ID   SRP72_SCHPO             Reviewed;         561 AA.
AC   O59787;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Signal recognition particle subunit srp72;
DE   AltName: Full=Signal recognition particle 72 kDa protein homolog;
GN   Name=srp72; ORFNames=SPCC320.10;
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).
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) in presence of
CC       srp68 (By similarity). Can bind 7SL RNA with low affinity (By
CC       similarity). The SRP complex possibly participates in the elongation
CC       arrest function (By similarity). {ECO:0000250|UniProtKB:O76094,
CC       ECO:0000250|UniProtKB:P38688}.
CC   -!- SUBUNIT: 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       {ECO:0000250|UniProtKB:O76094}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76094}.
CC       Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38688}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:P38688}.
CC   -!- SIMILARITY: Belongs to the SRP72 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA18312.1; -; Genomic_DNA.
DR   PIR; T41301; T41301.
DR   RefSeq; NP_587719.1; NM_001022714.2.
DR   AlphaFoldDB; O59787; -.
DR   SMR; O59787; -.
DR   BioGRID; 275372; 2.
DR   STRING; 4896.SPCC320.10.1; -.
DR   iPTMnet; O59787; -.
DR   MaxQB; O59787; -.
DR   PaxDb; O59787; -.
DR   PRIDE; O59787; -.
DR   EnsemblFungi; SPCC320.10.1; SPCC320.10.1:pep; SPCC320.10.
DR   GeneID; 2538791; -.
DR   KEGG; spo:SPCC320.10; -.
DR   PomBase; SPCC320.10; srp72.
DR   VEuPathDB; FungiDB:SPCC320.10; -.
DR   eggNOG; KOG2376; Eukaryota.
DR   HOGENOM; CLU_013808_1_0_1; -.
DR   InParanoid; O59787; -.
DR   OMA; NDMKVLA; -.
DR   PhylomeDB; O59787; -.
DR   Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   PRO; PR:O59787; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISO:PomBase.
DR   GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; ISO:PomBase.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR   InterPro; IPR026270; SRP72.
DR   InterPro; IPR031545; SRP_TPR-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR14094; PTHR14094; 1.
DR   Pfam; PF08492; SRP72; 1.
DR   Pfam; PF17004; SRP_TPR_like; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endoplasmic reticulum; Membrane; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Signal recognition particle.
FT   CHAIN           1..561
FT                   /note="Signal recognition particle subunit srp72"
FT                   /id="PRO_0000135237"
FT   REGION          505..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..550
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   561 AA;  63281 MW;  635A39547CA51BDB CRC64;
     MSNHEEEIEE LAQRIGKIEV GDTKSDIYQK VLNLIDIERY EHALKIIEKY LGETDAVYER
     AYCAFQLGKE DFSLEDKQFL QHLQAQKAYR LSDFSKALKI YEHLENDLPE QRADIRVNML
     AAASQLPGLQ LNNAVSLDDQ DSVFNLATRY LTIGDWNQAI ELLSSSLEKL ENSDSNSEDH
     KSQINLCRLQ LFFAYLQAGD NEKASKESLK ISKDCLDETS QAIFVNNLIS MSIDNPYISF
     RDLHGTNLEK ALSSLLASQK KQFIRNLALL DMAVGKQRSV RKEKKRNPEE SIYFSTILLR
     EETKSLISPK KLPGYLENLF KSDSDNIVVA LLLMQHKISN GNFRGALSIY QKLRTSLEAS
     QSLSVLYSPG LVGLGDALHY KIQSTGFKSQ LLHEAANYWR KQQSCEAKLL LCTRSLLAHL
     DERAPVSTIQ DDMSVIDDLL QWKGPISELV SCKVAALCYL DKEIESGMDK YLVPTKDLIT
     GIDVDDIEIR GVPVSAAIGP IKRSVEANSS NSSKKTRKRR KPTPKSFNPK ATPDPQRWIP
     KRDRTNVKIK SKGKSMQGGV A