MKT1_SCHPO
ID MKT1_SCHPO Reviewed; 802 AA.
AC Q9UTN2; P78828; Q9P6S7;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Post-transcriptional regulator mkt1 {ECO:0000312|PomBase:SPAC139.01c};
DE AltName: Full=Inactive endonuclease mkt1 {ECO:0000305};
DE AltName: Full=Post-transcriptional RNA stability regulator mkt1 {ECO:0000312|PomBase:SPAC139.01c};
GN Name=mkt1 {ECO:0000312|PomBase:SPAC139.01c};
GN ORFNames=SPAC139.01c {ECO:0000312|PomBase:SPAC139.01c},
GN SPAC955.02c {ECO:0000312|PomBase:SPAC139.01c};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-802.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; SER-228 AND SER-230, 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).
RN [4]
RP FUNCTION, INTERACTION WITH ATH1, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 8-LEU--ASP-12; ASP-32 AND ASP-201.
RX PubMed=31822915; DOI=10.1093/nar/gkz1157;
RA Taglini F., Chapman E., van Nues R., Theron E., Bayne E.H.;
RT "Mkt1 is required for RNAi-mediated silencing and establishment of
RT heterochromatin in fission yeast.";
RL Nucleic Acids Res. 48:1239-1253(2020).
CC -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC expression by 3'-UTR-mediated RNA regulation (PubMed:31822915).
CC Promotes interactions between mRNA and poly(A)-binding protein
CC (PubMed:31822915). Binds the 3' UTR of mRNAs, centromeric transcripts
CC and antisense-rDNA (PubMed:31822915). Required for the establishment
CC but not the maintenance of heterochromatin at pericentromeres, and for
CC the maintenance of small domains of facultative heterochromatin known
CC as HOODs (PubMed:31822915). {ECO:0000269|PubMed:31822915}.
CC -!- SUBUNIT: Interacts with pab1 binding protein ath1.
CC {ECO:0000305|PubMed:31822915}.
CC -!- DISRUPTION PHENOTYPE: Abnormal establishment of heterochromatin
CC (PubMed:31822915). Increased level of RNA-DNA hybrids
CC (PubMed:31822915). {ECO:0000269|PubMed:31822915}.
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the XPG/RAD2 endonuclease family, only
CC two of the seven Asp residues involved in Mg(2+) binding are conserved
CC suggesting that it has no nuclease activity.
CC {ECO:0000305|PubMed:31822915}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13838.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU329670; CAB88876.3; -; Genomic_DNA.
DR EMBL; D89176; BAA13838.1; ALT_FRAME; mRNA.
DR PIR; T37602; T37602.
DR PIR; T42541; T42541.
DR RefSeq; XP_001713046.1; XM_001712994.2.
DR AlphaFoldDB; Q9UTN2; -.
DR BioGRID; 278256; 52.
DR IntAct; Q9UTN2; 1.
DR STRING; 4896.SPAC139.01c.1; -.
DR iPTMnet; Q9UTN2; -.
DR MaxQB; Q9UTN2; -.
DR PaxDb; Q9UTN2; -.
DR PRIDE; Q9UTN2; -.
DR EnsemblFungi; SPAC139.01c.1; SPAC139.01c.1:pep; SPAC139.01c.
DR PomBase; SPAC139.01c; -.
DR VEuPathDB; FungiDB:SPAC139.01c; -.
DR eggNOG; ENOG502QVHA; Eukaryota.
DR HOGENOM; CLU_378548_0_0_1; -.
DR InParanoid; Q9UTN2; -.
DR OMA; FYQTKVI; -.
DR PhylomeDB; Q9UTN2; -.
DR PRO; PR:Q9UTN2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:PomBase.
DR GO; GO:0043488; P:regulation of mRNA stability; ISS:PomBase.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR022039; MKT1_C.
DR InterPro; IPR022040; MKT1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; PTHR11081; 1.
DR Pfam; PF12246; MKT1_C; 1.
DR Pfam; PF12247; MKT1_N; 1.
DR Pfam; PF00752; XPG_N; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Translation regulation.
FT CHAIN 1..802
FT /note="Post-transcriptional regulator mkt1"
FT /id="PRO_0000154048"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 8..12
FT /note="LFIID->AAAAA: Normal chromatin silencing by small
FT RNA."
FT /evidence="ECO:0000269|PubMed:31822915"
FT MUTAGEN 32
FT /note="D->A: Normal chromatin silencing by small RNA."
FT /evidence="ECO:0000269|PubMed:31822915"
FT MUTAGEN 201
FT /note="D->A: Normal chromatin silencing by small RNA."
FT /evidence="ECO:0000269|PubMed:31822915"
FT CONFLICT 608
FT /note="L -> F (in Ref. 2; BAA13838)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="D -> N (in Ref. 2; BAA13838)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="I -> M (in Ref. 2; BAA13838)"
FT /evidence="ECO:0000305"
FT CONFLICT 649
FT /note="S -> C (in Ref. 2; BAA13838)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="N -> K (in Ref. 2; BAA13838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 802 AA; 90153 MW; 83654B3E6BE085D2 CRC64;
MTIRSLNLFI IDKKHQHKSS LSSFQNCKLG IDASFYLTQI IHSFTPQELQ SLAVNGESEY
LQHRISEFLE QLRTENITPI FVFNGIPLTF EASSQLEVPG KQKSHSALTD FEAFDPYDAN
IQRNMYRMDA SGPANYGESK PTLLYTNQRD HLDRLCDQVK FYLDQCNVEY FVAPYLAMAQ
LAYFLNGTSS PYIDAIYGST DLLLFGVKKF ITSMNTSSNV KISSDPSSPS TQTTINSAAK
SSFTWLDGNA LLQDTNGLSW QQFIDSCLLC GTAISPTFPQ IEGTFLIKSA MELVRMFGSA
YRAVLHFAEI FPQPIFQDYL QQYKRAVCFS KFGIVMDTKG LTLPPVPTES VPNDINIYFG
TRLPNEIYFY ISRGLIPCKM IGALVSGCFS DPVSILEQHI GDKASQGTFS GANSGLNPGR
DNAAAVAAVD QRRFVDDLEE IWSQGLNLLT QPLNRFYQAR DIVSLHGHNQ QASLKVMHSY
DPPLYNDTRA WMIYEENLPS YLSSNFLKEE PVVLFDLLRA LNDPVFVKKS FCTEGNIGIK
NPPKHPLSST AEIVLSSCYR FLQIRSFVLT SHQLTSWGCP LLKALENCHL QNQTSVVVLF
ELLRLRQLKE PSLLSSSSAS IADLSITSAT EFLAKVATFL PIKQRPEVSK ISIVDENLLQ
FYQLQTSFGS NLKELMAMIL ASVILNRNVD KSKIDPKLIR KTLPFQNING SLVSGFVVKR
FFEIISKEQE ASSQQENIQK AYEIIEKEFP TIGSAENHIA QFLEFWKTFM EGVKEAENTS
AIGKLVLSKL FLTNQWIFSL GL
