ID   NMD2_SCHPO              Reviewed;        1049 AA.
AC   O13824;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 136.
DE   RecName: Full=Nonsense-mediated mRNA decay protein 2;
DE   AltName: Full=Up-frameshift suppressor 2;
GN   Name=upf2; ORFNames=SPAC19A8.08;
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 SUBCELLULAR LOCATION.
RX   PubMed=11073994; DOI=10.1128/mcb.20.23.8944-8957.2000;
RA   Mendell J.T., Medghalchi S.M., Lake R.G., Noensie E.N., Dietz H.C.;
RT   "Novel Upf2p orthologues suggest a functional link between translation
RT   initiation and nonsense surveillance complexes.";
RL   Mol. Cell. Biol. 20:8944-8957(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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-60, AND IDENTIFICATION BY
RP   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 nonsense-mediated decay of mRNAs containing
CC       premature stop codons. It interacts, via its C-terminus, with
CC       NAM7/UPF1. Could be involved in determining the efficiency of
CC       translational termination or reinitiation or factors involved in the
CC       initial assembly of an initiation- and termination-competent mRNP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11073994}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF301014; AAG33226.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329670; CAB11644.1; -; Genomic_DNA.
DR   PIR; T37953; T37953.
DR   RefSeq; NP_593784.1; NM_001019213.2.
DR   AlphaFoldDB; O13824; -.
DR   SMR; O13824; -.
DR   BioGRID; 278623; 2.
DR   STRING; 4896.SPAC19A8.08.1; -.
DR   iPTMnet; O13824; -.
DR   MaxQB; O13824; -.
DR   PaxDb; O13824; -.
DR   PRIDE; O13824; -.
DR   EnsemblFungi; SPAC19A8.08.1; SPAC19A8.08.1:pep; SPAC19A8.08.
DR   GeneID; 2542147; -.
DR   KEGG; spo:SPAC19A8.08; -.
DR   PomBase; SPAC19A8.08; upf2.
DR   VEuPathDB; FungiDB:SPAC19A8.08; -.
DR   eggNOG; KOG2051; Eukaryota.
DR   HOGENOM; CLU_002633_1_1_1; -.
DR   InParanoid; O13824; -.
DR   OMA; DFQHHQI; -.
DR   PhylomeDB; O13824; -.
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   PRO; PR:O13824; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0035145; C:exon-exon junction complex; IBA:GO_Central.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; ISO:PomBase.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IMP:PomBase.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   InterPro; IPR039762; Nmd2/UPF2.
DR   InterPro; IPR007193; Upf2/Nmd2_C.
DR   PANTHER; PTHR12839; PTHR12839; 1.
DR   Pfam; PF02854; MIF4G; 3.
DR   Pfam; PF04050; Upf2; 1.
DR   SMART; SM00543; MIF4G; 3.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1049
FT                   /note="Nonsense-mediated mRNA decay protein 2"
FT                   /id="PRO_0000096872"
FT   DOMAIN          41..282
FT                   /note="MIF4G 1"
FT   DOMAIN          446..634
FT                   /note="MIF4G 2"
FT   DOMAIN          649..855
FT                   /note="MIF4G 3"
FT   REGION          412..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..934
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         60
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1049 AA;  122096 MW;  E7E2077A17B70D98 CRC64;
     MSREEQIKKL NQYLDNRELA FRAKDGDKNI FHTESQLDSS LKKNTAFMKR CKSSLTSENY
     DSFIKEIKTL SLKKFIPEIT AAIVEGMMKC KATKDILSSV KIVWALNLRF STAFTGPMLA
     NLYCALYPNP GYSLCHESYF ELKQNENEVS EKDRSSHLLK VRPLLRFLIE FWLNGVVGTP
     EDFVSYLPST DSNDKKFRKP WFEEQNLKKP LVVLLFNDLM DTRFGFLLLP VLTSLVRTFS
     CELFTTEDFE DKETLELVNR LNPVVWRTYL RKSLNSYVDK LEVYCQKRKS LFEELNKQYQ
     EQSIIRADPN NEKFQRLANF SKSIESEFSS YASLSEVLNR KASEDLLELN FMEKASSGTN
     SVFNASGERS ESANVETAQV WDDREQYFFY EVFPNFNEGS IAEMKSSIYE SSQEGIRSSS
     ENNKKEDDLK DSTGDLNTTQ VSSRVDNFLL KLPSMVSLEL TNEMALEFYD LNTKASRNRL
     IKALCTIPRT SSFLVPYYVR LARILSQLSS EFSTSLVDHA RHSFKRMIHR KAKHEYDTRL
     LIVRYISELT KFQLMPFHMV FECYKLCINE FTPFDLEVLA LLLESCGRFL LRYPETKLQM
     QSFLEAIQKK KLASALASQD QLVLENALHF VNPPKRGIIV SKKKSLKEEF LYDLIQIRLK
     DDNVFPTLLL LRKFDWKDDY QILYNTIMEV WNIKYNSLNA LARLLSALYK FHPEFCIHVI
     DDTLESLFSA VNNSDHVEKQ KRLAQARFIS ELCVIHMLDV RAITNFLFHL LPLEKFESFL
     TMKASTLTNI NNDMFRLRLI VVVLQTCGPS IIRSKTKKTM LTYLLAYQCY FLIQPEMPLD
     MLYEFEDVIG YVRPSMKVYM HYEEARNALT ERLQAISDDW EEDDTRPVFQ GANDGDISSN
     EESVYLPEDI SDESETDEES SGLEESDLLD SEDEDIDNEM QLSRELDEEF ERLTNESLLT
     RMHEKNPGFD VPLPLRASSL GSPYVTRNEE SASESSHVMF TLLTKRGNKQ RSQYLEIPSH
     SSLVRSTKNQ QTEEIMERKR VKEMVLNFE