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PYM1_XENLA
ID   PYM1_XENLA              Reviewed;         199 AA.
AC   Q640E9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Partner of Y14 and mago {ECO:0000250|UniProtKB:P82804};
DE   AltName: Full=PYM homolog 1 exon junction complex-associated factor {ECO:0000250|UniProtKB:Q9BRP8};
DE   AltName: Full=Protein wibg homolog;
GN   Name=pym1 {ECO:0000250|UniProtKB:Q9BRP8}; Synonyms=pym, wibg;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Key regulator of the exon junction complex (EJC), a
CC       multiprotein complex that associates immediately upstream of the exon-
CC       exon junction on mRNAs and serves as a positional landmark for the
CC       intron exon structure of genes and directs post-transcriptional
CC       processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA
CC       decay (NMD) or translation. Acts as an EJC disassembly factor, allowing
CC       translation-dependent EJC removal and recycling by disrupting mature
CC       EJC from spliced mRNAs. Its association with the 40S ribosomal subunit
CC       probably prevents a translation-independent disassembly of the EJC from
CC       spliced mRNAs, by restricting its activity to mRNAs that have been
CC       translated. Interferes with NMD and enhances translation of spliced
CC       mRNAs, probably by antagonizing EJC functions (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with magoh and rbm8a; the
CC       interaction is direct. Associates (eIF2A-like region) with the 40S
CC       ribosomal subunit and the 48S preinitiation complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRP8}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9BRP8}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9BRP8}. Note=Shuttles between the nucleus and
CC       the cytoplasm. Nuclear export is mediated by XPO1/CRM1.
CC       {ECO:0000250|UniProtKB:Q9BRP8}.
CC   -!- SIMILARITY: Belongs to the pym family. {ECO:0000305}.
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DR   EMBL; BC082679; AAH82679.1; -; mRNA.
DR   RefSeq; NP_001087999.1; NM_001094530.1.
DR   AlphaFoldDB; Q640E9; -.
DR   SMR; Q640E9; -.
DR   BioGRID; 104768; 1.
DR   IntAct; Q640E9; 1.
DR   MaxQB; Q640E9; -.
DR   DNASU; 494688; -.
DR   GeneID; 494688; -.
DR   KEGG; xla:494688; -.
DR   CTD; 494688; -.
DR   Xenbase; XB-GENE-943127; pym1.L.
DR   OMA; MAKLESW; -.
DR   OrthoDB; 1545729at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 494688; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0035145; C:exon-exon junction complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:1903259; P:exon-exon junction complex disassembly; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
DR   InterPro; IPR039333; PYM1.
DR   InterPro; IPR015362; WIBG_mago-bd.
DR   InterPro; IPR036348; WIBG_N_sf.
DR   PANTHER; PTHR22959; PTHR22959; 1.
DR   Pfam; PF09282; Mago-bind; 1.
DR   SMART; SM01273; Mago-bind; 1.
DR   SUPFAM; SSF101931; SSF101931; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nonsense-mediated mRNA decay; Nucleus;
KW   Reference proteome; Translation regulation.
FT   CHAIN           1..199
FT                   /note="Partner of Y14 and mago"
FT                   /id="PRO_0000287288"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          83..199
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        95..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22553 MW;  0EC479CF1D8E3746 CRC64;
     MAAPYVSDDS GKYIASTQRP DGSWRKQRKV KEGYVPQEEV PVYENKYVKF FKSKPSLPPG
     LCEADGTTGQ AQPSKPDADA SLSKTAKRNL KRKEKRKQEK GEREQVEETR QDLERVNISD
     TPVQKNVTSA HKNGSASSDN SAAEKAKKIK NLRKKLRQVE ELQQKIDCGE IIQPSKEQLE
     KLARRKALED EIEDLELDL
 
 
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