MEX67_SCHPO
ID MEX67_SCHPO Reviewed; 596 AA.
AC Q9Y8G3; Q9UU47;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=mRNA export factor mex67;
GN Name=mex67; ORFNames=SPBC1921.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11073978; DOI=10.1128/mcb.20.23.8767-8782.2000;
RA Yoon J.H., Love D.C., Guhathakurta A., Hanover J.A., Dhar R.;
RT "Mex67p of Schizosaccharomyces pombe interacts with Rae1p in mediating mRNA
RT export.";
RL Mol. Cell. Biol. 20:8767-8782(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-125.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 460-VAL--GLY-462;
RP 478-ARG--THR-479; 492-ILE--ILE-493 AND 494-ASN--ASP-495.
RX PubMed=14963046; DOI=10.1074/jbc.m309731200;
RA Thakurta A.G., Gopal G., Yoon J.H., Saha T., Dhar R.;
RT "Conserved nuclear export sequences in Schizosaccharomyces pombe Mex67 and
RT human TAP function in mRNA export by direct nuclear pore interactions.";
RL J. Biol. Chem. 279:17434-17442(2004).
RN [5]
RP INTERACTION WITH MLO3.
RX PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT mRNA export in fission yeast.";
RL EMBO J. 24:2512-2523(2005).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-130 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in the export of mRNA from the nucleus to the
CC cytoplasm. {ECO:0000255|PROSITE-ProRule:PRU00611,
CC ECO:0000269|PubMed:11073978, ECO:0000269|PubMed:14963046}.
CC -!- SUBUNIT: Interacts with mlo3 and rae1. {ECO:0000269|PubMed:15990877}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14963046}. Cytoplasm
CC {ECO:0000269|PubMed:14963046, ECO:0000269|PubMed:16823372}.
CC Note=Localizes at both the nuclear and cytoplasmic site of the pores
CC (PubMed:14963046). Shuttles between the nucleus and the cytoplasm
CC (PubMed:14963046). {ECO:0000269|PubMed:14963046}.
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 -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA87120.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF055036; AAD43831.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB58969.1; -; Genomic_DNA.
DR EMBL; AB027816; BAA87120.1; ALT_INIT; Genomic_DNA.
DR PIR; T43683; T43683.
DR RefSeq; NP_595996.1; NM_001021904.2.
DR AlphaFoldDB; Q9Y8G3; -.
DR SMR; Q9Y8G3; -.
DR BioGRID; 277250; 75.
DR IntAct; Q9Y8G3; 1.
DR STRING; 4896.SPBC1921.03c.1; -.
DR iPTMnet; Q9Y8G3; -.
DR MaxQB; Q9Y8G3; -.
DR PaxDb; Q9Y8G3; -.
DR PRIDE; Q9Y8G3; -.
DR EnsemblFungi; SPBC1921.03c.1; SPBC1921.03c.1:pep; SPBC1921.03c.
DR GeneID; 2540727; -.
DR KEGG; spo:SPBC1921.03c; -.
DR PomBase; SPBC1921.03c; mex67.
DR VEuPathDB; FungiDB:SPBC1921.03c; -.
DR eggNOG; KOG3763; Eukaryota.
DR HOGENOM; CLU_024991_1_1_1; -.
DR InParanoid; Q9Y8G3; -.
DR OMA; FHADEEF; -.
DR PhylomeDB; Q9Y8G3; -.
DR Reactome; R-SPO-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR PRO; PR:Q9Y8G3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005643; C:nuclear pore; ISO:PomBase.
DR GO; GO:0042272; C:nuclear RNA export factor complex; IPI:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IGI:PomBase.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; ISO:PomBase.
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; 2.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Leucine-rich repeat; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..596
FT /note="mRNA export factor mex67"
FT /id="PRO_0000220541"
FT REPEAT 215..236
FT /note="LRR 1"
FT REPEAT 241..262
FT /note="LRR 2"
FT REPEAT 263..282
FT /note="LRR 3"
FT DOMAIN 283..338
FT /note="LRRCT"
FT DOMAIN 338..499
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 543..596
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 460..462
FT /note="VHG->AAA: No mRNA export from nucleus."
FT /evidence="ECO:0000269|PubMed:14963046"
FT MUTAGEN 478..479
FT /note="RT->AA: Reduced mRNA export from nucleus."
FT /evidence="ECO:0000269|PubMed:14963046"
FT MUTAGEN 492..493
FT /note="II->AA: Reduced mRNA export from nucleus."
FT /evidence="ECO:0000269|PubMed:14963046"
FT MUTAGEN 494..495
FT /note="ND->AA: Reduced mRNA export from nucleus."
FT /evidence="ECO:0000269|PubMed:14963046"
SQ SEQUENCE 596 AA; 66535 MW; B84345BBC0DC3D83 CRC64;
MLRRKRERRN AVKENEMVID TPLEKRRTPG KPRATREPPI SVVITGHSKG SEDDLISFVW
RKVKVRLMNI SYSPASVTAV VKSQDFSRLN GLNGAAFAGD HLAIRRVDGA SNVTQDYRKA
KTKRSFRSVS APSLSALATQ AQRNVSKTLP QSTNETIEKL RQFLQTRYQP ATKFLDLGNL
QQDPLLKQMG ILAEASTKSK MFPALMKVAS LNFPDVISVS LSDNNLQSVT AVTTLAQTWP
KLLNLSLANN RITSLSDLDP WSPKTKLPEL QELVLVGNPI VTTFANRAMD YQREMVSRFP
KLRLLDGNSI NSEIIASQST VPFPVYQSFF DKVETEQIVN SFLAAFFKGW DENRSALVNQ
LYSPNATFSI SLNASNVRTN FSQKTDTKKW GAYKMKSRNL LYSQSQKESK SRLFNGHEEI
SNAVKSLPAT AHDLSDRSQW VFDGWNLVLP SVGAAIKIVV HGQFEEPQNK RLLRSFDRTL
LILPGGSTGI LIINDLLVIR SFAGSLGWLP GQSSVRTSNN AMSASASKPS DIVQPRPEQA
MLDTRQQIVL KIKAETGLND YYAHMCCEQN NWDYNSALAS FLELKSRNVI PAEAFS
