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Signal recognition particle subunit SRP14 (Signal recognition particle 14 kDa protein homolog)

 SRP14_YEAST             Reviewed;         146 AA.
P38985; D6VRQ6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
10-OCT-2018, entry version 151.
RecName: Full=Signal recognition particle subunit SRP14;
AltName: Full=Signal recognition particle 14 kDa protein homolog;
Name=SRP14; OrderedLocusNames=YDL092W; ORFNames=D2404;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION IN THE SRP
COMPLEX.
STRAIN=ATCC 204508 / S288c;
PubMed=7925282;
Brown J.D., Hann B.C., Medzihradszky K.F., Niwa M., Burlingame A.L.,
Walter P.;
"Subunits of the Saccharomyces cerevisiae signal recognition particle
required for its functional expression.";
EMBO J. 13:4390-4400(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8923743;
DOI=10.1002/(SICI)1097-0061(199610)12:13<1377::AID-YEA35>3.0.CO;2-R;
Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
Jimenez A., Remacha M.A.;
"The sequence of a 16,691 bp segment of Saccharomyces cerevisiae
chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes,
and five new open reading frames.";
Yeast 12:1377-1384(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
RNA-BINDING.
PubMed=10573124; DOI=10.1017/S1355838299991045;
Strub K., Fornallaz M., Bui N.;
"The Alu domain homolog of the yeast signal recognition particle
consists of an Srp14p homodimer and a yeast-specific RNA structure.";
RNA 5:1333-1347(1999).
[7]
ASSEMBLY OF THE SRP COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=11352936; DOI=10.1083/jcb.153.4.745;
Grosshans H., Deinert K., Hurt E.C., Simos G.;
"Biogenesis of the signal recognition particle (SRP) involves import
of SRP proteins into the nucleolus, assembly with the SRP-RNA, and
Xpo1p-mediated export.";
J. Cell Biol. 153:745-762(2001).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Signal-recognition-particle (SRP) assembly has a crucial
role in targeting secretory proteins to the rough endoplasmic
reticulum (ER) membrane. SRP is required for the cotranslational
protein translocation for ER import and preferentially recognizes
strongly hydrophobic signal sequences. It is involved in targeting
the nascent chain-ribosome (RNC) complex to the ER and is proposed
to participate in the arrest of nascent chain elongation during
membrane targeting. SRP14 binds scR1 RNA to form the probable Alu
domain of SRP responsible for elongation arrest.
-!- SUBUNIT: Fungal signal recognition particle (SRP) complex consists
of a 7S RNA molecule (scR1) and at least six protein subunits:
SRP72, SRP68, SRP54, SEC65, SRP21 and SRP14. At least SRP14,
SRP21, SRP68 and SRP72 are proposed to get assembled together with
scR1 RNA as a pre-SRP complex in the nucleolus which is exported
to the cytoplasm. SRP14 binds RNA as a homodimer.
{ECO:0000269|PubMed:7925282}.
-!- INTERACTION:
P29478:SEC65; NbExp=7; IntAct=EBI-17977, EBI-16641;
P38688:SRP72; NbExp=6; IntAct=EBI-17977, EBI-18011;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:11352936}.
-!- MISCELLANEOUS: Present with 8000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SRP14 family. {ECO:0000305}.
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EMBL; L35155; AAA53402.1; -; Genomic_DNA.
EMBL; X95644; CAA64919.1; -; Genomic_DNA.
EMBL; Z74140; CAA98659.1; -; Genomic_DNA.
EMBL; Z74139; CAA98658.1; -; Genomic_DNA.
EMBL; AY558159; AAS56485.1; -; Genomic_DNA.
EMBL; BK006938; DAA11766.1; -; Genomic_DNA.
PIR; S51616; S51616.
RefSeq; NP_010191.1; NM_001180151.1.
ProteinModelPortal; P38985; -.
SMR; P38985; -.
BioGrid; 31968; 37.
ComplexPortal; CPX-609; Signal recognition particle.
DIP; DIP-4864N; -.
IntAct; P38985; 16.
MINT; P38985; -.
STRING; 4932.YDL092W; -.
iPTMnet; P38985; -.
MaxQB; P38985; -.
PaxDb; P38985; -.
PRIDE; P38985; -.
EnsemblFungi; YDL092W; YDL092W; YDL092W.
GeneID; 851466; -.
KEGG; sce:YDL092W; -.
EuPathDB; FungiDB:YDL092W; -.
SGD; S000002250; SRP14.
HOGENOM; HOG000065969; -.
InParanoid; P38985; -.
KO; K03104; -.
OMA; NEKHITV; -.
OrthoDB; EOG092C5UDY; -.
BioCyc; YEAST:G3O-29499-MONOMER; -.
PRO; PR:P38985; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IDA:SGD.
GO; GO:0008312; F:7S RNA binding; IDA:SGD.
GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
Gene3D; 3.30.720.10; -; 1.
InterPro; IPR003210; Signal_recog_particle_SRP14.
InterPro; IPR009018; Signal_recog_particle_SRP9/14.
PANTHER; PTHR12013; PTHR12013; 1.
Pfam; PF02290; SRP14; 1.
SUPFAM; SSF54762; SSF54762; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Ribonucleoprotein; RNA-binding;
Signal recognition particle.
CHAIN 1 146 Signal recognition particle subunit
SRP14.
/FTId=PRO_0000135196.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
SEQUENCE 146 AA; 16430 MW; 4AF76A26018367EF CRC64;
MANTGCLSPG AFLSKVPEFF QTANEKHITV RLTAKRLIEH DPVEGNLEFD STNHPDYDVS
KKASEISVSS RSDREYPLLI RMSYGSHDKK TKCSTVVKAS ELDQFWQEYS SVFKGGMQNL
IKKKKKKSKN GTISKTGKKN KVAKKN


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