ID SRP72_YEAST Reviewed; 640 AA.
AC P38688; D6W3G0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Signal recognition particle subunit SRP72;
DE AltName: Full=Signal recognition particle 72 kDa protein homolog;
GN Name=SRP72; OrderedLocusNames=YPL210C;
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 FUNCTION.
RX PubMed=10921896; DOI=10.1093/emboj/19.15.4164;
RA Mason N., Ciufo L.F., Brown J.D.;
RT "Elongation arrest is a physiologically important function of signal
RT recognition particle.";
RL EMBO J. 19:4164-4174(2000).
RN [5]
RP ASSEMBLY OF THE SRP COMPLEX, 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 [6]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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, PubMed:10921896). The SRP complex interacts with the
CC signal sequence in nascent secretory and membrane proteins and directs
CC them to the membrane of the ER (PubMed:10921896, PubMed:7925282). The
CC SRP complex targets the ribosome-nascent chain complex to the SRP
CC receptor (SR), which is anchored in the ER, where SR compaction and
CC GTPase rearrangement drive cotranslational protein translocation into
CC the ER (By similarity). Binds signal recognition particle RNA (7SL RNA)
CC in presence of SRP68 (By similarity). Can bind 7SL RNA with low
CC affinity (By similarity). The SRP complex possibly participates in the
CC elongation arrest function (PubMed:10921896).
CC {ECO:0000250|UniProtKB:O76094, ECO:0000269|PubMed:10921896,
CC ECO:0000269|PubMed:7925282}.
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 (PubMed:7925282). At least SRP14, SRP21, SRP68 and SRP72 are proposed
CC to get assembled together with scR1 RNA as a pre-SRP complex in the
CC nucleolus which is exported to the cytoplasm (PubMed:7925282).
CC {ECO:0000269|PubMed:7925282}.
CC -!- INTERACTION:
CC P38688; P29478: SEC65; NbExp=8; IntAct=EBI-18011, EBI-16641;
CC P38688; P38985: SRP14; NbExp=6; IntAct=EBI-18011, EBI-17977;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O76094}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:11352936}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:11352936}. Note=Transiently localizes to
CC the nucleolus during biogenesis of the SRP. The SRP-RNC complex is
CC bound to the endoplasmic reticulum membrane due to the interaction of
CC the SRP with the membrane SRP-receptor (SRP101-SRP102).
CC {ECO:0000269|PubMed:11352936}.
CC -!- MISCELLANEOUS: Present with 11800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SRP72 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA53400.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA97925.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L35178; AAA53400.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z73566; CAA97925.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006949; DAA11226.1; -; Genomic_DNA.
DR PIR; S47929; S47929.
DR RefSeq; NP_015114.2; NM_001184024.1.
DR AlphaFoldDB; P38688; -.
DR BioGRID; 35975; 123.
DR ComplexPortal; CPX-609; Signal recognition particle.
DR DIP; DIP-6763N; -.
DR IntAct; P38688; 16.
DR MINT; P38688; -.
DR STRING; 4932.YPL210C; -.
DR iPTMnet; P38688; -.
DR MaxQB; P38688; -.
DR PaxDb; 4932-YPL210C; -.
DR PeptideAtlas; P38688; -.
DR EnsemblFungi; YPL210C_mRNA; YPL210C; YPL210C.
DR GeneID; 855891; -.
DR KEGG; sce:YPL210C; -.
DR AGR; SGD:S000006131; -.
DR SGD; S000006131; SRP72.
DR VEuPathDB; FungiDB:YPL210C; -.
DR eggNOG; KOG2376; Eukaryota.
DR GeneTree; ENSGT00390000013264; -.
DR HOGENOM; CLU_013808_4_0_1; -.
DR InParanoid; P38688; -.
DR OMA; ELACNER; -.
DR OrthoDB; 91080at2759; -.
DR BioCyc; YEAST:G3O-34101-MONOMER; -.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR BioGRID-ORCS; 855891; 8 hits in 10 CRISPR screens.
DR PRO; PR:P38688; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P38688; Protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IPI:ComplexPortal.
DR GO; GO:0008312; F:7S RNA binding; IBA:GO_Central.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; NAS:ComplexPortal.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR InterPro; IPR026270; SRP72.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14094; SIGNAL RECOGNITION PARTICLE 72; 1.
DR PANTHER; PTHR14094:SF9; SIGNAL RECOGNITION PARTICLE SUBUNIT SRP72; 1.
DR Pfam; PF08492; SRP72; 1.
DR PIRSF; PIRSF038922; SRP72; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Nucleus; Reference proteome; Ribonucleoprotein;
KW Signal recognition particle; TPR repeat.
FT CHAIN 1..640
FT /note="Signal recognition particle subunit SRP72"
FT /id="PRO_0000135238"
FT REPEAT 188..221
FT /note="TPR"
FT REGION 574..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 73541 MW; DB2F536212F0871B CRC64;
MAKDNLTNLL SQLNIQLSQD EHSQVEQTCV KLLDSGCENP ADVFRRCLVA VIQQDKYQKA
LHYLKKFKHI DDKYGRKFAL EKLYIFYKLN MPDEFNTLYT AIITDDLDTV LKKDIESLRG
ILHVRAQYCY KNGLYQEAFK IYQHLASHNE KDQDSQIELS CNERVPLSVA TELMNRSPLV
TPMDESSYDL LFNESFIMAS VGKYDKAIEL LEKALQGATN EGYQNDINTI KLQLSFVLQM
VGKTAQSKEI LKGLLQELKA DSPFSLICQN NLNAFVDFSK YNTNFNLLLR ELNVEKLNTF
NLQTFTHEQW SNIQRNVLFL RLFNNVKIHS QESLLSRTFD KYSKLVDNVT LESYKTQAKK
LYHHTTKTIL SGTDGSTIGI LLLTIQLLII EKEWENAIRI GELFLNESWK SSFEKFNDSQ
AIVCYILFEL YKIKGRNNSK SVLLKKLGSV RVQLSGKIQE NIPFWKHVGF ELLSMGNAKE
SKALLREISN FSKGDADVLV DRVVSSDSLD IAQGIDLVRD IDIDKLIQLG VKPLESSAKR
SKNTAVSKVQ KRKVLELKKK RKIKRLEKFL QGRDTSKLPD PERWLPLRDR STYRPKKKQQ
GAKQTQGGAM NKKSEQALDI SKKGKPTVNK KPKNKKKGRK
//
