SRP68_DROME
ID SRP68_DROME Reviewed; 604 AA.
AC Q9VSS2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Signal recognition particle subunit SRP68;
DE Short=SRP68;
DE AltName: Full=Signal recognition particle 68 kDa protein;
GN Name=Srp68; ORFNames=CG5064;
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 [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 [2]
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 [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=15901661; DOI=10.1242/dev.01863;
RA Abrams E.W., Andrew D.J.;
RT "CrebA regulates secretory activity in the Drosophila salivary gland and
RT epidermis.";
RL Development 132:2743-2758(2005).
CC -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC (By similarity). The SRP complex interacts with the signal sequence in
CC nascent secretory and membrane proteins and directs them to the
CC membrane of the ER (By similarity). The SRP complex targets the
CC ribosome-nascent chain complex to the SRP receptor (SR), which is
CC anchored in the ER, where SR compaction and GTPase rearrangement drive
CC cotranslational protein translocation into the ER (By similarity).
CC Binds the signal recognition particle RNA (7SL RNA), Srp72 binds to
CC this complex subsequently (By similarity). The SRP complex possibly
CC participates in the elongation arrest function (By similarity).
CC {ECO:0000250|UniProtKB:P38687, ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- SUBUNIT: Heterodimer with Srp72 (By similarity). Srp68/Srp72
CC heterodimer formation is stabilized by the presence of 7SL RNA (By
CC similarity). Component of a signal recognition particle (SRP) complex
CC that consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC subunits: Srp72, Srp68, Srp54, Srp19, Srp14 and Srp9 (By similarity).
CC {ECO:0000250|UniProtKB:Q00004, ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB9}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UHB9}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
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DR EMBL; AE014296; AAF50341.1; -; Genomic_DNA.
DR EMBL; AY058698; AAL13927.1; -; mRNA.
DR RefSeq; NP_648273.1; NM_140016.3.
DR AlphaFoldDB; Q9VSS2; -.
DR SMR; Q9VSS2; -.
DR BioGRID; 64432; 19.
DR DIP; DIP-22114N; -.
DR IntAct; Q9VSS2; 12.
DR STRING; 7227.FBpp0076244; -.
DR PaxDb; Q9VSS2; -.
DR PRIDE; Q9VSS2; -.
DR DNASU; 39028; -.
DR EnsemblMetazoa; FBtr0076517; FBpp0076244; FBgn0035947.
DR GeneID; 39028; -.
DR KEGG; dme:Dmel_CG5064; -.
DR UCSC; CG5064-RA; d. melanogaster.
DR CTD; 6730; -.
DR FlyBase; FBgn0035947; Srp68.
DR VEuPathDB; VectorBase:FBgn0035947; -.
DR eggNOG; KOG2460; Eukaryota.
DR GeneTree; ENSGT00390000011856; -.
DR HOGENOM; CLU_018649_0_1_1; -.
DR InParanoid; Q9VSS2; -.
DR OMA; DERFIHI; -.
DR OrthoDB; 1019762at2759; -.
DR PhylomeDB; Q9VSS2; -.
DR Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; Q9VSS2; -.
DR BioGRID-ORCS; 39028; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39028; -.
DR PRO; PR:Q9VSS2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035947; Expressed in embryonic/larval hemocyte (Drosophila) and 46 other tissues.
DR Genevisible; Q9VSS2; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR CDD; cd15481; SRP68-RBD; 1.
DR Gene3D; 1.10.3450.40; -; 1.
DR InterPro; IPR026258; SRP68.
DR InterPro; IPR034652; SRP68-RBD.
DR InterPro; IPR038253; SRP68_N_sf.
DR PANTHER; PTHR12860; PTHR12860; 1.
DR Pfam; PF16969; SRP68; 1.
DR PIRSF; PIRSF038995; SRP68; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..604
FT /note="Signal recognition particle subunit SRP68"
FT /id="PRO_0000135230"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 69009 MW; 61F4A8317EC70BA4 CRC64;
MVVQEDNPNT GDVQEKTETA PVAEPSKIFT VEILHMIKDA QQQHGLRHGD FQRYRGYCSR
RIRRLRKALK YPQGDKRHFK RRDVTIGQLT GKKADERFIH IPLICAERAW AYAMQLKQES
NTEPRKRFHL VNKLRRACFY ALQLQELCNT EAFDARTKLE CEAYVAWMHG TLHFELQLWK
TAGEHLKRAQ VVYENLGKAL PEDEQELYRA KVNEFTPNLR YCAYNISGGA SGGKIDEILE
LRAQGVLENL DVLVSQTKTE SSEGLQTIDW RGRKVTVRPE KVRLFLLSAQ ELDKSLAKTT
KQDAKIELIE RILMDCKDAI QAVRDEIKQD PKLRSLTTGQ TVSGVQYLLA YLSYIRHSRT
LQRNLCLVEQ AKLNFYDPNL QSQQNVGDGK RVRPQDLARL YEIILQNVTE MQQINGLEDD
ATYQSEVENL AITFKAFRCY YIALTLIDIK KWKEAVALYE RASNYATEAL KGKSSPEFQL
QEELKKVVSA IDGCKFSAHA YSVLEDDNSE ESGTTTKSQK TTKPLYERLS LYKEDQSLHT
KAPNVFKLTP DMEPIPCKPI FFDLAMTYVE LPSLEGKLES PGKKGASITG FVKGFLGWGG
GGNK
