ID   SRP14_YEAST             Reviewed;         146 AA.
AC   P38985; D6VRQ6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 172.
DE   RecName: Full=Signal recognition particle subunit SRP14;
DE   AltName: Full=Signal recognition particle 14 kDa protein homolog;
GN   Name=SRP14; OrderedLocusNames=YDL092W; ORFNames=D2404;
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], FUNCTION, AND IDENTIFICATION IN THE SRP
RP   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 [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8923743;
RX   DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA   Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA   Jimenez A., Remacha M.A.;
RT   "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT   IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT   reading frames.";
RL   Yeast 12:1377-1384(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   FUNCTION, AND RNA-BINDING.
RX   PubMed=10573124; DOI=10.1017/s1355838299991045;
RA   Strub K., Fornallaz M., Bui N.;
RT   "The Alu domain homolog of the yeast signal recognition particle consists
RT   of an Srp14p homodimer and a yeast-specific RNA structure.";
RL   RNA 5:1333-1347(1999).
RN   [7]
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP   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:10573124). The SRP complex is required for the
CC       cotranslational protein translocation for ER import and preferentially
CC       recognizes strongly hydrophobic signal sequences (PubMed:10573124). It
CC       is involved in targeting the nascent chain-ribosome (RNC) complex to
CC       the ER and is proposed to participate in the arrest of nascent chain
CC       elongation during membrane targeting (PubMed:10573124). SRP14 binds
CC       scR1 RNA to form the probable Alu domain of SRP responsible for
CC       elongation arrest (PubMed:10573124). {ECO:0000269|PubMed:10573124,
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. SRP14 binds RNA as a
CC       homodimer (PubMed:7925282). {ECO:0000269|PubMed:7925282}.
CC   -!- INTERACTION:
CC       P38985; P29478: SEC65; NbExp=7; IntAct=EBI-17977, EBI-16641;
CC       P38985; P38688: SRP72; NbExp=6; IntAct=EBI-17977, EBI-18011;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000269|PubMed:11352936}.
CC   -!- MISCELLANEOUS: Present with 8000 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the SRP14 family. {ECO:0000305}.
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DR   EMBL; L35155; AAA53402.1; -; Genomic_DNA.
DR   EMBL; X95644; CAA64919.1; -; Genomic_DNA.
DR   EMBL; Z74140; CAA98659.1; -; Genomic_DNA.
DR   EMBL; Z74139; CAA98658.1; -; Genomic_DNA.
DR   EMBL; AY558159; AAS56485.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11766.1; -; Genomic_DNA.
DR   PIR; S51616; S51616.
DR   RefSeq; NP_010191.1; NM_001180151.1.
DR   AlphaFoldDB; P38985; -.
DR   SMR; P38985; -.
DR   BioGRID; 31968; 39.
DR   ComplexPortal; CPX-609; Signal recognition particle.
DR   DIP; DIP-4864N; -.
DR   IntAct; P38985; 16.
DR   MINT; P38985; -.
DR   STRING; 4932.YDL092W; -.
DR   iPTMnet; P38985; -.
DR   MaxQB; P38985; -.
DR   PaxDb; P38985; -.
DR   PRIDE; P38985; -.
DR   EnsemblFungi; YDL092W_mRNA; YDL092W; YDL092W.
DR   GeneID; 851466; -.
DR   KEGG; sce:YDL092W; -.
DR   SGD; S000002250; SRP14.
DR   VEuPathDB; FungiDB:YDL092W; -.
DR   eggNOG; KOG1761; Eukaryota.
DR   HOGENOM; CLU_094309_3_0_1; -.
DR   InParanoid; P38985; -.
DR   OMA; DKFWQDY; -.
DR   BioCyc; YEAST:G3O-29499-MON; -.
DR   Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   PRO; PR:P38985; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P38985; protein.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
DR   GO; GO:0008312; F:7S RNA binding; IDA:SGD.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR   GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR   GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
DR   Gene3D; 3.30.720.10; -; 1.
DR   InterPro; IPR003210; Signal_recog_particle_SRP14.
DR   InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR   PANTHER; PTHR12013; PTHR12013; 1.
DR   Pfam; PF02290; SRP14; 1.
DR   SUPFAM; SSF54762; SSF54762; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW   RNA-binding; Signal recognition particle.
FT   CHAIN           1..146
FT                   /note="Signal recognition particle subunit SRP14"
FT                   /id="PRO_0000135196"
FT   REGION          121..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
SQ   SEQUENCE   146 AA;  16430 MW;  4AF76A26018367EF CRC64;
     MANTGCLSPG AFLSKVPEFF QTANEKHITV RLTAKRLIEH DPVEGNLEFD STNHPDYDVS
     KKASEISVSS RSDREYPLLI RMSYGSHDKK TKCSTVVKAS ELDQFWQEYS SVFKGGMQNL
     IKKKKKKSKN GTISKTGKKN KVAKKN