ID   SRP68_SCHPO             Reviewed;         597 AA.
AC   O74436;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Signal recognition particle subunit srp68;
DE   AltName: Full=Signal recognition particle 68 kDa protein homolog;
GN   Name=srp68; ORFNames=SPCC1682.05c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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 7SL RNA, srp72 binds to this complex subsequently (By
CC       similarity). The SRP complex possibly participates in the elongation
CC       arrest function (By similarity). {ECO:0000250|UniProtKB:P38687,
CC       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 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 (By
CC       similarity). {ECO:0000250|UniProtKB:P38687,
CC       ECO:0000250|UniProtKB:Q00004, ECO:0000250|UniProtKB:Q9UHB9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P38687}.
CC   -!- SIMILARITY: Belongs to the SRP68 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA20671.1; -; Genomic_DNA.
DR   PIR; T41062; T41062.
DR   RefSeq; NP_587798.1; NM_001022791.2.
DR   AlphaFoldDB; O74436; -.
DR   SMR; O74436; -.
DR   BioGRID; 275956; 3.
DR   STRING; 4896.SPCC1682.05c.1; -.
DR   iPTMnet; O74436; -.
DR   MaxQB; O74436; -.
DR   PaxDb; O74436; -.
DR   PRIDE; O74436; -.
DR   EnsemblFungi; SPCC1682.05c.1; SPCC1682.05c.1:pep; SPCC1682.05c.
DR   PomBase; SPCC1682.05c; srp68.
DR   VEuPathDB; FungiDB:SPCC1682.05c; -.
DR   eggNOG; KOG2460; Eukaryota.
DR   HOGENOM; CLU_018649_0_1_1; -.
DR   InParanoid; O74436; -.
DR   OMA; HIFYLEA; -.
DR   PhylomeDB; O74436; -.
DR   Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   PRO; PR:O74436; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISO:PomBase.
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:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; ISO:PomBase.
DR   Gene3D; 1.10.3450.40; -; 1.
DR   InterPro; IPR026258; SRP68.
DR   InterPro; IPR038253; SRP68_N_sf.
DR   PANTHER; PTHR12860; PTHR12860; 1.
DR   Pfam; PF16969; SRP68; 1.
DR   PIRSF; PIRSF038995; SRP68; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Signal recognition particle.
FT   CHAIN           1..597
FT                   /note="Signal recognition particle subunit srp68"
FT                   /id="PRO_0000351070"
FT   REGION          566..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   597 AA;  67860 MW;  D6AF1A80853D515B CRC64;
     MDPHVKLSTS LVIIAFRYLP NNFNDSRLGC DNLSTVGLCL KNGTGEVLFS GLIKQMANFY
     IFPLLLEARS DHFYEGNEYI KYLSHRIHGL RKSLHITQRG GKPKSSVDKR YAEILLFNAD
     RAFQQFVFLR SSQRRHALRR LKRADQFGKE LVSFTNAFDC NDHIFYLEAI AFAKYIEGTL
     NYEKRDWEGS LSAFSISRLS FLVLQNKIDT LAEHEKSVLG ELQNQIDSNL RYVAQRTGLQ
     NQTKSLDILM LSSIPKDEEV IQHVNSVDSE ILQMTGDEQD SLQTITVIEW RDQRVKIEHP
     DVVLALYAIH DVKNSPGTID SKRDRLLAAW ARAEEITKSV LDNTGLEDEQ KFQTLSICYT
     YLAYNVVLLR IQRDLAVEND SELVASQAQL RSRQSLYDSI IKNIEIAKEL PGIARDTGMT
     AQLEAQISLA KSKRCQAIAD AYQAQDKLAS LAMCVRAASY LQQVNDILRN FEEKPHLIAF
     DIIPELKKDE KELKKKILLL QSLASMGNIN QPPKNLSLVE TLDSYQTLAE LEPSWNLTDA
     DIRAIPAKPL FFDLAITYLG QQTSFDKKKA QPEKPVTSVS KEPKQKNKGF FSSLLGR