ID   HEK2_YEAS8              Reviewed;         381 AA.
AC   C8Z3W4;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Heterogeneous nuclear rnp K-like protein 2;
DE   AltName: Full=KH domain-containing protein 1;
GN   Name=HEK2; Synonyms=KHD1; ORFNames=EC1118_1B15_0914g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA   Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
CC   -!- FUNCTION: RNA-binding protein involved in the correct localization of
CC       transcripts in the cell. RNA localization is a widespread mechanism for
CC       achieving localized protein synthesis. Required for the asymmetric
CC       localization to the daughter cell nucleus of the ASH1 transcript,
CC       coding for a specific repressor of transcription. Overexpression
CC       inhibits translation of the ASH1 transcript. Involved in the stability
CC       of transcripts, like the MTL1 mRNA. Involved in structural and
CC       functional organization of telomeric chromatin and regulates silencing
CC       at the HMR locus (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds RNA. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, P-body
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by the plasma membrane-Anchored casein kinase YCK1.
CC       Phosphorylation at its C-terminus reduces its RNA-binding capacity (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HEK2 family. {ECO:0000305}.
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DR   EMBL; FN393060; CAY77753.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8Z3W4; -.
DR   SMR; C8Z3W4; -.
DR   EnsemblFungi; CAY77753; CAY77753; EC1118_1B15_0914g.
DR   HOGENOM; CLU_022670_2_0_1; -.
DR   Proteomes; UP000000286; Chromosome II, Scaffold EC1118_1B15.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1370.10; -; 3.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   SUPFAM; SSF54791; SSF54791; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   3: Inferred from homology;
KW   Chromatin regulator; Chromosome; Cytoplasm; mRNA transport; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding; Telomere; Translation regulation;
KW   Transport.
FT   CHAIN           1..381
FT                   /note="Heterogeneous nuclear rnp K-like protein 2"
FT                   /id="PRO_0000408195"
FT   DOMAIN          43..107
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          156..221
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          258..326
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38199"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38199"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P38199"
SQ   SEQUENCE   381 AA;  41698 MW;  CAEAEEFBE6D77A5C CRC64;
     MSQFFEAATP VAIPTNNTNG GSSDAGSAAT GGAPVVGTTA QPTINHRLLL SLKEAAKIIG
     TKGSTISRIR AANSVKIGIS EKVPGCSDRI LSCAGNVINV ANAIGDIVDV LNKRNPENED
     AAEGEAEEHY YFHFLNHILP APSKDEIRDL QQLEDIGYVR LIVANSHISS IIGKAGATIK
     SLINKHGVKI VASKDFLPAS DERIIEIQGF PGSITNVLIE ISEIILSDVD VRFSTERSYF
     PHLKKSSGEP TSPSTSSNTR IELKIPELYV GAIIGRGMNR IKNLKTFTKT NIVVERKDDD
     DKDENFRKFI ITSKFPKNVK LAESMLLKNL NTEIEKRENY KRKLEAAEGD ATVVTERSDS
     ASFLEEKEEP QKNHDNKEEQ S