YRA2_YEAST
ID YRA2_YEAST Reviewed; 203 AA.
AC P36036; D6VWY9;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=RNA annealing protein YRA2;
GN Name=YRA2; OrderedLocusNames=YKL214C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7941750; DOI=10.1002/yea.320100511;
RA Tzermia M., Horaitis O., Alexandraki D.;
RT "The complete sequencing of a 24.6 kb segment of yeast chromosome XI
RT identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open
RT reading frames including homologues to the threonine dehydratases, membrane
RT transporters, hydantoinases and the phospholipase A2-activating protein.";
RL Yeast 10:663-679(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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, ASSOCIATION WITH MRNPS, AND SUBCELLULAR LOCATION.
RX PubMed=11390651; DOI=10.1128/mcb.21.13.4219-4232.2001;
RA Zenklusen D., Vinciguerra P., Strahm Y., Stutz F.;
RT "The yeast hnRNP-Like proteins Yra1p and Yra2p participate in mRNA export
RT through interaction with Mex67p.";
RL Mol. Cell. Biol. 21:4219-4232(2001).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH YRA1.
RX PubMed=15584090; DOI=10.1002/yea.1185;
RA Kashyap A.K., Schieltz D., Yates J. III, Kellogg D.R.;
RT "Biochemical and genetic characterization of Yra1p in budding yeast.";
RL Yeast 22:43-56(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH MRNPS.
RX PubMed=17922018; DOI=10.1038/nmeth1101;
RA Oeffinger M., Wei K.E., Rogers R., DeGrasse J.A., Chait B.T.,
RA Aitchison J.D., Rout M.P.;
RT "Comprehensive analysis of diverse ribonucleoprotein complexes.";
RL Nat. Methods 4:951-956(2007).
RN [8]
RP DNA-BINDING.
RX PubMed=19376128; DOI=10.1016/j.jmb.2009.04.018;
RA Shukla A., Durairaj G., Schneider J., Duan Z., Shadle T., Bhaumik S.R.;
RT "Stimulation of mRNA export by an F-box protein, Mdm30p, in vivo.";
RL J. Mol. Biol. 389:238-247(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in export of poly(A) mRNAs from the nucleus.
CC Recruited to the coding sequences as well as poly-A sites of active
CC genes. {ECO:0000269|PubMed:11390651, ECO:0000269|PubMed:15584090}.
CC -!- SUBUNIT: Associates with mRNPs. Interacts with YRA1.
CC {ECO:0000269|PubMed:15584090}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11390651}.
CC -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the YRA1 family. {ECO:0000305}.
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DR EMBL; X75951; CAA53559.1; -; Genomic_DNA.
DR EMBL; Z28214; CAA82059.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08955.1; -; Genomic_DNA.
DR PIR; S38052; S38052.
DR RefSeq; NP_012708.1; NM_001179779.1.
DR AlphaFoldDB; P36036; -.
DR SMR; P36036; -.
DR BioGRID; 33951; 299.
DR DIP; DIP-6538N; -.
DR IntAct; P36036; 8.
DR MINT; P36036; -.
DR STRING; 4932.YKL214C; -.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; P36036; -.
DR MaxQB; P36036; -.
DR PaxDb; P36036; -.
DR PRIDE; P36036; -.
DR EnsemblFungi; YKL214C_mRNA; YKL214C; YKL214C.
DR GeneID; 853666; -.
DR KEGG; sce:YKL214C; -.
DR SGD; S000001697; YRA2.
DR VEuPathDB; FungiDB:YKL214C; -.
DR eggNOG; ENOG502S444; Eukaryota.
DR HOGENOM; CLU_111217_0_0_1; -.
DR InParanoid; P36036; -.
DR OMA; KQTAQEH; -.
DR BioCyc; YEAST:G3O-31972-MON; -.
DR PRO; PR:P36036; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36036; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR CDD; cd12295; RRM_YRA2; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025715; FoP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034396; Yra2_RRM.
DR Pfam; PF13865; FoP_duplication; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; mRNA transport; Nucleus; Reference proteome;
KW RNA-binding; Transport.
FT CHAIN 1..203
FT /note="RNA annealing protein YRA2"
FT /id="PRO_0000082033"
FT DOMAIN 64..138
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 203 AA; 23778 MW; 89B7A4B210438652 CRC64;
MDKAFDEIIG NSHTDSSSNH KVTRYRRRDL RNELGPRLGF APSDAASRSK DRLYREREEP
PLPKRIRISK IPLDVSDYTL DDMIKEFGSP IFSKIFDNKE DRTCIYEFED PEVLEKIVER
YNGHELHNAK IEVEIYQPQR KHSRMNAHNR RKQTAQEHGR GRPGSHYRQK PNRVSKKNKG
REKNNTPTSV EALDAELDAY MKG