MEX67_YEAST
ID MEX67_YEAST Reviewed; 599 AA.
AC Q99257; D6W3J9;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=mRNA export factor MEX67;
GN Name=MEX67; OrderedLocusNames=YPL169C; ORFNames=P2520;
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 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION, AND INTERACTION WITH MIP6.
RX PubMed=9214641; DOI=10.1093/emboj/16.11.3256;
RA Segref A., Sharma K., Doye V., Hellwig A., Huber J., Luehrmann R., Hurt E.;
RT "Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA
RT and nuclear pores.";
RL EMBO J. 16:3256-3271(1997).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF HIS-400.
RX PubMed=10952996; DOI=10.1083/jcb.150.4.695;
RA Straesser K., Bassler J., Hurt E.C.;
RT "Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat
RT nucleoporins is essential for nuclear mRNA export.";
RL J. Cell Biol. 150:695-706(2000).
RN [6]
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 [7]
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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 268-488 IN COMPLEX WITH MTR2.
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: Involved in the export of mRNA from the nucleus to the
CC cytoplasm. {ECO:0000255|PROSITE-ProRule:PRU00611,
CC ECO:0000269|PubMed:9214641}.
CC -!- SUBUNIT: Interacts with nucleoporin complex NUP84 and MTR2. Interacts
CC with MIP6. {ECO:0000269|PubMed:12835756, ECO:0000269|PubMed:9214641}.
CC -!- INTERACTION:
CC Q99257; P17629: HPR1; NbExp=4; IntAct=EBI-11642, EBI-8526;
CC Q99257; P34232: MTR2; NbExp=2; IntAct=EBI-11642, EBI-11585;
CC Q99257; Q02630: NUP116; NbExp=5; IntAct=EBI-11642, EBI-11703;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes at both the
CC nuclear and cytoplasmic site of the pores. Shuttles between the nucleus
CC and the cytoplasm.
CC -!- DOMAIN: The leucine-rich repeats and the NTF2-domain are essential for
CC the export of mRNA from the nucleus. {ECO:0000250}.
CC -!- DOMAIN: The NTF2 domain heterodimerizes with MTR2. The formation of
CC this heterodimer is essential for mRNA export and binds to all of the
CC nucleoporin-FG-repeats.
CC -!- DOMAIN: The RNA-binding domain is conserved in most NXF proteins but
CC may be absent in yeasts.
CC -!- MISCELLANEOUS: Present with 2830 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
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DR EMBL; X96770; CAA65552.1; -; Genomic_DNA.
DR EMBL; Z73525; CAA97875.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11265.1; -; Genomic_DNA.
DR PIR; S65180; S65180.
DR RefSeq; NP_015156.1; NM_001183983.1.
DR PDB; 1OF5; X-ray; 2.80 A; A=268-484.
DR PDB; 2JP7; NMR; -; A=543-599.
DR PDB; 2KHH; NMR; -; A=543-599.
DR PDB; 4WWU; X-ray; 3.30 A; A/B/D/E/G/H/J/K=1-487.
DR PDB; 6EXZ; X-ray; 1.30 A; A=528-599.
DR PDBsum; 1OF5; -.
DR PDBsum; 2JP7; -.
DR PDBsum; 2KHH; -.
DR PDBsum; 4WWU; -.
DR PDBsum; 6EXZ; -.
DR AlphaFoldDB; Q99257; -.
DR SMR; Q99257; -.
DR BioGRID; 36014; 376.
DR ComplexPortal; CPX-1142; mRNA nuclear export factor complex, MEX67-MTR2.
DR DIP; DIP-3984N; -.
DR IntAct; Q99257; 24.
DR MINT; Q99257; -.
DR STRING; 4932.YPL169C; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR TCDB; 3.A.22.1.1; the transcription-coupled trex/tap nuclear mrna export complex (trex) family.
DR iPTMnet; Q99257; -.
DR MaxQB; Q99257; -.
DR PaxDb; Q99257; -.
DR PRIDE; Q99257; -.
DR TopDownProteomics; Q99257; -.
DR EnsemblFungi; YPL169C_mRNA; YPL169C; YPL169C.
DR GeneID; 855934; -.
DR KEGG; sce:YPL169C; -.
DR SGD; S000006090; MEX67.
DR VEuPathDB; FungiDB:YPL169C; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_024991_1_1_1; -.
DR InParanoid; Q99257; -.
DR OMA; YGGHEAW; -.
DR BioCyc; YEAST:G3O-34065-MON; -.
DR EvolutionaryTrace; Q99257; -.
DR PRO; PR:Q99257; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q99257; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0042272; C:nuclear RNA export factor complex; IPI:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0015288; F:porin activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0030619; F:U1 snRNA binding; IDA:SGD.
DR GO; GO:0030620; F:U2 snRNA binding; IDA:SGD.
DR GO; GO:0030621; F:U4 snRNA binding; IDA:SGD.
DR GO; GO:0030623; F:U5 snRNA binding; IDA:SGD.
DR GO; GO:0017070; F:U6 snRNA binding; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:SGD.
DR GO; GO:0051168; P:nuclear export; IMP:SGD.
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:0055085; P:transmembrane transport; IDA:SGD.
DR CDD; cd14342; UBA_TAP-C; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR040736; Mex67_RRM.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR005637; TAP_C_dom.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10662; PTHR10662; 1.
DR Pfam; PF18444; RRM_9; 1.
DR Pfam; PF03943; TAP_C; 1.
DR SMART; SM00804; TAP_C; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Leucine-rich repeat; mRNA transport;
KW Nucleus; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..599
FT /note="mRNA export factor MEX67"
FT /id="PRO_0000220542"
FT REPEAT 163..184
FT /note="LRR 1"
FT REPEAT 189..210
FT /note="LRR 2"
FT DOMAIN 224..262
FT /note="LRRCT"
FT DOMAIN 280..467
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 546..599
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 408..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 400
FT /note="H->Y: Impairs association with the nuclear pores and
FT interaction with MTR2."
FT /evidence="ECO:0000269|PubMed:10952996"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:4WWU"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 177..182
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:4WWU"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 279..294
FT /evidence="ECO:0007829|PDB:1OF5"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 303..313
FT /evidence="ECO:0007829|PDB:1OF5"
FT TURN 332..337
FT /evidence="ECO:0007829|PDB:4WWU"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 347..353
FT /evidence="ECO:0007829|PDB:4WWU"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1OF5"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:1OF5"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:1OF5"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 394..405
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 441..454
FT /evidence="ECO:0007829|PDB:1OF5"
FT STRAND 457..469
FT /evidence="ECO:0007829|PDB:1OF5"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:6EXZ"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:6EXZ"
FT HELIX 546..559
FT /evidence="ECO:0007829|PDB:6EXZ"
FT HELIX 563..572
FT /evidence="ECO:0007829|PDB:6EXZ"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:2JP7"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:6EXZ"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6EXZ"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:6EXZ"
SQ SEQUENCE 599 AA; 67352 MW; 6CE55EEC6FA40B40 CRC64;
MSGFHNVGNI NMMAQQQMQQ NRIKISVRNW QNATMNDLIN FISRNARVAV YDAHVEGPLV
IGYVNSKAEA ESLMKWNGVR FAGSNLKFEL LDNNGASAGT SDTISFLRGV LLKRYDPQTK
LLNLGALHSD PELIQKGVFS SISTQSKMFP AMMKLASTEK SLIVESVNLA DNQLKDISAI
STLAQTFPNL KNLCLANNQI FRFRSLEVWK NKFKDLRELL MTNNPITTDK LYRTEMLRLF
PKLVVLDNVI VRDEQKLQTV YSLPMKIQQF FFENDALGQS STDFATNFLN LWDNNREQLL
NLYSPQSQFS VSVDSTIPPS TVTDSDQTPA FGYYMSSSRN ISKVSSEKSI QQRLSIGQES
INSIFKTLPK TKHHLQEQPN EYSMETISYP QINGFVITLH GFFEETGKPE LESNKKTGKN
NYQKNRRYNH GYNSTSNNKL SKKSFDRTWV IVPMNNSVII ASDLLTVRAY STGAWKTASI
AIAQPPQQQA SVLPQVASMN PNITTPPQPQ PSVVPGGMSI PGAPQGAMVM APTLQLPPDV
QSRLNPVQLE LLNKLHLETK LNAEYTFMLA EQSNWNYEVA IKGFQSSMNG IPREAFVQF
