YRA1_YEAST
ID YRA1_YEAST Reviewed; 226 AA.
AC Q12159; D6VT14;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=RNA annealing protein YRA1;
GN Name=YRA1; OrderedLocusNames=YDR381W; ORFNames=D9481.2, D9509.1;
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], AND PROTEIN SEQUENCE OF 39-53 AND 57-70.
RC STRAIN=BJ5626;
RX PubMed=9149233;
RA Portman D.S., O'Connor J.P., Dreyfuss G.;
RT "YRA1, an essential Saccharomyces cerevisiae gene, encodes a novel nuclear
RT protein with RNA annealing activity.";
RL RNA 3:527-537(1997).
RN [2]
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 [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 IDENTIFICATION IN TREX COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11979277; DOI=10.1038/nature746;
RA Straesser K., Masuda S., Mason P., Pfannstiel J., Oppizzi M.,
RA Rodriguez-Navarro S., Rondon A.G., Aguilera A., Struhl K., Reed R.,
RA Hurt E.;
RT "TREX is a conserved complex coupling transcription with messenger RNA
RT export.";
RL Nature 417:304-308(2002).
RN [5]
RP INTERACTION WITH RDS3.
RX PubMed=14517302; DOI=10.1128/mcb.23.20.7339-7349.2003;
RA Wang Q., Rymond B.C.;
RT "Rds3p is required for stable U2 snRNP recruitment to the splicing
RT apparatus.";
RL Mol. Cell. Biol. 23:7339-7349(2003).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH YRA2.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP 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).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: RNA-binding RNA annealing protein. May have a role in pre-
CC mRNA metabolism. Component the TREX complex, which operates in coupling
CC transcription elongation to mRNA export. {ECO:0000269|PubMed:15584090}.
CC -!- SUBUNIT: Component of the transcription/export (TREX) complex, which is
CC at least is formed of SUB2, TEX1 and YRA1 and the THO complex composed
CC of HPR1, MFT1, THO2 and THP1. Interacts with RDS3 and YRA2.
CC {ECO:0000269|PubMed:11979277, ECO:0000269|PubMed:14517302,
CC ECO:0000269|PubMed:15584090}.
CC -!- INTERACTION:
CC Q12159; P39081: PCF11; NbExp=2; IntAct=EBI-29516, EBI-12980;
CC Q12159; Q07478: SUB2; NbExp=5; IntAct=EBI-29516, EBI-18500;
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; U72633; AAC09951.1; -; Genomic_DNA.
DR EMBL; U28373; AAB64817.1; -; Genomic_DNA.
DR EMBL; U32274; AAB64823.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12224.1; -; Genomic_DNA.
DR PIR; S61176; S61176.
DR RefSeq; NP_010669.1; NM_001180689.1.
DR PDB; 5SUP; X-ray; 2.60 A; G/H/I=200-226.
DR PDBsum; 5SUP; -.
DR AlphaFoldDB; Q12159; -.
DR SMR; Q12159; -.
DR BioGRID; 32441; 507.
DR ComplexPortal; CPX-1793; TREX complex.
DR DIP; DIP-1791N; -.
DR IntAct; Q12159; 49.
DR MINT; Q12159; -.
DR STRING; 4932.YDR381W; -.
DR iPTMnet; Q12159; -.
DR MaxQB; Q12159; -.
DR PaxDb; Q12159; -.
DR PRIDE; Q12159; -.
DR TopDownProteomics; Q12159; -.
DR EnsemblFungi; YDR381W_mRNA; YDR381W; YDR381W.
DR GeneID; 851988; -.
DR KEGG; sce:YDR381W; -.
DR SGD; S000002789; YRA1.
DR VEuPathDB; FungiDB:YDR381W; -.
DR eggNOG; KOG0533; Eukaryota.
DR HOGENOM; CLU_052367_2_1_1; -.
DR InParanoid; Q12159; -.
DR OMA; GIARVWF; -.
DR BioCyc; YEAST:G3O-29929-MON; -.
DR PRO; PR:Q12159; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12159; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000346; C:transcription export complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:1990119; F:RNA helicase inhibitor activity; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IGI:SGD.
DR GO; GO:1902281; P:negative regulation of RNA helicase activity; IDA:SGD.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IDA:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:SGD.
DR CDD; cd12267; RRM_YRA1_MLO3; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034357; Yra1/Mlo3_RRM.
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 3D-structure; Acetylation; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..226
FT /note="RNA annealing protein YRA1"
FT /id="PRO_0000082007"
FT DOMAIN 78..158
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:5SUP"
SQ SEQUENCE 226 AA; 24956 MW; 480B5B6DC0D14BE9 CRC64;
MSANLDKSLD EIIGSNKAGS NRARVGGTRG NGPRRVGKQV GSQRRSLPNR RGPIRKNTRA
PPNAVARVAK LLDTTREVKV NVEGLPRDIK QDAVREFFAS QVGGVQRVLL SYNERGQSTG
MANITFKNGE LARRAVERFN GSPIDGGRSR LRLNLIVDPN QRPVKSLADR IKAMPQKGGN
APRPVKRGPN RKAAMAKSQN KPKREKPAKK SLEDLDKEMA DYFEKK
