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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
 
 
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