK FTIQEDGHTD WVSCVRFSPN HSNPIIVSCG WDRTVKVWNL
     ANCKLKNNHH GHNGYLNTVT VSPDGSLCTS GGKDSKALLW DLNDGKNLYT LEHNDIINAL
     CFSPNRYWLC VAYGPSIKIW DLACKKTVEE LRPEVVSPTS KADQPQCLSL AWSTDGQTLF
     AGYSDNTIRV WQVSVSAH
 
 
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