ID   MTR2_YEAST              Reviewed;         184 AA.
AC   P34232; D6VX14;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 174.
DE   RecName: Full=mRNA transport regulator MTR2;
GN   Name=MTR2; OrderedLocusNames=YKL186C;
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].
RX   PubMed=7865887; DOI=10.1091/mbc.5.11.1253;
RA   Kadowaki T., Hitomi M., Chen S., Tartakoff A.M.;
RT   "Nuclear mRNA accumulation causes nucleolar fragmentation in yeast mtr2
RT   mutant.";
RL   Mol. Biol. Cell 5:1253-1263(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8154185; DOI=10.1002/yea.320091208;
RA   Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA   Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT   "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT   from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT   FAS1 gene.";
RL   Yeast 9:1343-1348(1993).
RN   [3]
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   [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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 14-178 IN COMPLEX WITH MEX67.
RX   PubMed=12835756; DOI=10.1038/sj.embor.embor883;
RA   Fribourg S., Conti E.;
RT   "Structural similarity in the absence of sequence homology of the messenger
RT   RNA export factors Mtr2 and p15.";
RL   EMBO Rep. 4:699-703(2003).
CC   -!- FUNCTION: Affects mRNA transport from the nucleus to the cytoplasm.
CC   -!- SUBUNIT: Interacts with MEX67. {ECO:0000269|PubMed:12835756}.
CC   -!- INTERACTION:
CC       P34232; Q99257: MEX67; NbExp=3; IntAct=EBI-11585, EBI-11642;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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DR   EMBL; S77467; AAB33484.1; -; Genomic_DNA.
DR   EMBL; X74151; CAA52252.1; -; Genomic_DNA.
DR   EMBL; Z28186; CAA82029.1; -; Genomic_DNA.
DR   EMBL; AY558555; AAS56881.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08980.1; -; Genomic_DNA.
DR   PIR; S34684; S34684.
DR   RefSeq; NP_012735.1; NM_001179752.1.
DR   PDB; 1OF5; X-ray; 2.80 A; B=1-184.
DR   PDB; 4WWU; X-ray; 3.30 A; C/F/I/L=1-184.
DR   PDB; 8HBN; EM; 3.81 A; B=1-184.
DR   PDB; 8HFR; EM; 2.64 A; Bt/DK/FR=1-184.
DR   AlphaFoldDB; P34232; -.
DR   EMDB; EMD-34638; -.
DR   EMDB; EMD-34640; -.
DR   EMDB; EMD-34725; -.
DR   SMR; P34232; -.
DR   BioGRID; 33936; 166.
DR   ComplexPortal; CPX-1142; MEX67-MTR2 mRNA nuclear export factor complex.
DR   DIP; DIP-4856N; -.
DR   FunCoup; P34232; 212.
DR   IntAct; P34232; 14.
DR   MINT; P34232; -.
DR   STRING; 4932.YKL186C; -.
DR   TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR   iPTMnet; P34232; -.
DR   PaxDb; 4932-YKL186C; -.
DR   PeptideAtlas; P34232; -.
DR   EnsemblFungi; YKL186C_mRNA; YKL186C; YKL186C.
DR   GeneID; 853649; -.
DR   KEGG; sce:YKL186C; -.
DR   AGR; SGD:S000001669; -.
DR   SGD; S000001669; MTR2.
DR   VEuPathDB; FungiDB:YKL186C; -.
DR   eggNOG; ENOG502RZK7; Eukaryota.
DR   HOGENOM; CLU_128326_0_0_1; -.
DR   InParanoid; P34232; -.
DR   OMA; FDCHLIP; -.
DR   OrthoDB; 25408at2759; -.
DR   BioCyc; YEAST:G3O-31949-MONOMER; -.
DR   BioGRID-ORCS; 853649; 6 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P34232; -.
DR   PRO; PR:P34232; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P34232; protein.
DR   GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR   GO; GO:0042272; C:nuclear RNA export factor complex; IPI:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0006406; P:mRNA export from nucleus; NAS:ComplexPortal.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IDA:ComplexPortal.
DR   GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR   GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR   FunFam; 3.10.450.50:FF:000018; mRNA transport regulator; 1.
DR   Gene3D; 3.10.450.50; -; 1.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR019488; Nucl_pore_RNA_shuttling_Mtr2.
DR   Pfam; PF10429; Mtr2; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   PDBsum; 1OF5; -.
DR   PDBsum; 4WWU; -.
DR   PDBsum; 8HBN; -.
DR   PDBsum; 8HFR; -.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transport.
FT   CHAIN           1..184
FT                   /note="mRNA transport regulator MTR2"
FT                   /id="PRO_0000096634"
FT   REGION          111..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         125
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   HELIX           14..30
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   HELIX           40..44
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:4WWU"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:1OF5"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1OF5"
FT   HELIX           62..71
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          76..87
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          94..104
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:4WWU"
FT   HELIX           136..140
FT                   /evidence="ECO:0007829|PDB:4WWU"
FT   STRAND          145..153
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   TURN            155..160
FT                   /evidence="ECO:0007829|PDB:8HFR"
FT   STRAND          168..175
FT                   /evidence="ECO:0007829|PDB:8HFR"
SQ   SEQUENCE   184 AA;  20784 MW;  D3AE487A11FA2750 CRC64;
     MNTNSNTMVM NDANQAQITA TFTKKILAHL DDPDSNKLAQ FVQLFNPNNC RIIFNATPFA
     QATVFLQMWQ NQVVQTQHAL TGVDYHAIPG SGTLICNVNC KVRFDESGRD KMGQDATVPI
     QPNNTGNRNR PNDMNKPRPL WGPYFGISLQ LIIDDRIFRN DFNGVISGFN YNMVYKPEDS
     LLKI
//