SRP68_YEAST
ID SRP68_YEAST Reviewed; 599 AA.
AC P38687; D6W3C8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Signal recognition particle subunit SRP68;
DE AltName: Full=Signal recognition particle 68 kDa protein homolog;
GN Name=SRP68; OrderedLocusNames=YPL243W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP IDENTIFICATION IN THE SRP COMPLEX.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7925282; DOI=10.1002/j.1460-2075.1994.tb06759.x;
RA Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,
RA Walter P.;
RT "Subunits of the Saccharomyces cerevisiae signal recognition particle
RT required for its functional expression.";
RL EMBO J. 13:4390-4400(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP ASSEMBLY OF THE SRP COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11352936; DOI=10.1083/jcb.153.4.745;
RA Grosshans H., Deinert K., Hurt E.C., Simos G.;
RT "Biogenesis of the signal recognition particle (SRP) involves import of SRP
RT proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated
RT export.";
RL J. Cell Biol. 153:745-762(2001).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 (PubMed:7925282). 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 (PubMed:7925282).
CC {ECO:0000250|UniProtKB:Q9UHB9, ECO:0000269|PubMed:7925282}.
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 fungal signal recognition particle (SRP)
CC complex that consists of a 7SL RNA molecule (scR1) and at least six
CC protein subunits: SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14
CC (PubMed:7925282, PubMed:11352936). {ECO:0000250|UniProtKB:Q00004,
CC ECO:0000250|UniProtKB:Q9UHB9, ECO:0000269|PubMed:11352936,
CC ECO:0000269|PubMed:7925282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O74436}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:11352936}.
CC -!- MISCELLANEOUS: Present with 6280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
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DR EMBL; L35177; AAA53401.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91601.1; -; Genomic_DNA.
DR EMBL; Z73599; CAA97964.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11194.1; -; Genomic_DNA.
DR PIR; S47928; S47928.
DR RefSeq; NP_015081.1; NM_001184057.1.
DR AlphaFoldDB; P38687; -.
DR BioGRID; 35920; 79.
DR ComplexPortal; CPX-609; Signal recognition particle.
DR DIP; DIP-6742N; -.
DR IntAct; P38687; 20.
DR MINT; P38687; -.
DR STRING; 4932.YPL243W; -.
DR iPTMnet; P38687; -.
DR MaxQB; P38687; -.
DR PaxDb; P38687; -.
DR PRIDE; P38687; -.
DR EnsemblFungi; YPL243W_mRNA; YPL243W; YPL243W.
DR GeneID; 855833; -.
DR KEGG; sce:YPL243W; -.
DR SGD; S000006164; SRP68.
DR VEuPathDB; FungiDB:YPL243W; -.
DR eggNOG; KOG2460; Eukaryota.
DR GeneTree; ENSGT00390000011856; -.
DR HOGENOM; CLU_018649_2_1_1; -.
DR InParanoid; P38687; -.
DR OMA; LAYIKYN; -.
DR BioCyc; YEAST:G3O-34129-MON; -.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR PRO; PR:P38687; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P38687; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
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 Cytoplasm; Direct protein sequencing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT CHAIN 1..599
FT /note="Signal recognition particle subunit SRP68"
FT /id="PRO_0000135232"
FT REGION 559..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 69006 MW; 241749187CE95499 CRC64;
MVAYSPIIAT YGNRAEQFLE TDSDFAKYHA KLNKKLQHLR SRCHLVTKDT KKYSSKNKYG
EINSEDYDNK TKLIGVLILL HAERDLALAE TLKLRARQRG KLKKSEEKVL STRLKKACKT
ADKLVNVTQN EQQWITRAQY LAFAKLVHSE YLINGKRFKR KDNAKISNNL ALVFAALEHL
KNLSLLAEEV VDNIVNKYQY SLKQYAGNLI TTPEINNFIV ERVQSDENKD DELVKLLLDN
GFNMKKITTS TEDQKVTTNI NWRSFNAKII DAEVAQFLEQ GLSIHPTQIT QYTQRLSKLE
KALDRHEFFI ANHDDQDDID EMVENSSENN QIILAYIKYN ILLTSISRER DLFTHLWNQW
LKLNTSLPSK LTKYKEMERI VKNLTKYLSD IMELPGVYSD DELLSQLDLC KLYFQLFLNT
GCLSVLYQSK GRYMEALALY VDAYRRLENK LSEIESLDEI LLPANLLSLN SVRSLQKRIE
NGGNSVITLA EYEKRNHGGS LGKYDLTVIE KLDSKKILPT DIQLKNLFPL KPKMLPIPSK
PTLFDLAFNY ITYDKQEPSA SQVKDSVTET ESISQTPISN EQTEGEPKKK RGFLGLFGR
