SRP68_MOUSE
ID SRP68_MOUSE Reviewed; 625 AA.
AC Q8BMA6; A2AAN1; Q6NS76;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Signal recognition particle subunit SRP68;
DE Short=SRP68;
DE AltName: Full=Signal recognition particle 68 kDa protein;
GN Name=Srp68;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Within the SRP complex, interacts (via C-terminus) with SRP72 (via N-
CC terminus) (By similarity). {ECO:0000250|UniProtKB:Q00004,
CC 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 -!- DOMAIN: The N-terminus is required for RNA-binding.
CC {ECO:0000250|UniProtKB:Q9UHB9}.
CC -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK033010; BAC28124.1; -; mRNA.
DR EMBL; AL645861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL669925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34568.1; -; Genomic_DNA.
DR EMBL; BC070422; AAH70422.1; -; mRNA.
DR CCDS; CCDS25662.1; -.
DR RefSeq; NP_666144.3; NM_146032.3.
DR AlphaFoldDB; Q8BMA6; -.
DR SMR; Q8BMA6; -.
DR BioGRID; 229892; 20.
DR STRING; 10090.ENSMUSP00000021133; -.
DR iPTMnet; Q8BMA6; -.
DR PhosphoSitePlus; Q8BMA6; -.
DR SwissPalm; Q8BMA6; -.
DR EPD; Q8BMA6; -.
DR jPOST; Q8BMA6; -.
DR MaxQB; Q8BMA6; -.
DR PaxDb; Q8BMA6; -.
DR PeptideAtlas; Q8BMA6; -.
DR PRIDE; Q8BMA6; -.
DR ProteomicsDB; 257401; -.
DR Antibodypedia; 19656; 141 antibodies from 24 providers.
DR DNASU; 217337; -.
DR Ensembl; ENSMUST00000021133; ENSMUSP00000021133; ENSMUSG00000020780.
DR GeneID; 217337; -.
DR KEGG; mmu:217337; -.
DR UCSC; uc007mkq.1; mouse.
DR CTD; 6730; -.
DR MGI; MGI:1917447; Srp68.
DR VEuPathDB; HostDB:ENSMUSG00000020780; -.
DR eggNOG; KOG2460; Eukaryota.
DR GeneTree; ENSGT00390000011856; -.
DR HOGENOM; CLU_018649_0_1_1; -.
DR InParanoid; Q8BMA6; -.
DR OMA; DERFIHI; -.
DR OrthoDB; 1019762at2759; -.
DR PhylomeDB; Q8BMA6; -.
DR TreeFam; TF105779; -.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR BioGRID-ORCS; 217337; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Srp68; mouse.
DR PRO; PR:Q8BMA6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BMA6; protein.
DR Bgee; ENSMUSG00000020780; Expressed in lacrimal gland and 257 other tissues.
DR ExpressionAtlas; Q8BMA6; baseline and differential.
DR Genevisible; Q8BMA6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0048500; C:signal recognition particle; ISO:MGI.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISO:MGI.
DR GO; GO:0008312; F:7S RNA binding; ISO:MGI.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0005047; F:signal recognition particle binding; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..625
FT /note="Signal recognition particle subunit SRP68"
FT /id="PRO_0000135228"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..251
FT /note="RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT REGION 586..608
FT /note="Required for interaction with SRP72"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT COMPBIAS 34..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT MOD_RES 451
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB9"
FT CONFLICT 176
FT /note="R -> Q (in Ref. 1; BAC28124)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="S -> Y (in Ref. 1; BAC28124)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 625 AA; 70574 MW; 0CC69D6CB102CEF5 CRC64;
MAAEKQIPGG GSGGGGSGSG GGGGGSGGGR SAGGDENKEN ERPSAGSKAN KEFGDSLSLE
ILQIIKESQQ QHGLRHGDFQ RYRGYCSRRQ RRLRKTLNFK MGNRHKFTGK KVTEELLTDN
RYLLLVLMDA ERAWSYAMQL KQEANTEPRK RFHLLSRLRK AVKHAEELER LCESNRVDAK
TKLEAQAYTA YLSGMLRFEH QEWKSAIEAF NKCKTIYEKL ASAFTEEQAV LYNQRVEEIS
PNIRYCAYNI GDQSAINELM QMRLRSGGTE GLLAEKLEAL ITQTRAKQAA TMSEVEWRGR
TVPVKIDKVR IFLLGLADNE AAIVQAESEE TKERLFESML SECRDALQAV REELKPDQKQ
RDYALDGESG KVSNLQYLHS YLTYIKLSTA IRRNENMAKG LHRALLQQQP EDDSKRSPRP
QDLIRLYDII LQNLVELLQL PGLEEDRTFQ KEISLKTLVF KAYRCFFIAQ SYVLVKKWSE
ALVLYDRVLK YANEVSSHGG ASKNSLKDLP DVQELITQVR SEKCSLQAAA ILDANDSHQT
DTSSQVKDNT PLVERFESFC LDPSLVTKQA NLVHFPPGFQ PIPCKPLFFD LALNHVAFPP
LEDKLEQKTK SGLTGYIKGI FGFRS
